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Regulation of short-chain fatty acids in the immune system

Xiao-feng Liu, Jia-hao Shao, Yi-Tao Liao and 7 more

Frontiers in Immunology · 2023 · Review · CC BY

doi:10.3389/fimmu.2023.1186892

Abstract

A growing body of research suggests that short-chain fatty acids (SCFAs), metabolites produced by intestinal symbiotic bacteria that ferment dietary fibers (DFs), play a crucial role in the health status of symbiotes. SCFAs act on a variety of cell types to regulate important biological processes, including host metabolism, intestinal function, and immune function. SCFAs also affect the function and fate of immune cells. This finding provides a new concept in immune metabolism and a better understanding of the regulatory role of SCFAs in the immune system, which impacts the prevention and treatment of disease. The mechanism by which SCFAs induce or regulate the immune response is becoming increasingly clear. This review summarizes the different mechanisms through which SCFAs act in cells. According to the latest research, the regulatory role of SCFAs in the innate immune system, including in NLRP3 inflammasomes, receptors of TLR family members, neutrophils, macrophages, natural killer cells, eosinophils, basophils and innate lymphocyte subsets, is emphasized. The regulatory role of SCFAs in the adaptive immune system, including in T-cell subsets, B cells, and plasma cells, is also highlighted. In addition, we discuss the role that SCFAs play in regulating allergic airway inflammation, colitis, and osteoporosis by influencing the immune system. These findings provide evidence for determining treatment options based on metabolic regulation.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 17, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

Parts of the colon and small intestine contain many microorganisms, mainly bacteria and some fungi. These microorganisms produce short-chain fatty acids (SCFAs) from dietary components in the gut and from biomolecules produced by the host. Intestinal SCFAs mainly include acetate (C2), propionate (C3), butyrate (C4) and valerate (C5). Most SCFAs function in the gut, but a small amount of SCFAs reach the peripheral circulation via the portal vein. A growing body of evidence suggests that SCFAs regulate immunity and suppress or promote inflammatory responses in the gut and other organs. They play an important role in the regulation of innate and adaptive immunity mediated by a variety of mechanisms, including histone deacetylase (HDAC) inhibition, G-protein-coupled receptor (GPR) signaling, acetyl-CoA production, and metabolic integration. Through a combination of these mechanisms, SCFAs induce or modulate immune responses. However, the mechanism through which SCFAs regulate the immune system is relatively complex, and the mechanism of SCFAs differs among different immune cells; thus, a comprehensive summary is currently lacking. In this review, we more comprehensively introduce the regulatory role of SCFAs in the immune system. In the innate immune system, SCFAs play a role by regulating protein molecules, including the NLRP3 inflammasome and Toll-like receptors (TLRs). SCFAs also play a role by regulating innate immune cells, including neutrophils, macrophages, natural killer cells, eosinophils, basophils, and innate lymphocyte subsets (ILCs). We also highlight the regulatory role of SCFAs in the adaptive immune system, including in T-cell subsets, B cells, and plasma cells.

Synthesis and metabolism of SCFAs

SCFAs are the most abundant microbial metabolites in the colonic lumen and are mainly produced by the microbial fermentation of prebiotics, such as dietary fiber. Among them, the ratio of C2, C3 and C4 is approximately 3:1:1. The differentiation of colon epithelial stem cells and the metabolism of facultative anaerobes in the colon ensure the anaerobic environment of the colon. Obligate anaerobes in the colon (e.g., Clostridium and Bacteroides) encode broad-spectrum enzymes that hydrolyze carbohydrates and decompose dietary fibers into sugars ( Table 1 ). The released sugars are then fermented through glycolysis and the pentose phosphate pathway to hydrolyze dietary fibers into SCFAs. C2 is produced by pyruvates via acetyl-CoA or the Wood-Ljungdahl pathway. C3 is synthesized from acrylates using lactic acid as a precursor and is produced by the acrylate and propylene glycol pathways or by the succinate pathway that converts succinate to methylmalonyl-CoA. C4 is reduced by condensation of two molecules of acetyl-CoA to butyryl-CoA, which can be synthesized through the butyrate kinase and phosphotransbutyrylase pathways. Butyryl-CoA can also be converted to C4 via the acetate CoA transferase pathway. In addition, C4 can be synthesized from proteins via the lysine pathway. Other nutrients, including proteins and peptides, can be metabolized to produce low levels of SCFAs. Among them, the acidic amino acid glutamic acid mainly produces C2 and C4, and aspartic acid fermentation mainly produces C2 and C3. The deamination of the alkaline amino acids lysine, arginine and histidine produces C2 and C4. The neutral amino acid cysteine can produce C2, C3 and C4, and the main products of methionine metabolism are C3 and C4. In this respect, proteins are more likely to be decomposed into small amino acids in pH neutral and weakly alkaline environments and are thus more likely to produce SCFAs in these environments. In short, when the pH value in the lumen is 5.5, the bacteria that produce C4 dominate; at a pH of 6.5 in the lumen, C2- and C3-producing bacteria dominate.

The concentration of SCFAs in the proximal colon was 9-131 mmol/L, while the concentration of SCFAs in the distal colon was lower (11-80 mmol/L). SCFAs enter cells in the following ways: the dissociated anions bind to MCT1 (SLC16A1), MCT4 (SLC16A3), SMCT1 (SLC5A8), and SMCT2 (SLC5A12)-mediated transporters and GPR receptors in a hydrogen-dependent or sodium-dependent manner. Most SCFAs are consumed by the epithelial cells of the colon. The remaining SCFAs enter the superior mesenteric vein, inferior mesenteric vein and portal vein through passive diffusion and active transport by transporters (C2, C3 and C4 concentrations are 262.8 μM/L, 30.3 μM/L, and 30.1 μM/L, respectively). Some SCFAs are metabolized by the liver, and the remaining SCFAs are dispersed to peripheral circulation (the concentrations of C2, C3, and C4 were 172.9 μM/L, 3.6 μM/L, and 7.5 μM/L, respectively). These blood concentrations of SCFAs are thought to be high enough to affect host cells, depending on the type and amount of dietary fiber ingested by the host and the health status of the host (e.g., helminthic infection, viral infection, autoinflammation).

The receptors of SCFAs that have been widely reported are GPR41, GPR43, GPR109A, OR51E2 (human) and OLFR78 (mouse). SCFAs with different carbon chain lengths have different abilities to activate GPR41, GPR43 and GPR109A receptors. Two to three carbon chains are more likely to activate GPR43 receptors, while 3-5 carbon chains are more likely to activate GPR41 receptors. C4 activates the GPR109A receptor more easily. SCFAs are found in high levels in the gut, and most of these receptors are activated in intestinal tissues.

SCFAs are natural inhibitors of HDAC, of which there are 18 types. There are four classes of HDAC as follows: Class I (HDAC1-3 and HDAC8), Class II (HDAC4-7 and HDAC9-10), Class III (SIRT1-7) and Class IV (HDAC11). Different types of SCFAs have different inhibition rates of different types of HDAC. For example, C4 can inhibit HDAC up to 80%, C3 can inhibit HDAC up to 60%, and C2 has the lowest inhibition rate. SCFAs can affect histone acetylation by regulating the homeostasis between histone acetyltransferase (HAT) and HDAC. HAT transfers acetyl groups to lysine residues in the tail, forming acetylated lysine, which neutralizes the positive charge carried by the histones. HDAC deacetylates the acetylated lysine in the histone tail, making the nucleosome compact and making it more difficult to perform gene transcription and expression. Therefore, different types of SCFAs affect gene transcription in immune cells by inhibiting the activity of different types of HDACs

NF-κB signaling pathway

Nuclear factor-κB (NF-κB) mediates the transcription of various cytokines and chemokines, such as the cytokines TNF-α, TNF-β, IL-1β, IL-2, IL-3, IL-5, IL-12, and IL-18 and the chemokines IL-8, MIP-1α, MIP-2, and MCP-1. Two subunits of NF-κB, P65 and P50, are acetylated and transferred from the cytoplasm into the nucleus to promote the secretion of proinflammatory cytokines. SCFAs produce anti-inflammatory effects by inhibiting NF-κB. The order of inhibition of NF-κB activity was C4>C3>C2.

HDAC can regulate the secretion of inflammatory cytokines by inhibiting the acetylation of NF-KB. It was found that the subunits p65 and p50 of NF-κB interact with HDAC to inhibit transcription. Deacetylation of p65 by HDAC3 enhances the binding of p65 to IκBα, resulting in the export of the NF-κB complex from the nucleus back into the cytoplasm to inhibit the transcription of proinflammatory factors. C3 and C4 are known HDAC inhibitors and have been shown to regulate NF-κB activity. For example, C4 upregulates the production of IL-10 and inhibits the production of the proinflammatory molecules IL-12, TNF-α, IL-1β, and NO by inhibiting NF-κB activity.

GPR receptors influence the secretion of inflammatory cytokines by regulating the β-arrestin 2 pathway upstream of the NF-κB signaling pathway. The GPR43 receptor reduces the level of NF-κB through the β-arrestin 2 signaling pathway and reduces the amount of the two subunits of NF-κB, p65 and p50, entering the nucleus; thus, the GPR43 receptor inhibits the transcription of proinflammatory cytokines (IL-1β and IL-6) ( Figure 1 ).

MAPK signaling pathway

Phosphorylated mitogen-activated protein kinase (MAPK) regulates the ERK, JNK and P38 MAPK signaling pathways, gene transcription, and proinflammatory cytokine secretion. The acetylated state of MAPK phosphatase-1 (MKP-1) interacts with the MAPK substrate to dephosphorylate MAPK and inhibit the activation of the ERK, JNK and P38 MAPK signaling pathways.

SCFAs may regulate MAPK pathways by inhibiting HDAC. HDAC1-3 deacetylates MP-1, and the deacetylation of MP-1 leads to an increase in MAPK signaling and proinflammatory cytokine secretion. However, the effect of HDAC may also be independent of MAPK signaling pathways. Treatment of bone marrow-derived macrophages exposed to lipopolysaccharide (LPS) with TSA (an HDAC inhibitor) inhibited TNF-α and IL-6 production in cells in a time- and dose-dependent manner. However, TSA did not inhibit ERK1/2 and p38 phosphorylation in macrophages.

SCFAs can participate in proinflammatory effects by activating GPR41 and GPR43 receptors. It has been shown that activation of the GPR41 and GPR43 receptors can induce ERK1/2 phosphorylation, while activation of GPR43 receptors can induce p38 MAPK phosphorylation. C2 activates the GPR41 and GPR43 receptors and their downstream ERK2/1 and MAPK signaling pathways and increases the production of proinflammatory factors and chemokines ( Figure 1 ).

mTOR signaling pathway

Rapamycin target (mTOR) is a serine/threonine protein kinase. There are two distinct functional complexes, mTORC1 and mTORC2, that regulate cell growth, proliferation, transcription, mRNA renewal, translation and other important processes. Activation of mTOR helps regulate barrier function in the gut and can influence the production of immune cells and cytokines. mTOR increases the acetyl-coA content via the glycolysis pathway, and excess acetyl-coA is converted to citrate via the tricarboxylic acid cycle (TCA cycle). Citrate, which is involved in the TCA cycle, is converted to acetyl-CoA in the nucleus via ATP-citrate lyase. Acetyl-CoA in the nucleus promotes the binding of acetyl groups to histones and increases the acetylation of histones, ultimately regulating gene expression and the production of cytokines such as IL-10 and TNF. SCFAs enter cells to inhibit HDAC and increase the acetylation of p70 S6 kinase and the phosphorylation of rS6, thereby regulating the mTOR pathway and increasing IL-10 cytokine production ( Figure 1 ).

The activated GPR41 receptor was shown to bind to intracellular Gαi, reducing the level of cAMP. The activated GPR43 receptor conjugates with intracellular Gαq and Gαi to inhibit cAMP levels. Increased intracellular cAMP levels facilitate the entry of intracellular calcium ions into the cytoplasm, a process that regulates gene transcription and translation in immune cells ( Figure 1 ).

Regulation of the NLRP3 inflammasome by SCFAs

The inflammasome is a multiprotein complex assembled by intracytoplasmic pattern recognition receptors (PRRs) and is an important part of the innate immune system. The NLRP3 inflammasome is responsible for the maturation and secretion of the related cytokines IL-1β and IL-18. Studies have shown that SCFAs, after binding with GPR43 and GPR109A in intestinal epithelial cells (IECs), cause intracellular potassium ion outflow and hyperpolarization, calcium ion inflow and activation of the NLRP3 inflammasome. In addition, after activating the GPR43 receptor of IEC cells, SCFAs activate the NLRP3 inflammasome by increasing the phosphorylation of ERK. However, SCFAs have been shown to inhibit NLRP3 inflammasome activation in other cells. For example, intervention by SCFAs significantly reduced NLRP3 inflammasome activation in astrocytes. C4 exerts anti-inflammatory effects by inhibiting the formation and activation of the NLRP3 inflammasome in vascular endothelial cells, but C2 and C3 do not show the same effect; thus, C4 plays an anti-inflammatory role and contributes to the formation of new carotid intima. The results discussed above indicate that not only do the same type of SCFAs have different inhibitory or promoting effects on different types of cells, but different types of SCFAs also have different effects on the same types of cells. This reminds us of previous findings that showed that SCFAs have proinflammatory effects on some cell types, such as macrophages and microglia, and anti-inflammatory effects on others. Therefore, how SCFAs exert their proinflammatory and anti-inflammatory effects requires further study.

Regulation of TLR family members by SCFAs

The expression of PRRs enables the immune system to distinguish intestinal commensal microorganisms from harmful microorganisms. TLRs, a subtype of PRRs, play an important role in the innate immune response. TLRs can promote the proliferation of intestinal epithelial cells and the expression of antimicrobial peptides (AMPs). Studies have shown that C3 and C4 regulate the response of multiple TLRs and TNF-α by inhibiting the histone acetylation of HDAC. Among them, TLR5 is highly expressed in the colon and can recognize the flagellin of gram-negative bacteria by activating a series of pathways within the cell. In patients with ulcerative colitis, the concentration of SCFAs in the colon is generally consistent with the expression of TLR5 in the colon. The content of SCFAs decreases gradually from the proximal end of the colon to the distal end, and the expression of TLR5 also decreases gradually from the proximal end of the colon to the distal end, indicating that there may be a certain relationship between the two. Further studies showed that the regulation of TLR5 by C4 occurred at the transcriptional level rather than at the translational level. C4 activates PKC isoforms to dephosphorylate and acetylate specific protein 1 (Sp1) by serine and threonine phosphatases, respectively, and phosphorylates specific protein 3 (Sp3) by ERK-MAPK. This leads to displacement of Sp1 from the promoter and binding to Sp3, which activates the transcription of TLR5 in intestinal epithelial cells. This is consistent with a recent study showing that enterobacterial flagellin activates the release of anti-inflammatory factors (IL-10, TGF-β) and reduces inflammation in IECs. C4 is the main metabolite secreted by Enterobacterium, which can initiate TLR5 transcription through Sp3, upregulate TLR5 expression, and inhibit the expression and release of inflammatory factors (IL-6, IFN-γ and TNF-α). In addition, TLR4 can activate innate immune responses by sensing LPS in the cell walls of gram-negative bacteria. C4 can promote TLR4 expression and the phosphorylation of MAPKs and NF-κB to regulate the innate immunity of colon cancer cells, but the specific mechanism remains unclear. To date, there are relatively few studies on the pathway mechanism of SCFA-TLRs in innate immunity, and the correlation between SCFAs and TLR signaling pathways is not clear. However, existing studies have clearly shown that SCFAs play an anti-inflammatory role by regulating the expression of TLRs, which is important for the regulation of immune homeostasis in the body.

Regulation of neutrophils by SCFAs

Neutrophils are considered the most abundant innate immune cells in the bone marrow and peripheral blood. SCFAs affect the recruitment of neutrophils to the site of inflammation and reduce inflammation. SCFAs increase the expression of L-selectin on the surface of neutrophil granulocytes, activate neutrophil chemotactic recruitment to the inflammatory site, and aggravate the inflammatory process without affecting the expression of β2 integrin mRNA. SCFAs induce the aggregation of neutrophils to the site of inflammation through the CPR43 receptor. This process is associated with the activation of intracellular protein kinase P38 and the coupling of Gi/o and Gq proteins. In a model of gout induced by sodium urate monohydrate (MSU), C2 promoted neutrophil reactive oxygen species (ROS) production in a GPR43-dependent manner, indirectly activated the NLRP3 inflammasome, led to neutrophil recruitment to the inflammatory site, promoted inflammasome activation, and promoted the release of IL-1β and IL-10. C4 significantly inhibits the production of proinflammatory cytokines (e.g., IL-6, TNF-α and IFN-γ) and chemokines (e.g., CCL3, CCL4, CXCL1 and IL-8) secreted by neutrophils in the intestines of patients with colitis to reduce intestinal inflammation, and C4 inhibits the secretion of proinflammatory cytokines in an HCDAC-dependent manner. C2 also reduces the infiltration of pancreatic neutrophils and significantly reduces pancreatitis in mice.

Macrophages

Macrophages are essential for maintaining homeostasis in the gut. Previous studies have shown that the process by which C4 inhibits the production of inflammatory cytokines by intestinal macrophages is related to the inhibition of HDAC activity. C4 induces anti-inflammatory properties of macrophages in a GPR109-dependent manner. A recent study showed that C4 alters macrophage metabolism and increases their antibacterial activity. Metabolomic analysis of butyrate-treated macrophages revealed a substantial reduction in glycolysis. This was associated with higher amounts of adenosine monophosphate, an inducer of MAPK, which, in turn, inhibits mTOR. As mTOR is a positive regulator of glycolytic enzymes, its inhibition may explain the observed reduction in glycolysis. Moreover, mTOR is considered a key regulator of autophagy. The bacteria-associated autophagy protein microtubule-associated protein 1 light chain 3α (LC3) is a key participant in autophagy, and experiments have shown that the conversion rate of LC3 and ROS production are increased. Further analysis by single-cell RNA sequencing revealed that the C4-induced antibacterial signature is characterized by increased expression of the S100A8 and S100A9 genes, which encode calprotectin, a protein with antibacterial properties. Therefore, C4 helps increase the antibacterial activity of macrophages by inhibiting mTOR. In addition, in the presence of C4 and pertussis toxin (GPCR inhibitors), macrophages exhibit enhanced antibacterial activity, indicating that C4 enhances the antibacterial activity of macrophages without the involvement of GPCR. Further studies have shown that butyrate increases the expression of the S100A8 mRNA gene through its inhibition of HDAC3. Changes in metabolism enhance the bactericidal function of macrophages. Similarly, in mouse pancreatitis caused by Staphylococcus aureus, C4 enhances the antibacterial program of macrophages by inhibiting HDAC3. Earlier studies have also found that the in vitro stimulation of mouse macrophages with butyrate leads to inhibition of inflammatory responses and decreases in nitric oxide levels, a process mediated by HDAC. In addition, SCFAs downregulate M2 polarization in human and mouse alveolar macrophages in vitro and may activate GPR43 but not GPR41. Butyrate and propionate (but not acetate) increase H3 acetylation and inhibit M2 polarization in part through HDAC inhibition.

Natural killer cells

Natural killer cells, which are the first identified ILC subtype, can respond to virus-infected or virus-transformed cells with a variety of effector functions, primarily cell killing and proinflammatory cytokine production. The combination of IL-12 and IL-15 activates natural killer cells and promotes metabolic changes needed for increased receptor expression and cytokine secretion. In IL-12/IL-15-stimulated natural killer cells, C4 inhibits the expression of the cell surface receptors TRAIL, NKp44, NKp30, and NKG2D and significantly inhibits the production of the proinflammatory cytokines TNF-α, IFN-γ, IL-22, soluble Fas ligand, granzyme A, granzyme B and perforin. C3 inhibits the expression of the receptor NKp30 and the production of the proinflammatory cytokines IFN-γ and granzyme B, but C2 does not have the same effect. Researchers have found that C4-treated natural killer cells express higher levels of bromodomain-containing protein 2 (BRD2). BRD2 is an inflammatory cytokine that controls the production of natural killer cells. mTORC1 is a key regulator of natural killer cell metabolism. c-Myc regulates the secretion of survival cytokines in natural killer cells. C4 has been shown to have anti-inflammatory effects by reducing mTOR activity and c-Myc mRNA expression in natural killer cells. In addition, C4 inhibits glycolysis and oxidative phosphorylation in natural killer cells by inhibiting the expression of the first enzyme in the glycolysis pathway, HK2.

Eosinophils

Eosinophils promote a variety of complex immunomodulatory functions. Under inflammatory conditions, proinflammatory factors can activate eosinophils and prolong their survival. Activated eosinophils are important participants in the inflammatory process and secrete proinflammatory factors, including IL-3, IL-6, and tumor necrosis factor-α. These cells also secrete proinflammatory lipid mediators, including platelet activating factor and cysteine-leukotriene. Anti-inflammatory lipid mediators, including lipoxygenase, lysins and protectors, release reactive oxygen species. In a mouse model of allergic airway inflammation, a high-fiber diet, probiotics, or direct administration of SCFAs effectively reduced airway eosinophils by altering the gut microbiome and SCFA levels. Similarly, SCFAs exert the same effect in eosinophilia-related diseases (including asthma, atopic dermatitis, inflammatory bowel diseases, and eosinophilic oesophagitis). A recent study illustrated the mechanism through which SCFAs directly affect eosinophils. Eosinophils treated with C3 and C4 exhibit decreased cell size and number, loss of bilobate nuclei, mitochondrial membrane potential depolarization, and effector caspase activation, which results in the induction of apoptosis by regulating intracellular pathways, a process that may be mediated by inhibition of HDAC independent of the GPR41 and GPR43 receptor pathways. However, C2 does not impair the survival of eosinophils. These findings are consistent with a previous study that revealed that C4 alleviates airway hyperresponsiveness and eosinophilic increases in patients with allergic asthma through HDAC inhibition and a process independent of GPR41 and GPR43 receptor activation. C2 and C3 bind to GPR43 in human eosinophils, resulting in increased intracellular calcium influx. Moreover, C2 and C3 stimulate the production of ROS in human eosinophils in a concentration-dependent manner. Researchers have further investigated the potential of SCFAs to regulate the transcription of genes involved in eosinophilic adhesion, migration, and survival. C3 and C4 have been shown to inhibit eosinophilic adhesion and migration to the endothelial monolayer in response to eotaxin-2 (CCL24). In addition, the surface expression of L-selectin on eosinophils is not affected by SCFAs.

Basophils

At present, there are many studies on the relationship between SCFAs and eosinophils, but there are relatively few studies on the relationship between SCFAs and basophils. C2-treated basophils resulted in increased intracellular calcium influx, but treatment with C3 and C4 did not have the same effect. Activation of basophils is associated with IL-3 induction of CD69 on the cell surface. C3 and C4 showed increased IL-3-induced CD69 expression and increased cell IL-13 and IL-4 secretion by inhibiting HDAC. In addition, C3 and C4 promote an increase in IgE-mediated basophil degranulation. This suggests that SCFAs may be one of the important factors regulating alkaline granulocyte activation, IL-13 expression and degranulation.

Differential regulation of ILC subpopulations by SCFAs

ILCs were divided into groups 1 (NK cells and non-NK cells ILC1), 2 (ILC2) and 3 (ILC3) according to their developmental and functional characteristics. It was found that C2, C3, and C4 triggered the P13K, AKT, and mTOR signaling pathways through the excitatory action of GPR43 receptors, thereby promoting the proliferation of intestinal ILC1s and ILC3s but inhibiting the proliferation of intestinal ILC2s. Similarly, C4 has been shown to inhibit ILC2 proliferation in allergic asthma, but this process may be related to the inhibitory effect of HDAC. This suggests that the effect of SCFAs on ILCs is mediated by both GPR receptors and HDAC.

ILC3s are a major producer of intestinal barrier IL-22, which is a member of the IL-10 family and a key cytokine regulating inflammation. It is upregulated in chronic inflammation and achieves anti-inflammatory effects by inducing intestinal epithelial cells to produce AMP and mucin and repair the integrity of the damaged intestinal epithelial barrier. In ILC3s, SCFAs differentially activate AKT or ERK signaling and increase IL-22 secretion via the AKT and STAT3 axes. Among them, C2 increased the secretion of IL-22 to a greater extent by activating the GPR43 receptor, and C3 increased the secretion of IL-22 to a lesser extent by activating the GPR43 receptor, but C4 had no effect on the secretion of IL-22. The reasons for these findings may be that, on the one hand, C2 and C3 activate the GPR43 receptor in ILCs more easily than C4. On the other hand, it may be that there are other pathways of regulation. For example, C2 enhances the expression of IL-1R in ILC3 cells by activating the GPR43 receptor, and the increased level of IL-1R increases the sensitivity of IL-1β, thereby indirectly inducing the production of IL-22. In addition, SCFAs can promote IL-22 secretion in ILC3s by activating the GPR41 receptor and inhibiting the HDAC pathway ( Figure 2 ). After SCFAs enter cells, they upregulate the expression of hypoxia-inducing factor 1α (HIF1α) and aromatic receptor (AhR), which are differentially regulated by mTOR and STAT3. HIF1α directly binds to the IL-22 promoter. Finally, histone modification increases the binding of HIF1α to the IL-22 promoter to increase IL-22 secretion. In conclusion, different types of SCFAs have different regulatory effects on different types of ILCs, and the mechanism is closely related to the expression of the GPR receptor and the inhibition of HDAC.

T cells

Previous studies have shown that 17 strains in the mouse gut microbiota (belonging to clusters IV, XIVa, and XVIII of Clostridium difficile) induce the TGF-β response by producing SCFAs, which may contribute to the differentiation and amplification of Tregs in the colons of mice. It was later determined that SCFAs promote the proliferation of Tregs. Treg cells include FoxP3+ T cells, which prevent inflammatory reactions in the gut by producing IL-10. In the presence of Treg cell polarization, C4 treatment of naive T cells enhanced histone H3 acetylation in the promoter, specifically inducing differentiation of mouse colon Treg cells by upregulating the acetylation of conserved noncoding sequences at FoxP3. SCFAs can also indirectly promote the proliferation of Treg cells and IL-10 production through other cell types. For example, C4 can act on macrophages and DCs in a GPR109A-dependent manner, indirectly inducing FoxP3+ T-cell and IL-10 production. However, a recent study found that C5 did not increase the amplification of Treg cells but increased the amount of additional acetyl-CoA in T cells, enhanced glycolysis through the mTOR activation pathway, and increased IL-10 production in lymphocytes by acting as a substrate for HAT to regulate the gene recoding process.

SCFAs regulate T-cell metabolism through HDAC inhibition. SCFAs can increase the differentiation of naive T cells into effector T cells, such as Th1 and Th17 effector T cells, which may be related to the inhibitory activity of HDAC. In T cells, SCFAs were found to increase the acetylation of p70 S6 kinase and the phosphorylation of rS6 by inhibiting HDAC activity, thereby increasing mTOR activity to increase the production of Th17 and Th1 cells and IL-10(+) T cells.

SCFAs can affect T cells during the antiviral process. It was found that oral SCFAs may affect CD8+ T-cell metabolism in a GPR-dependent manner and by inhibiting HDAC action during active immunity to ensure rapid activation of effector T cells in response to viral infection. Further studies later found that the regulation of C4 on CD8+ T cells was mediated by the inhibitory activity of HDAC, independent of the GPR41 and GPR43 receptors. SCFAs (specifically C4) also increase the number of CD8+ memory T cells in the spleen and liver and play an important role in establishing an optimal secondary antigen-specific response. This process is generally thought to increase glycolysis and mitochondrial mass to promote the survival and activation of CD8+ memory T cells. SCFAs have been widely recognized as an energy source for cells. In the tumor microenvironment, SCFAs can enhance the ability of CD8+ T cells to compete with tumor cells for glucose, thus increasing the survival and activation of CD8+ T cells. SCFAs enhance the antitumor activity of CD8+ T cells and chimeric antigen receptor (CAR) T cells through metabolic and epigenetic reprogramming. Therefore, SCFAs can regulate the metabolism of T cells according to the states of the host.

B cells

B cells require glycolysis, oxidative phosphorylation, and the synthesis of palmitic acid (PA) in the processes of proliferation, differentiation, and secretion of antibodies. Glycolysis and oxidative phosphorylation are essential for the survival of germinal B cells, and fatty acids (FAs) are involved in the process of antibody secretion by regulatory plasma cells (PCs). Previous studies have shown that certain probiotics, such as Lactobacillus and Bifidobacterium species, increase fecal and serum IgA and IgG levels but decrease fecal and serum IgA levels in germ-free and antibiotic-treated mice. In mice fed prebiotics, SCFA content and IgA levels in feces and the large intestine increased in a dose-dependent manner, with increased IgA and IgG levels in serum and no change in IgE and IgM levels. These findings suggest that SCFAs produced by prebiotics may promote the differentiation of B cells and the production of antibodies. The differentiation of B cells into PCs and the production of antibodies require energy metabolism within the cell to produce sufficient ATP. Previous studies have shown that SCFAs can be converted to acetyl-CoA (which produces ATP in the TCA cycle) via acetyl/propionyl/butyryl CoA. Acetyl-coA is the main substrate for FA synthesis. FA contributes to the differentiation of plasma B cells and stimulates B cells to produce antibodies. The contents of acetyl-CoA, ATP, lipids, malonyl CoA and fatty acid synthase (FAS) were increased in B cells treated with SCFAs, and ATP, malonyl CoA and FAS were essential for FA production. In addition, SCFAs promote B-cell differentiation and antibody production by increasing glycolysis in B cells.

SCFAs affect B-cell differentiation and antibody production through HDAC inhibition and GPR receptor mediation. Studies have found that SCFAs change the expression of B-cell-related genes (IgGs, IgA, Igj, Igk, Igl, Aicda, Xbp1, Irf4, etc.) by inhibiting HDAC. These genes participate in the differentiation of B cells and promote their differentiation into antibody-producing PCs. B cells can express the GPR receptor, and studies have found that compared with wild-type mice, mice lacking the GPR43 receptor have relatively low IgA levels in the gut.

SCFAs regulate B cells through a number of indirect mechanisms. SCFAs increase glucose uptake by T helper cells and follicular helper T-cell (Tfh) induction, which regulates B-cell and antibody production. C2 amplifies TLR signals in Tfh cells, and TLR selectively changes the levels of some IgA-producing microorganisms by sensing LPS from different microorganisms. In addition, C2 regulates antibody secretion by regulating dendritic cells (DCs), activates B cells by producing BAFF/APRIL and produces retinoic acid (RA) to induce IgA production.

SCFAs can regulate the production of B10 cells (regulatory B cells (Bregs) that produce IL-10 to maintain immune homeostasis) by a different mechanism. C2 can be converted to acetyl-CoA synthetase (ACSS), which increases the differentiation of B10 cells in the peritoneal cavity of mice by promoting the acetylation of ATP and lysine produced by the TCA cycle. C3 has no direct effect on the differentiation of B10 cells. C4 has been reported to induce an increase in splenic B10 cells by indirectly promoting the production of the serotonin-derived metabolite 5-hydroxyindole-3-acetic acid. C4 can also induce IL-10-producing splenic B10 cells by regulating the circadian clock-related genes RAR-associated orphan receptor α and nuclear receptor subfamily 1 group D member 1. A subsequent study showed that SCFAs upregulated peritoneal B10 cells in colitis mice in a manner dependent on their HDAC inhibitory activity. Independent of the GPR receptor pathway, transcriptional analysis showed that the action of C4 on B10 cells was related to the activation of p38 MAPK. C5 can not only increase the secretion of IL-10 but also significantly inhibit the apoptosis of Bregs. These results indicate that different SCFAs have different effects on B10 cell development, which encourages us to conduct further research.

Allergic asthma

The pathogenesis of allergic asthma is not well understood. Clinical treatment focuses on reducing symptoms by inhalation of corticosteroids and β-2 adrenergic agonists. Recently, mice fed SCFAs showed the protective effects of SCFAs against allergic airway inflammation. The inflow of eosinophils into the lung parenchyma is the signature feature of the most common allergic asthma.

During allergic inflammation, IL-5, IL-13, and granulocyte macrophage colony-stimulating factor (GM-CSF) secreted by Th2 and ILC2 cells promote eosinophil survival. Activated eosinophils are major sources of cytokines, growth factors, and cytotoxic granulocytes (such as eosinophil-derived neurotoxins and major basic proteins) that can cause tissue damage and airway remodeling when released. Recent in vitro studies using human peripheral blood eosinophils have shown that C3 and C4 inhibit eosinophils from adhering to endothelial cells in response to CCL24 flow, and C4 inhibits eosinophil migration and promotes eosinophil apoptosis. Surprisingly, these effects may be independent of GPR43 or GPR41 receptors but depend on the flow of these SCFAs into eosinophils via monocarboxylate transporters. In addition, we found that the biological effects of SCFAs on eosinophils are consistent with epigenetic regulation of gene expression by class IIa DAC, suggesting that these effects of SCFAs on eosinophils may be mediated by HDAC. However, a previous study showed that diet-induced C3 prevents airway inflammation, resulting in decreased eosinophilic infiltration in lung tissue and decreased concentrations of the cytokines IL-4, IL-5, and IL-17A. This effect requires the participation of GPR41 but not GPR43 and is attributable to impaired DC activation. Therefore, whether the effect of SCFAs on eosinophils depends on GPR43 or GPR41 receptors needs to be further investigated.

ILCs function to coordinate immunity, inflammation and tissue repair and can be present on the mucosal surface of the lung and drive allergic airway inflammatory responses. ILC2s are of great concern in the context of asthma and allergic diseases because they promote Th2 immunity. Systemic and local administration of C4 attenuates ILC2-driven airway hyperresponsiveness and eosinophil inflammation. C4 can regulate the expression of ILC2s and inhibit their proliferation at the transcriptional level. C4 inhibits the proliferation of ILC2s and the production of the cytokines IL-5 and IL-13 by inhibiting the activity of HDAC without affecting cell viability and without being mediated by the activation of GPR41 or GPR43. C2 may increase the acetylation of the Foxp3 promoter through the inhibition of HDAC9, thus inhibiting the occurrence of allergic asthma. In addition, SCFAs can also affect allergic airway inflammation by affecting lung airway mast cells, Treg cells, Th9 cells, DCs, etc.. There are multiple mechanisms for the beneficial effects of SCFAs on the human airway immune inflammatory response, and further well-controlled long-term intervention studies are needed to confirm the beneficial effects of SCFAs in airway immune inflammatory diseases.

Colitis

High dietary fiber intake and increased SCFA levels play an important role in protecting colon immune barrier function and in the colonic secretion of anti-inflammatory factors. SCFA administration can improve the symptoms of various types of colitis and reduce the probability of human colitis. Chronic intestinal inflammation can increase the risk of colon cancer. The concentration of SCFAs in stool is closely related to the incidence of colitis and colon cancer. SCFAs can reduce the risk of chronic colitis developing into colon cancer and promote the apoptosis of cancer cells to play an antitumor role. Studies have shown that the number of butyrate-producing bacteria in colon cancer patients is significantly reduced, and the expression of receptors GPR43 and GPR109A is also reduced considerably, indicating that SCFAs have a protective effect on colitis and colon cancer. The protective effect of SCFAs on colitis has been discussed extensively. SCFAs can regulate colon inflammation through innate immunity and antigen-specific adaptive immunity. As previously discussed, SCFAs can mediate a natural immune inflammatory response by inhibiting HDAC activity via GPR receptors. SCFAs can also affect intestinal IL-10 production and IgA secretion through multiple mechanisms. SCFAs generally show anti-inflammatory effects in the colon depending on the concentration and the immunological environment.

Osteoporosis

Osteohomeostasis is maintained through coordination between the bone formation process managed by osteoblasts and bone resorption managed by osteoclasts. Probiotics prevent bone loss, promote bone formation and increase bone volume in mice. Previous studies have shown that SCFAs can indirectly stimulate bone formation. C4 increases the proportion of CD4+/CD8+ T cells and the number of Treg cells in the bone marrow. Treg cells activate NFAT and SMAD signal transduction, which results in indirect induction of Wnt10b production in CD8+ T cells and thus indirect stimulation of bone formation. A recent study showed that C3 and C4 directly upregulate osteoblast differentiation. Alkaline phosphatase (ALP) activity is a marker of osteogenic differentiation of mouse embryonic osteoblast progenitor cells (MC3T3-E1 cells). C2 and C3 increase the activity of ALP, and C2 increases the expression of ALP mRNA; however, C4 does not affect the activity of ALP or the expression of ALP mRNA. Osteopathic (OPN) is a highly phosphorylated and glycosylated salivary protein that is expressed in osteoblasts and osteoclasts. C2, C3 and C4 increase the expression of OPN in MC3T3-E1 cells. SCFAs can inhibit osteoclast differentiation. The differentiation of precursor cells into mature osteoclasts depends on oxidative phosphorylation, and the bone resorption of mature osteoclasts depends on glycolysis. By inducing the metabolic recoding of osteoclasts, C3 and C4 weaken the oxidative phosphorylation of precursor cells through a process dependent on mature osteoclasts, enhance glycolysis, induce a stress response, and prevent osteoclast differentiation. Moreover, C3 and C4 downregulate the expression of the osteoclast genes TRAF6 and NFATC1 to inhibit osteoclast differentiation.

Conclusion

Over the past few decades, by sequencing and analyzing different types of human gut microbiota and constructing their metabolic processes, researchers have recognized the important roles of microbial metabolites in health and disease mediated through microbe-host interactions. As one of the most important metabolites of intestinal microorganisms, SCFAs have been shown to regulate host physiology and health through innate and adaptive immunity. For example, SCFAs can affect the inflammatory response of the central nervous system and affect bone diseases. In addition, it can regulate rheumatic diseases, osteoarthritis, hepatitis, vasculitis and so on. Although the current review has limitations, it is challenging to decipher all the complexities of the effects of intestinal SCFAs on immune metabolism. This calls for further exploration of the relationship between SCFA pairs and the immune system, which is critical for identifying treatment options based on SCFAs.

Author contributions

All authors listed have made a substantial, direct, and intellectual contribution to the work and approved it for publication.

References 209

  1. 1.

    Macfarlane S Macfarlane GT. Regulation of short-chain fatty acid production. Proc Nutr Soc (2003 ) 62(1):67–72

    Not in our library10.1079/pns2002207

  2. 2.

    Cummings JH Pomare EW Branch WJ Naylor CP Macfarlane GT. Short chain fatty acids in human Large intestine, portal, hepatic and venous blood. Gut (1987 ) 28(10):1221–7

    Not in our library10.1136/gut.28.10.1221

  3. 3.

    Murase M Kimura Y Nagata Y. Determination of portal short-chain fatty acids in rats fed various dietary fibers by capillary gas chromatography. J Chromatogr B Biomed Appl (1995 ) 664(2):415–20

    Not in our library10.1016/0378-4347(94)00491-m

  4. 4.

    Alexander KL Targan SR Elson CO 3rd. Microbiota activation and regulation of innate and adaptive immunity. Immunol Rev (2014 ) 260(1):206–20

    Not in our library10.1111/imr.12180

  5. 5.

    Belkaid Y Hand TW. Role of the microbiota in immunity and inflammation. Cell (2014 ) 157(1):121–41

    Not in our library10.1016/j.cell.2014.03.011

  6. 6.

    Fernandes J Su W Rahat-Rozenbloom S Wolever TM Comelli EM. Adiposity, gut microbiota and faecal short chain fatty acids are linked in adult humans. Nutr Diabetes (2014 ) 4(6):e121

    Not in our library10.1038/nutd.2014.23

  7. 7.

    Litvak Y Byndloss MX Bäumler AJ. Colonocyte metabolism shapes the gut microbiota. Sci (New York NY) (2018 ) 362(6418):eaat9076

    Not in our library10.1126/science.aat9076

  8. 8.

    Bronner DN Faber F Olsan EE Byndloss MX Sayed NA Xu G. Genetic ablation of butyrate utilization attenuates gastrointestinal salmonella disease. Cell Host Microbe (2018 ) 23(2):266–73.e4

    Not in our library10.1016/j.chom.2018.01.004

  9. 9.

    Spiga L Winter MG Furtado de Carvalho T Zhu W Hughes ER Gillis CC. An oxidative central metabolism enables salmonella to utilize microbiota-derived succinate. Cell Host Microbe (2017 ) 22(3):291–301.e6

    Not in our library10.1016/j.chom.2017.07.018

  10. 10.

    El Kaoutari A Armougom F Gordon JI Raoult D Henrissat B. The abundance and variety of carbohydrate-active enzymes in the human gut microbiota. Nat Rev Microbiol (2013 ) 11(7):497–504

    Not in our library10.1038/nrmicro3050

  11. 11.

    Louis P Hold GL Flint HJ. The gut microbiota, bacterial metabolites and colorectal cancer. Nat Rev Microbiol (2014 ) 12(10):661–72

    Not in our library10.1038/nrmicro3344

  12. 12.
  13. 13.

    Koh A De Vadder F Kovatcheva-Datchary P Bäckhed F. From dietary fiber to host physiology: short-chain fatty acids as key bacterial metabolites. Cell (2016 ) 165(6):1332–45

    Not in our library10.1016/j.cell.2016.05.041

  14. 14.

    Reichardt N Duncan SH Young P Belenguer A McWilliam Leitch C Scott KP. Phylogenetic distribution of three pathways for propionate production within the human gut microbiota. ISME J (2014 ) 8(6):1323–35

    Not in our library10.1038/ismej.2014.14

  15. 15.

    Louis P Flint HJ. Diversity, metabolism and microbial ecology of butyrate-producing bacteria from the human Large intestine. FEMS Microbiol Lett (2009 ) 294(1):1–8

    Not in our library10.1111/j.1574-6968.2009.01514.x

  16. 16.

    Krautkramer KA Fan J Bäckhed F. Gut microbial metabolites as multi-kingdom intermediates. Nat Rev Microbiol (2021 ) 19(2):77–94

    Not in our library10.1038/s41579-020-0438-4

  17. 17.

    Qin J Li R Raes J Arumugam M Burgdorf KS Manichanh C. A human gut microbial gene catalogue established by metagenomic sequencing. Nature (2010 ) 464(7285):59–65

    Not in our library10.1038/nature08821

  18. 18.

    Louis P Flint HJ. Formation of propionate and butyrate by the human colonic microbiota. Environ Microbiol (2017 ) 19(1):29–41

    Not in our library10.1111/1462-2920.13589

  19. 19.

    Ragsdale SW Pierce E. Acetogenesis and the wood-ljungdahl pathway of Co(2) fixation. Biochim Biophys Acta (2008 ) 1784(12):1873–98

    Not in our library10.1016/j.bbapap.2008.08.012

  20. 20.

    Hetzel M Brock M Selmer T Pierik AJ Golding BT Buckel W. Acryloyl-coa reductase from clostridium propionicum. an enzyme complex of propionyl-coa dehydrogenase and electron-transferring flavoprotein. Eur J Biochem (2003 ) 270(5):902–10

    Not in our library10.1046/j.1432-1033.2003.03450.x

  21. 21.

    Scott KP Martin JC Campbell G Mayer CD Flint HJ. Whole-genome transcription profiling reveals genes up-regulated by growth on fucose in the human gut bacterium “Roseburia inulinivorans”. J bacteriology (2006 ) 188(12):4340–9

    Not in our library10.1128/jb.00137-06

  22. 22.

    Louis P Duncan SH McCrae SI Millar J Jackson MS Flint HJ. Restricted distribution of the butyrate kinase pathway among butyrate-producing bacteria from the human colon. J bacteriology (2004 ) 186(7):2099–106

    Not in our library10.1128/jb.186.7.2099-2106.2004

  23. 23.

    Duncan SH Barcenilla A Stewart CS Pryde SE Flint HJ. Acetate utilization and butyryl coenzyme a (Coa):Acetate-coa transferase in butyrate-producing bacteria from the human Large intestine. Appl Environ Microbiol (2002 ) 68(10):5186–90

    Not in our library10.1128/aem.68.10.5186-5190.2002

  24. 24.
  25. 25.

    Smith EA Macfarlane GT. Dissimilatory amino acid metabolism in human colonic bacteria. Anaerobe (1997 ) 3(5):327–37

    Not in our library10.1006/anae.1997.0121

  26. 26.

    Windey K De Preter V Verbeke K. Relevance of protein fermentation to gut health. Mol Nutr Food Res (2012 ) 56(1):184–96

    Not in our library10.1002/mnfr.201100542

  27. 27.
  28. 28.

    Topping DL Clifton PM. Short-chain fatty acids and human colonic function: roles of resistant starch and nonstarch polysaccharides. Physiol Rev (2001 ) 81(3):1031–64

    Not in our library10.1152/physrev.2001.81.3.1031

  29. 29.

    Li H Myeroff L Smiraglia D Romero MF Pretlow TP Kasturi L. Slc5a8, a sodium transporter, is a tumor suppressor gene silenced by methylation in human colon aberrant crypt foci and cancers. Proc Natl Acad Sci United States America (2003 ) 100(14):8412–7

    Not in our library10.1073/pnas.1430846100

  30. 30.

    Miyauchi S Gopal E Fei YJ Ganapathy V. Functional identification of Slc5a8, a tumor suppressor down-regulated in colon cancer, as a na(+)-coupled transporter for short-chain fatty acids. J Biol Chem (2004 ) 279(14):13293–6

    Not in our library10.1074/jbc.c400059200

  31. 31.

    Martin PM Dun Y Mysona B Ananth S Roon P Smith SB. Expression of the sodium-coupled monocarboxylate transporters Smct1 (Slc5a8) and Smct2 (Slc5a12) in retina. Invest Ophthalmol Visual Sci (2007 ) 48(7):3356–63

    Not in our library10.1167/iovs.06-0888

  32. 32.

    Suzuki T Yoshida S Hara H. Physiological concentrations of short-chain fatty acids immediately suppress colonic epithelial permeability. Br J Nutr (2008 ) 100(2):297–305

    Not in our library10.1017/s0007114508888733

  33. 33.

    Gopal E Fei YJ Miyauchi S Zhuang L Prasad PD Ganapathy V. Sodium-coupled and electrogenic transport of b-complex vitamin nicotinic acid by Slc5a8, a member of the Na/Glucose Co-transporter gene family. Biochem J (2005 ) 388(Pt 1):309–16

    Not in our library10.1042/bj20041916

  34. 34.

    Sivaprakasam S Bhutia YD Yang S Ganapathy V. Short-chain fatty acid transporters: role in colonic homeostasis. Compr Physiol (2017 ) 8(1):299–314

    Not in our library10.1002/cphy.c170014

  35. 35.

    Gurav A Sivaprakasam S Bhutia YD Boettger T Singh N Ganapathy V. Slc5a8, a na+-coupled high-affinity transporter for short-chain fatty acids, is a conditional tumour suppressor in colon that protects against colitis and colon cancer under low-fibre dietary conditions. Biochem J (2015 ) 469(2):267–78

    Not in our library10.1042/bj20150242

  36. 36.

    Binder HJ Mehta P. Short-chain fatty acids stimulate active sodium and chloride absorption in vitro in the rat distal colon. Gastroenterology (1989 ) 96(4):989–96

    Not in our library10.1016/0016-5085(89)91614-4

  37. 37.

    Bloemen JG Venema K van de Poll MC Olde Damink SW Buurman WA Dejong CH. Short chain fatty acids exchange across the gut and liver in humans measured at surgery. Clin Nutr (Edinburgh Scotland) (2009 ) 28(6):657–61

    Not in our library10.1016/j.clnu.2009.05.011

  38. 38.

    Canfora EE Jocken JW Blaak EE. Short-chain fatty acids in control of body weight and insulin sensitivity. Nat Rev Endocrinol (2015 ) 11(10):577–91

    Not in our library10.1038/nrendo.2015.128

  39. 39.

    Kim M Qie Y Park J Kim CH. Gut microbial metabolites fuel host antibody responses. Cell Host Microbe (2016 ) 20(2):202–14

    Not in our library10.1016/j.chom.2016.07.001

  40. 40.

    Piekarska J Miśta D Houszka M Króliczewska B Zawadzki W Gorczykowski M. Trichinella spiralis: the influence of short chain fatty acids on the proliferation of lymphocytes, the goblet cell count and apoptosis in the mouse intestine. Exp Parasitol (2011 ) 128(4):419–26

    Not in our library10.1016/j.exppara.2011.05.019

  41. 41.

    Sencio V Barthelemy A Tavares LP Machado MG Soulard D Cuinat C. Gut dysbiosis during influenza contributes to pulmonary pneumococcal superinfection through altered short-chain fatty acid production. Cell Rep (2020 ) 30(9):2934–47.e6

    Not in our library10.1016/j.celrep.2020.02.013

  42. 42.
  43. 43.

    Brown AJ Goldsworthy SM Barnes AA Eilert MM Tcheang L Daniels D. The orphan G protein-coupled receptors Gpr41 and Gpr43 are activated by propionate and other short chain carboxylic acids. J Biol Chem (2003 ) 278(13):11312–9

    Not in our library10.1074/jbc.m211609200

  44. 44.

    Singh N Gurav A Sivaprakasam S Brady E Padia R Shi H. Activation of Gpr109a, receptor for niacin and the commensal metabolite butyrate, suppresses colonic inflammation and carcinogenesis. Immunity (2014 ) 40(1):128–39

    Not in our library10.1016/j.immuni.2013.12.007

  45. 45.

    Pluznick J. A novel scfa receptor, the microbiota, and blood pressure regulation. Gut Microbes (2014 ) 5(2):202–7

    Not in our library10.4161/gmic.27492

  46. 46.

    de Ruijter AJ van Gennip AH Caron HN Kemp S van Kuilenburg AB. Histone deacetylases (Hdacs): characterization of the classical hdac family. Biochem J (2003 ) 370(Pt 3):737–49

    Not in our library10.1042/bj20021321

  47. 47.

    Gregoretti IV Lee YM Goodson HV. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol (2004 ) 338(1):17–31

    Not in our library10.1016/j.jmb.2004.02.006

  48. 48.

    Hinnebusch BF Meng S Wu JT Archer SY Hodin RA. The effects of short-chain fatty acids on human colon cancer cell phenotype are associated with histone hyperacetylation. J Nutr (2002 ) 132(5):1012–7

    Not in our library10.1093/jn/132.5.1012

  49. 49.

    Haberland M Montgomery RL Olson EN. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat Rev Genet (2009 ) 10(1):32–42

    Not in our library10.1038/nrg2485

  50. 50.

    Roth SY Denu JM Allis CD. Histone acetyltransferases. Annu Rev Biochem (2001 ) 70:81–120

    Not in our library10.1146/annurev.biochem.70.1.81

  51. 51.

    Kuo MH Allis CD. Roles of histone acetyltransferases and deacetylases in gene regulation. BioEssays: News Rev molecular Cell Dev Biol (1998 ) 20(8):615–26

    Not in our library10.1002/(sici)1521-1878(199808)20:8<615::aid-bies4>3.0.co;2-h

  52. 52.

    Smith BC Denu JM. Chemical mechanisms of histone lysine and arginine modifications. Biochim Biophys Acta (2009 ) 1789(1):45–57

    Not in our library10.1016/j.bbagrm.2008.06.005

  53. 53.

    Baeuerle PA Baichwal VR. Nf-kappa b as a frequent target for immunosuppressive and anti-inflammatory molecules. Adv Immunol (1997 ) 65:111–37

    Not in our library10.1016/s0065-2776(08)60742-7

  54. 54.

    Pahl HL. Activators and target genes of Rel/Nf-kappab transcription factors. Oncogene (1999 ) 18(49):6853–66

    Not in our library10.1038/sj.onc.1203239

  55. 55.

    Liu SF Malik AB. Nf-kappa b activation as a pathological mechanism of septic shock and inflammation. Am J Physiol Lung Cell Mol Physiol (2006 ) 290(4):L622–l45

    Not in our library10.1152/ajplung.00477.2005

  56. 56.

    Li M van Esch B Wagenaar GTM Garssen J Folkerts G Henricks PAJ. Pro- and anti-inflammatory effects of short chain fatty acids on immune and endothelial cells. Eur J Pharmacol (2018 ) 831:52–9

    Not in our library10.1016/j.ejphar.2018.05.003

  57. 57.

    Vallabhapurapu S Karin M. Regulation and function of nf-kappab transcription factors in the immune system. Annu Rev Immunol (2009 ) 27:693–733

    Not in our library10.1146/annurev.immunol.021908.132641

  58. 58.

    Tedelind S Westberg F Kjerrulf M Vidal A. Anti-inflammatory properties of the short-chain fatty acids acetate and propionate: a study with relevance to inflammatory bowel disease. World J Gastroenterol (2007 ) 13(20):2826–32

    Not in our library10.3748/wjg.v13.i20.2826

  59. 59.

    Ashburner BP Westerheide SD Baldwin AS Jr. The P65 (Rela) subunit of nf-kappab interacts with the histone deacetylase (Hdac) corepressors Hdac1 and Hdac2 to negatively regulate gene expression. Mol Cell Biol (2001 ) 21(20):7065–77

    Not in our library10.1128/mcb.21.20.7065-7077.2001

  60. 60.

    Chen L Fischle W Verdin E Greene WC. Duration of nuclear nf-kappab action regulated by reversible acetylation. Sci (New York NY) (2001 ) 293(5535):1653–7

    Not in our library10.1126/science.1062374

  61. 61.

    Säemann MD Böhmig GA Osterreicher CH Burtscher H Parolini O Diakos C. Anti-inflammatory effects of sodium butyrate on human monocytes: potent inhibition of il-12 and up-regulation of il-10 production. FASEB J (2000 ) 14(15):2380–2

    Not in our library10.1096/fj.00-0359fje

  62. 62.

    Usami M Kishimoto K Ohata A Miyoshi M Aoyama M Fueda Y. Butyrate and trichostatin a attenuate nuclear factor kappab activation and tumor necrosis factor alpha secretion and increase prostaglandin E2 secretion in human peripheral blood mononuclear cells. Nutr Res (New York NY) (2008 ) 28(5):321–8

    Not in our library10.1016/j.nutres.2008.02.012

  63. 63.

    Ni YF Wang J Yan XL Tian F Zhao JB Wang YJ. Histone deacetylase inhibitor, butyrate, attenuates lipopolysaccharide-induced acute lung injury in mice. Respir Res (2010 ) 11(1):33

    Not in our library10.1186/1465-9921-11-33

  64. 64.

    Lee SU In HJ Kwon MS Park BO Jo M Kim MO. β-arrestin 2 mediates G protein-coupled receptor 43 signals to nuclear factor-κb. Biol Pharm Bull (2013 ) 36(11):1754–9

    Not in our library10.1248/bpb.b13-00312

  65. 65.

    Luttrell LM Lefkowitz RJ. The role of beta-arrestins in the termination and transduction of G-Protein-Coupled receptor signals. J Cell Sci (2002 ) 115(Pt 3):455–65

    Not in our library10.1242/jcs.115.3.455

  66. 66.

    Yao Y Cai X Fei W Ye Y Zhao M Zheng C. The role of short-chain fatty acids in immunity, inflammation and metabolism. Crit Rev Food Sci Nutr (2022 ) 62(1):1–12

    Not in our library10.1080/10408398.2020.1854675

  67. 67.

    Luu M Visekruna A. Short-chain fatty acids: bacterial messengers modulating the immunometabolism of T cells. Eur J Immunol (2019 ) 49(6):842–8

    Not in our library10.1002/eji.201848009

  68. 68.

    Arthur JS Ley SC. Mitogen-activated protein kinases in innate immunity. Nat Rev Immunol (2013 ) 13(9):679–92

    Not in our library10.1038/nri3495

  69. 69.

    Liu Y Shepherd EG Nelin LD. Mapk phosphatases–regulating the immune response. Nat Rev Immunol (2007 ) 7(3):202–12

    Not in our library10.1038/nri2035

  70. 70.

    Jeong Y Du R Zhu X Yin S Wang J Cui H. Histone deacetylase isoforms regulate innate immune responses by deacetylating mitogen-activated protein kinase phosphatase-1. J leukocyte Biol (2014 ) 95(4):651–9

    Not in our library10.1189/jlb.1013565

  71. 71.

    Roger T Lugrin J Le Roy D Goy G Mombelli M Koessler T. Histone deacetylase inhibitors impair innate immune responses to toll-like receptor agonists and to infection. Blood (2011 ) 117(4):1205–17

    Not in our library10.1182/blood-2010-05-284711

  72. 72.

    Seljeset S Siehler S. Receptor-specific regulation of Erk1/2 activation by members of the “Free fatty acid receptor” family. J receptor Signal transduction Res (2012 ) 32(4):196–201

    Not in our library10.3109/10799893.2012.692118

  73. 73.

    Thorburn AN Macia L Mackay CR. Diet, metabolites, and “Western-lifestyle” inflammatory diseases. Immunity (2014 ) 40(6):833–42

    Not in our library10.1016/j.immuni.2014.05.014

  74. 74.

    Noureldein MH Eid AA. Gut microbiota and mtor signaling: insight on a new pathophysiological interaction. Microbial pathogenesis (2018 ) 118:98–104

    Not in our library10.1016/j.micpath.2018.03.021

  75. 75.

    Wellen KE Hatzivassiliou G Sachdeva UM Bui TV Cross JR Thompson CB. Atp-citrate lyase links cellular metabolism to histone acetylation. Sci (New York NY) (2009 ) 324(5930):1076–80

    Not in our library10.1126/science.1164097

  76. 76.
  77. 77.

    Balmer ML Ma EH Bantug GR Grählert J Pfister S Glatter T. Memory Cd8(+) T cells require increased concentrations of acetate induced by stress for optimal function. Immunity (2016 ) 44(6):1312–24

    Not in our library10.1016/j.immuni.2016.03.016

  78. 78.

    Kawai T Akira S. Signaling to nf-kappab by toll-like receptors. Trends Mol Med (2007 ) 13(11):460–9

    Not in our library10.1016/j.molmed.2007.09.002

  79. 79.

    Kawai T Akira S. Toll-like receptor and rig-I-Like receptor signaling. Ann New York Acad Sci (2008 ) 1143:1–20

    Not in our library10.1196/annals.1443.020

  80. 80.

    Kanneganti TD Body-Malapel M Amer A Park JH Whitfield J Franchi L. Critical role for Cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded rna. J Biol Chem (2006 ) 281(48):36560–8

    Not in our library10.1074/jbc.m607594200

  81. 81.

    Macia L Tan J Vieira AT Leach K Stanley D Luong S. Metabolite-sensing receptors Gpr43 and Gpr109a facilitate dietary fibre-induced gut homeostasis through regulation of the inflammasome. Nat Commun (2015 ) 6:6734

    Not in our library10.1038/ncomms7734

  82. 82.
  83. 83.

    Yuan X Wang L Bhat OM Lohner H Li PL. Differential effects of short chain fatty acids on endothelial Nlrp3 inflammasome activation and neointima formation: antioxidant action of butyrate. Redox Biol (2018 ) 16:21–31

    Not in our library10.1016/j.redox.2018.02.007

  84. 84.

    Gao Y Xie D Wang Y Niu L Jiang H. Short-chain fatty acids reduce oligodendrocyte precursor cells loss by inhibiting the activation of astrocytes Via the Sgk1/Il-6 signalling pathway. Neurochemical Res (2022 ) 47(11):3476–89

    Not in our library10.1007/s11064-022-03710-0

  85. 85.

    Bailón E Cueto-Sola M Utrilla P Rodríguez-Cabezas ME Garrido-Mesa N Zarzuelo A. Butyrate in vitro immune-modulatory effects might be mediated through a proliferation-related induction of apoptosis. Immunobiology (2010 ) 215(11):863–73

    Not in our library10.1016/j.imbio.2010.01.001

  86. 86.

    Halili MA Andrews MR Labzin LI Schroder K Matthias G Cao C. Differential effects of selective hdac inhibitors on macrophage inflammatory responses to the toll-like receptor 4 agonist lps. J leukocyte Biol (2010 ) 87(6):1103–14

    Not in our library10.1189/jlb.0509363

  87. 87.

    Abreu MT. Toll-like receptor signalling in the intestinal epithelium: how bacterial recognition shapes intestinal function. Nat Rev Immunol (2010 ) 10(2):131–44

    Not in our library10.1038/nri2707

  88. 88.
  89. 89.

    Gay NJ Symmons MF Gangloff M Bryant CE. Assembly and localization of toll-like receptor signalling complexes. Nat Rev Immunol (2014 ) 14(8):546–58

    Not in our library10.1038/nri3713

  90. 90.

    Arumugam M Raes J Pelletier E Le Paslier D Yamada T Mende DR. Enterotypes of the human gut microbiome. Nature (2011 ) 473(7346):174–80

    Not in our library10.1038/nature09944

  91. 91.

    Thakur BK Dasgupta N Ta A Das S. Physiological Tlr5 expression in the intestine is regulated by differential DNA binding of Sp1/Sp3 through simultaneous Sp1 dephosphorylation and Sp3 phosphorylation by two different pkc isoforms. Nucleic Acids Res (2016 ) 44(12):5658–72

    Not in our library10.1093/nar/gkw189

  92. 92.

    Ruan G Chen M Chen L Xu F Xiao Z Yi A. Roseburia intestinalis and its metabolite butyrate inhibit colitis and upregulate Tlr5 through the Sp3 signaling pathway. Nutrients (2022 ) 14(15):3041

    Not in our library10.3390/nu14153041

  93. 93.

    Ganeshan K Nikkanen J Man K Leong YA Sogawa Y Maschek JA. Energetic trade-offs and hypometabolic states promote disease tolerance. Cell (2019 ) 177(2):399–413.e12

    Not in our library10.1016/j.cell.2019.01.050

  94. 94.

    Xiao T Wu S Yan C Zhao C Jin H Yan N. Butyrate upregulates the Tlr4 expression and the phosphorylation of mapks and nk-κb in colon cancer cell in vitro. Oncol Lett (2018 ) 16(4):4439–47

    Not in our library10.3892/ol.2018.9201

  95. 95.

    Coffelt SB Wellenstein MD de Visser KE. Neutrophils in cancer: neutral no more. Nat Rev Cancer (2016 ) 16(7):431–46

    Not in our library10.1038/nrc.2016.52

  96. 96.

    Vinolo MA Rodrigues HG Hatanaka E Hebeda CB Farsky SH Curi R. Short-chain fatty acids stimulate the migration of neutrophils to inflammatory sites. Clin Sci (London England: 1979) (2009 ) 117(9):331–8

    Not in our library10.1042/cs20080642

  97. 97.

    Le Poul E Loison C Struyf S Springael JY Lannoy V Decobecq ME. Functional characterization of human receptors for short chain fatty acids and their role in polymorphonuclear cell activation. J Biol Chem (2003 ) 278(28):25481–9

    Not in our library10.1074/jbc.m301403200

  98. 98.

    Vieira AT Macia L Galvão I Martins FS Canesso MC Amaral FA. A role for gut microbiota and the metabolite-sensing receptor Gpr43 in a murine model of gout. Arthritis Rheumatol (Hoboken NJ) (2015 ) 67(6):1646–56

    Not in our library10.1002/art.39107

  99. 99.
  100. 100.
  101. 101.
  102. 102.

    Chang PV Hao L Offermanns S Medzhitov R. The microbial metabolite butyrate regulates intestinal macrophage function Via histone deacetylase inhibition. Proc Natl Acad Sci United States America (2014 ) 111(6):2247–52

    Not in our library10.1073/pnas.1322269111

  103. 103.
  104. 104.

    Flemming A. Butyrate boosts microbicidal macrophages. Nat Rev Immunol (2019 ) 19(3):135

    Not in our library10.1038/s41577-019-0132-9

  105. 105.

    Lobel L Garrett WS. Butyrate makes macrophages “Go nuclear” against bacterial pathogens. Immunity (2019 ) 50(2):275–8

    Not in our library10.1016/j.immuni.2019.01.015

  106. 106.

    Inoki K Zhu T Guan KL. Tsc2 mediates cellular energy response to control cell growth and survival. Cell (2003 ) 115(5):577–90

    Not in our library10.1016/s0092-8674(03)00929-2

  107. 107.

    Zhao C Bao L Zhao Y Wu K Qiu M Feng L. A fiber-enriched diet alleviates staphylococcus aureus-induced mastitis by activating the Hdac3-mediated antimicrobial program in macrophages Via butyrate production in mice. PloS Pathog (2023 ) 19(1):e1011108

    Not in our library10.1371/journal.ppat.1011108

  108. 108.

    Huang C Du W Ni Y Lan G Shi G. The effect of short-chain fatty acids on M2 macrophages polarization in vitro and in vivo. Clin Exp Immunol (2022 ) 207(1):53–64

    Not in our library10.1093/cei/uxab028

  109. 109.

    Herberman RB Nunn ME Holden HT Lavrin DH. Natural cytotoxic reactivity of mouse lymphoid cells against syngeneic and allogeneic tumors. ii. characterization of effector cells. Int J Cancer (1975 ) 16(2):230–9

    Not in our library10.1002/ijc.2910160205

  110. 110.

    Kiessling R Klein E Wigzell H. Natural” killer cells in the mouse. i. cytotoxic cells with specificity for mouse moloney leukemia cells. specificity and distribution according to genotype. Eur J Immunol (1975 ) 5(2):112–7

    Not in our library10.1002/eji.1830050208

  111. 111.

    Zaiatz-Bittencourt V Finlay DK Gardiner CM. Canonical tgf-β signaling pathway represses human nk cell metabolism. J Immunol (Baltimore Md: 1950) (2018 ) 200(12):3934–41

    Not in our library10.4049/jimmunol.1701461

  112. 112.

    Zaiatz-Bittencourt V Jones F Tosetto M Scaife C Cagney G Jones E. Butyrate limits human natural killer cell effector function. Sci Rep (2023 ) 13(1):2715

    Not in our library10.1038/s41598-023-29731-5

  113. 113.

    Cribbs AP Filippakopoulos P Philpott M Wells G Penn H Oerum H. Dissecting the role of bet bromodomain proteins Brd2 and Brd4 in human nk cell function. Front Immunol (2021 ) 12:626255

    Not in our library10.3389/fimmu.2021.626255

  114. 114.

    Keating SE Zaiatz-Bittencourt V Loftus RM Keane C Brennan K Finlay DK. Metabolic reprogramming supports ifn-Γ production by Cd56bright nk cells. J Immunol (Baltimore Md: 1950) (2016 ) 196(6):2552–60

    Not in our library10.4049/jimmunol.1501783

  115. 115.
  116. 116.

    Bianchi T Gasser S Trumpp A MacDonald HR. C-myc acts downstream of il-15 in the regulation of memory Cd8 T-cell homeostasis. Blood (2006 ) 107(10):3992–9

    Not in our library10.1182/blood-2005-09-3851

  117. 117.

    Acharya KR Ackerman SJ. Eosinophil granule proteins: form and function. J Biol Chem (2014 ) 289(25):17406–15

    Not in our library10.1074/jbc.r113.546218

  118. 118.

    Miyata J Fukunaga K Kawashima Y Ohara O Arita M. Cysteinyl leukotriene metabolism of human eosinophils in allergic disease. Allergology Int (2020 ) 69(1):28–34

    Not in our library10.1016/j.alit.2019.06.002

  119. 119.

    Tani Y Isobe Y Imoto Y Segi-Nishida E Sugimoto Y Arai H. Eosinophils control the resolution of inflammation and draining lymph node hypertrophy through the proresolving mediators and Cxcl13 pathway in mice. FASEB J (2014 ) 28(9):4036–43

    Not in our library10.1096/fj.14-251132

  120. 120.

    Miyata J Fukunaga K Iwamoto R Isobe Y Niimi K Takamiya R. Dysregulated synthesis of protectin D1 in eosinophils from patients with severe asthma. J Allergy Clin Immunol (2013 ) 131(2):353–60.e1-2

    Not in our library10.1016/j.jaci.2012.07.048

  121. 121.

    Lacy P Abdel-Latif D Steward M Musat-Marcu S Man SF Moqbel R. Divergence of mechanisms regulating respiratory burst in blood and sputum eosinophils and neutrophils from atopic subjects. J Immunol (Baltimore Md: 1950) (2003 ) 170(5):2670–9

    Not in our library10.4049/jimmunol.170.5.2670

  122. 122.

    Cait A Hughes MR Antignano F Cait J Dimitriu PA Maas KR. Microbiome-driven allergic lung inflammation is ameliorated by short-chain fatty acids. Mucosal Immunol (2018 ) 11(3):785–95

    Not in our library10.1038/mi.2017.75

  123. 123.

    Zhang Z Shi L Pang W Liu W Li J Wang H. Dietary fiber intake regulates intestinal microflora and inhibits ovalbumin-induced allergic airway inflammation in a mouse model. PloS One (2016 ) 11(2):e0147778

    Not in our library10.1371/journal.pone.0147778

  124. 124.

    Zhang Z Shi L Pang W Wang X Li J Wang H. Is a high-fiber diet able to influence ovalbumin-induced allergic airway inflammation in a mouse model? Allergy rhinology (Providence RI) (2016 ) 7(4):213–22

    Not in our library10.2500/ar.2016.7.0186

  125. 125.

    Thio CL Chi PY Lai AC Chang YJ. Regulation of type 2 innate lymphoid cell-dependent airway hyperreactivity by butyrate. J Allergy Clin Immunol (2018 ) 142(6):1867–83.e12

    Not in our library10.1016/j.jaci.2018.02.032

  126. 126.

    Sturm EM Knuplez E Marsche G. Role of short chain fatty acids and apolipoproteins in the regulation of eosinophilia-associated diseases. Int J Mol Sci (2021 ) 22(9):4377

    Not in our library10.3390/ijms22094377

  127. 127.

    Berthon BS Macdonald-Wicks LK Gibson PG Wood LG. Investigation of the association between dietary intake, disease severity and airway inflammation in asthma. Respirology (Carlton Vic) (2013 ) 18(3):447–54

    Not in our library10.1111/resp.12015

  128. 128.

    Theiler A Bärnthaler T Platzer W Richtig G Peinhaupt M Rittchen S. Butyrate ameliorates allergic airway inflammation by limiting eosinophil trafficking and survival. J Allergy Clin Immunol (2019 ) 144(3):764–76

    Not in our library10.1016/j.jaci.2019.05.002

  129. 129.

    Barshishat M Levi I Benharroch D Schwartz B. Butyrate down-regulates Cd44 transcription and liver colonisation in a highly metastatic human colon carcinoma cell line. Br J Cancer (2002 ) 87(11):1314–20

    Not in our library10.1038/sj.bjc.6600574

  130. 130.

    Shi Y Xu M Pan S Gao S Ren J Bai R. Induction of the apoptosis, degranulation and il-13 production of human basophils by butyrate and propionate Via suppression of histone deacetylation. Immunology (2021 ) 164(2):292–304

    Not in our library10.1111/imm.13370

  131. 131.

    Yoshimura C Yamaguchi M Iikura M Izumi S Kudo K Nagase H. Activation markers of human basophils: Cd69 expression is strongly and preferentially induced by il-3. J Allergy Clin Immunol (2002 ) 109(5):817–23

    Not in our library10.1067/mai.2002.123532

  132. 132.

    Min B Prout M Hu-Li J Zhu J Jankovic D Morgan ES. Basophils produce il-4 and accumulate in tissues after infection with a Th2-inducing parasite. J Exp Med (2004 ) 200(4):507–17

    Not in our library10.1084/jem.20040590

  133. 133.

    Brunner T Heusser CH Dahinden CA. Human peripheral blood basophils primed by interleukin 3 (Il-3) produce il-4 in response to immunoglobulin e receptor stimulation. J Exp Med (1993 ) 177(3):605–11

    Not in our library10.1084/jem.177.3.605

  134. 134.

    Kurimoto Y De Weck AL Dahinden CA. The effect of interleukin 3 upon ige-dependent and ige-independent basophil degranulation and leukotriene generation. Eur J Immunol (1991 ) 21(2):361–8

    Not in our library10.1002/eji.1830210217

  135. 135.

    Vivier E Artis D Colonna M Diefenbach A Di Santo JP Eberl G. Innate lymphoid cells: 10 years on. Cell (2018 ) 174(5):1054–66

    Not in our library10.1016/j.cell.2018.07.017

  136. 136.

    Mortha A Chudnovskiy A Hashimoto D Bogunovic M Spencer SP Belkaid Y. Microbiota-dependent crosstalk between macrophages and Ilc3 promotes intestinal homeostasis. Sci (New York NY) (2014 ) 343(6178):1249288

    Not in our library10.1126/science.1249288

  137. 137.

    Zelante T Iannitti RG Cunha C De Luca A Giovannini G Pieraccini G. Tryptophan catabolites from microbiota engage aryl hydrocarbon receptor and balance mucosal reactivity Via interleukin-22. Immunity (2013 ) 39(2):372–85

    Not in our library10.1016/j.immuni.2013.08.003

  138. 138.

    Sepahi A Liu Q Friesen L Kim CH. Dietary fiber metabolites regulate innate lymphoid cell responses. Mucosal Immunol (2021 ) 14(2):317–30

    Not in our library10.1038/s41385-020-0312-8

  139. 139.

    Serafini N Jarade A Surace L Goncalves P Sismeiro O Varet H. Trained Ilc3 responses promote intestinal defense. Sci (New York NY) (2022 ) 375(6583):859–63

    Not in our library10.1126/science.aaz8777

  140. 140.

    Chun E Lavoie S Fonseca-Pereira D Bae S Michaud M Hoveyda HR. Metabolite-sensing receptor Ffar2 regulates colonic group 3 innate lymphoid cells and gut immunity. Immunity (2019 ) 51(5):871–84.e6

    Not in our library10.1016/j.immuni.2019.09.014

  141. 141.

    Fachi JL Sécca C Rodrigues PB Mato FCP Di Luccia B Felipe JS. Acetate coordinates neutrophil and Ilc3 responses against c. difficile through Ffar2. J Exp Med (2020 ) 217(3):jem.20190489

    Not in our library10.1084/jem.20190489

  142. 142.

    Durant L Watford WT Ramos HL Laurence A Vahedi G Wei L. Diverse targets of the transcription factor Stat3 contribute to T cell pathogenicity and homeostasis. Immunity (2010 ) 32(5):605–15

    Not in our library10.1016/j.immuni.2010.05.003

  143. 143.

    Jung JE Lee HG Cho IH Chung DH Yoon SH Yang YM. Stat3 is a potential modulator of hif-1-Mediated vegf expression in human renal carcinoma cells. FASEB J (2005 ) 19(10):1296–8

    Not in our library10.1096/fj.04-3099fje

  144. 144.
  145. 145.

    Smith PM Howitt MR Panikov N Michaud M Gallini CA Bohlooly YM. The microbial metabolites, short-chain fatty acids, regulate colonic treg cell homeostasis. Sci (New York NY) (2013 ) 341(6145):569–73

    Not in our library10.1126/science.1241165

  146. 146.

    Barbi J Pardoll D Pan F. Treg functional stability and its responsiveness to the microenvironment. Immunol Rev (2014 ) 259(1):115–39

    Not in our library10.1111/imr.12172

  147. 147.

    Furusawa Y Obata Y Fukuda S Endo TA Nakato G Takahashi D. Commensal microbe-derived butyrate induces the differentiation of colonic regulatory T cells. Nature (2013 ) 504(7480):446–50

    Not in our library10.1038/nature12721

  148. 148.
  149. 149.

    Park J Kim M Kang SG Jannasch AH Cooper B Patterson J. Short-chain fatty acids induce both effector and regulatory T cells by suppression of histone deacetylases and regulation of the mtor-S6k pathway. Mucosal Immunol (2015 ) 8(1):80–93

    Not in our library10.1038/mi.2014.44

  150. 150.

    Fenton TR Gwalter J Ericsson J Gout IT. Histone acetyltransferases interact with and acetylate P70 ribosomal S6 kinases in vitro and in vivo. Int J Biochem Cell Biol (2010 ) 42(2):359–66

    Not in our library10.1016/j.biocel.2009.11.022

  151. 151.

    Trompette A Gollwitzer ES Pattaroni C Lopez-Mejia IC Riva E Pernot J. Dietary fiber confers protection against flu by shaping Ly6c(-) patrolling monocyte hematopoiesis and Cd8(+) T cell metabolism. Immunity (2018 ) 48(5):992–1005.e8

    Not in our library10.1016/j.immuni.2018.04.022

  152. 152.
  153. 153.

    Bachem A Makhlouf C Binger KJ de Souza DP Tull D Hochheiser K. Microbiota-derived short-chain fatty acids promote the memory potential of antigen-activated Cd8(+) T cells. Immunity (2019 ) 51(2):285–97.e5

    Not in our library10.1016/j.immuni.2019.06.002

  154. 154.

    He Y Fu L Li Y Wang W Gong M Zhang J. Gut microbial metabolites facilitate anticancer therapy efficacy by modulating cytotoxic Cd8(+) T cell immunity. Cell Metab (2021 ) 33(5):988–1000.e7

    Not in our library10.1016/j.cmet.2021.03.002

  155. 155.

    Ersching J Efeyan A Mesin L Jacobsen JT Pasqual G Grabiner BC. Germinal center selection and affinity maturation require dynamic regulation of Mtorc1 kinase. Immunity (2017 ) 46(6):1045–58.e6

    Not in our library10.1016/j.immuni.2017.06.005

  156. 156.

    Moreau MC Ducluzeau R Guy-Grand D Muller MC. Increase in the population of duodenal immunoglobulin a plasmocytes in axenic mice associated with different living or dead bacterial strains of intestinal origin. Infection Immun (1978 ) 21(2):532–9

    Not in our library10.1128/iai.21.2.532-539.1978

  157. 157.

    Ishikawa T Nanjo F. Dietary cycloinulooligosaccharides enhance intestinal immunoglobulin a production in mice. Bioscience biotechnology Biochem (2009 ) 73(3):677–82

    Not in our library10.1271/bbb.80733

  158. 158.

    Bergman EN. Energy contributions of volatile fatty acids from the gastrointestinal tract in various species. Physiol Rev (1990 ) 70(2):567–90

    Not in our library10.1152/physrev.1990.70.2.567

  159. 159.

    Bloch K Vance D. Control mechanisms in the synthesis of saturated fatty acids. Annu Rev Biochem (1977 ) 46:263–98

    Not in our library10.1146/annurev.bi.46.070177.001403

  160. 160.

    Kunisawa J Hashimoto E Inoue A Nagasawa R Suzuki Y Ishikawa I. Regulation of intestinal iga responses by dietary palmitic acid and its metabolism. J Immunol (Baltimore Md: 1950) (2014 ) 193(4):1666–71

    Not in our library10.4049/jimmunol.1302944

  161. 161.

    Girard J Perdereau D Foufelle F Prip-Buus C Ferré P. Regulation of lipogenic enzyme gene expression by nutrients and hormones. FASEB journal: Off Publ Fed Am Societies Exp Biol (1994 ) 8(1):36–42

    Not in our library10.1096/fasebj.8.1.7905448

  162. 162.

    Muramatsu M Kinoshita K Fagarasan S Yamada S Shinkai Y Honjo T. Class switch recombination and hypermutation require activation-induced cytidine deaminase (Aid), a potential rna editing enzyme. Cell (2000 ) 102(5):553–63

    Not in our library10.1016/s0092-8674(00)00078-7

  163. 163.

    Muramatsu M Kinoshita K Fagarasan S Yamada S Shinkai Y Honjo T. Pillars article: class switch recombination and hypermutation require activation-induced cytidine deaminase (Aid), a potential rna editing enzyme. Cell (2000 ) 102:553–63.

    Not in our library10.1016/s0092-8674(00)00078-7

  164. 164.

    Aldrich MB Chen W Blackburn MR Martinez-Valdez H Datta SK Kellems RE. Impaired germinal center maturation in adenosine deaminase deficiency. J Immunol (Baltimore Md: 1950) (2003 ) 171(10):5562–70

    Not in our library10.4049/jimmunol.171.10.5562

  165. 165.

    Wu W Sun M Chen F Cao AT Liu H Zhao Y. Microbiota metabolite short-chain fatty acid acetate promotes intestinal iga response to microbiota which is mediated by Gpr43. Mucosal Immunol (2017 ) 10(4):946–56

    Not in our library10.1038/mi.2016.114

  166. 166.

    Arpaia N Campbell C Fan X Dikiy S van der Veeken J deRoos P. Metabolites produced by commensal bacteria promote peripheral regulatory T-cell generation. Nature (2013 ) 504(7480):451–5

    Not in our library10.1038/nature12726

  167. 167.

    Takeuchi T Miyauchi E Kanaya T Kato T Nakanishi Y Watanabe T. Acetate differentially regulates iga reactivity to commensal bacteria. Nature (2021 ) 595(7868):560–4

    Not in our library10.1038/s41586-021-03727-5

  168. 168.

    Daïen CI Tan J Audo R Mielle J Quek LE Krycer JR. Gut-derived acetate promotes B10 cells with antiinflammatory effects. JCI Insight (2021 ) 6(7):793

    Not in our library10.1172/jci.insight.144156

  169. 169.
  170. 170.

    Kim DS Woo JS Min HK Choi JW Moon JH Park MJ. Short-chain fatty acid butyrate induces il-10-Producing b cells by regulating circadian-Clock-Related genes to ameliorate sjögren’s syndrome. J Autoimmun (2021 ) 119:102611

    Not in our library10.1016/j.jaut.2021.102611

  171. 171.

    Kuang Z Wang Y Li Y Ye C Ruhn KA Behrendt CL. The intestinal microbiota programs diurnal rhythms in host metabolism through histone deacetylase 3. Sci (New York NY) (2019 ) 365(6460):1428–34

    Not in our library10.1126/science.aaw3134

  172. 172.
  173. 173.

    Holgate ST. The sentinel role of the airway epithelium in asthma pathogenesis. Immunol Rev (2011 ) 242(1):205–19

    Not in our library10.1111/j.1600-065x.2011.01030.x

  174. 174.

    Dunican EM Fahy JV. The role of type 2 inflammation in the pathogenesis of asthma exacerbations. Ann Am Thorac Soc (2015 ) 12 Suppl 2(Suppl 2):S144–9

    Not in our library10.1513/annalsats.201506-377aw

  175. 175.
  176. 176.

    Fulkerson PC Rothenberg ME. Targeting eosinophils in allergy, inflammation and beyond. Nat Rev Drug Discovery (2013 ) 12(2):117–29

    Not in our library10.1038/nrd3838

  177. 177.
  178. 178.

    Trompette A Gollwitzer ES Yadava K Sichelstiel AK Sprenger N Ngom-Bru C. Gut microbiota metabolism of dietary fiber influences allergic airway disease and hematopoiesis. Nat Med (2014 ) 20(2):159–66

    Not in our library10.1038/nm.3444

  179. 179.

    Eckalbar WL Erle DJ. Singling out Th2 cells in eosinophilic esophagitis. J Clin Invest (2019 ) 129(5):1830–2

    Not in our library10.1172/jci128479

  180. 180.

    Halim TY Krauss RH Sun AC Takei F. Lung natural helper cells are a critical source of Th2 cell-type cytokines in protease allergen-induced airway inflammation. Immunity (2012 ) 36(3):451–63

    Not in our library10.1016/j.immuni.2011.12.020

  181. 181.

    Gold MJ Antignano F Halim TY Hirota JA Blanchet MR Zaph C. Group 2 innate lymphoid cells facilitate sensitization to local, but not systemic, Th2-inducing allergen exposures. J Allergy Clin Immunol (2014 ) 133(4):1142–8

    Not in our library10.1016/j.jaci.2014.02.033

  182. 182.

    Toki S Goleniewska K Reiss S Zhou W Newcomb DC Bloodworth MH. The histone deacetylase inhibitor trichostatin a suppresses murine innate allergic inflammation by blocking group 2 innate lymphoid cell (Ilc2) activation. Thorax (2016 ) 71(7):633–45

    Not in our library10.1136/thoraxjnl-2015-207728

  183. 183.

    Thorburn AN McKenzie CI Shen S Stanley D Macia L Mason LJ. Evidence that asthma is a developmental origin disease influenced by maternal diet and bacterial metabolites. Nat Commun (2015 ) 6:7320

    Not in our library10.1038/ncomms8320

  184. 184.

    Folkerts J Redegeld F Folkerts G Blokhuis B van den Berg MPM de Bruijn MJW. Butyrate inhibits human mast cell activation Via epigenetic regulation of fcϵri-mediated signaling. Allergy (2020 ) 75(8):1966–78

    Not in our library10.1111/all.14254

  185. 185.
  186. 186.

    Vieira RS Castoldi A Basso PJ Hiyane MI Câmara NOS Almeida RR. Butyrate attenuates lung inflammation by negatively modulating Th9 cells. Front Immunol (2019 ) 10:67

    Not in our library10.3389/fimmu.2019.00067

  187. 187.

    Sehra S Yao W Nguyen ET Glosson-Byers NL Akhtar N Zhou B. Th9 cells are required for tissue mast cell accumulation during allergic inflammation. J Allergy Clin Immunol (2015 ) 136(2):433–40.e1

    Not in our library10.1016/j.jaci.2015.01.021

  188. 188.

    Frank DN St Amand AL Feldman RA Boedeker EC Harpaz N Pace NR. Molecular-phylogenetic characterization of microbial community imbalances in human inflammatory bowel diseases. Proc Natl Acad Sci United States America (2007 ) 104(34):13780–5

    Not in our library10.1073/pnas.0706625104

  189. 189.

    Cresci GA Thangaraju M Mellinger JD Liu K Ganapathy V. Colonic gene expression in conventional and germ-free mice with a focus on the butyrate receptor Gpr109a and the butyrate transporter Slc5a8. J gastrointestinal surgery: Off J Soc Surg Alimentary Tract (2010 ) 14(3):449–61

    Not in our library10.1007/s11605-009-1045-x

  190. 190.

    Messora MR Oliveira LF Foureaux RC Taba M Jr. Zangerônimo MG Furlaneto FA. Probiotic therapy reduces periodontal tissue destruction and improves the intestinal morphology in rats with ligature-induced periodontitis. J periodontology (2013 ) 84(12):1818–26

    Not in our library10.1902/jop.2013.120644

  191. 191.

    Li JY Chassaing B Tyagi AM Vaccaro C Luo T Adams J. Sex steroid deficiency-associated bone loss is microbiota dependent and prevented by probiotics. J Clin Invest (2016 ) 126(6):2049–63

    Not in our library10.1172/jci86062

  192. 192.
  193. 193.

    Tyagi AM Yu M Darby TM Vaccaro C Li JY Owens JA. The microbial metabolite butyrate stimulates bone formation Via T regulatory cell-mediated regulation of Wnt10b expression. Immunity (2018 ) 49(6):1116–31.e7

    Not in our library10.1016/j.immuni.2018.10.013

  194. 194.

    Kondo T Chiba T Tousen Y. Short-chain fatty acids, acetate and propionate, directly upregulate osteoblastic differentiation. Int J Food Sci Nutr (2022 ) 73(6):800–8

    Not in our library10.1080/09637486.2022.2078285

  195. 195.

    Si J Wang C Zhang D Wang B Zhou Y. Osteopontin in bone metabolism and bone diseases. Med Sci monitor: Int Med J Exp Clin Res (2020 ) 26:e919159

    Not in our library10.12659/msm.919159

  196. 196.

    Indo Y Takeshita S Ishii KA Hoshii T Aburatani H Hirao A. Metabolic regulation of osteoclast differentiation and function. J Bone mineral Res (2013 ) 28(11):2392–9

    Not in our library10.1002/jbmr.1976

  197. 197.

    Lemma S Sboarina M Porporato PE Zini N Sonveaux P Di Pompo G. Energy metabolism in osteoclast formation and activity. Int J Biochem Cell Biol (2016 ) 79:168–80

    Not in our library10.1016/j.biocel.2016.08.034

  198. 198.

    Perry RJ Peng L Barry NA Cline GW Zhang D Cardone RL. Acetate mediates a microbiome-Brain-β-Cell axis to promote metabolic syndrome. Nature (2016 ) 534(7606):213–7

    Not in our library10.1038/nature18309

  199. 199.

    Smith PA. The tantalizing links between gut microbes and the brain. Nature (2015 ) 526(7573):312–4

    Not in our library10.1038/526312a

  200. 200.

    Shirvani-Rad S Ejtahed HS Ettehad Marvasti F Taghavi M Sharifi F Arzaghi SM. The role of gut microbiota-brain axis in pathophysiology of adhd: a systematic review. J attention Disord (2022 ) 26(13):1698–710

    Not in our library10.1177/10870547211073474

  201. 201.

    Peh A O’Donnell JA Broughton BRS Marques FZ. Gut microbiota and their metabolites in stroke: a double-edged sword. Stroke (2022 ) 53(5):1788–801

    Not in our library10.1161/strokeaha.121.036800

  202. 202.

    Zhou T Wang M Ma H Li X Heianza Y Qi L. Dietary fiber, genetic variations of gut microbiota-derived short-chain fatty acids, and bone health in uk biobank. J Clin Endocrinol Metab (2021 ) 106(1):201–10

    Not in our library10.1210/clinem/dgaa740

  203. 203.

    Tao ZS Zhou WS Xu HG Yang M. Intermittent administration sodium valproate has a protective effect on bone health in ovariectomized rats. Eur J Pharmacol (2021 ) 906:174268

    Not in our library10.1016/j.ejphar.2021.174268

  204. 204.

    Wallimann A Magrath W Thompson K Moriarty T Richards RG Akdis CA. Gut microbial-derived short-chain fatty acids and bone: a potential role in fracture healing. Eur Cells materials (2021 ) 41:454–70

    Not in our library10.22203/ecm.v041a29

  205. 205.

    Abdollahi-Roodsaz S Abramson SB Scher JU. The metabolic role of the gut microbiota in health and rheumatic disease: mechanisms and interventions. Nat Rev Rheumatol (2016 ) 12(8):446–55

    Not in our library10.1038/nrrheum.2016.68

  206. 206.

    Witkowski M Weeks TL Hazen SL. Gut microbiota and cardiovascular disease. Circ Res (2020 ) 127(4):553–70

    Not in our library10.1161/circresaha.120.316242

  207. 207.

    Maslowski KM Vieira AT Ng A Kranich J Sierro F Yu D. Regulation of inflammatory responses by gut microbiota and chemoattractant receptor Gpr43. Nature (2009 ) 461(7268):1282–6

    Not in our library10.1038/nature08530

  208. 208.

    Kendrick SF O’Boyle G Mann J Zeybel M Palmer J Jones DE. Acetate, the key modulator of inflammatory responses in acute alcoholic hepatitis. Hepatol (Baltimore Md) (2010 ) 51(6):1988–97

    Not in our library10.1002/hep.23572

  209. 209.

    Kundi ZM Lee JC Pihlajamäki J Chan CB Leung KS So SSY. Dietary fiber from oat and rye brans ameliorate Western diet-induced body weight gain and hepatic inflammation by the modulation of short-chain fatty acids, bile acids, and tryptophan metabolism. Mol Nutr Food Res (2021 ) 65(1):e1900580

    Not in our library10.1002/mnfr.201900580

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