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Green Tea Extracts Epigallocatechin-3-gallate for Different Treatments

Chenyu Chu, Jia Deng, Yi Man and 1 more

BioMed Research International · 2017 · Review

doi:10.1155/2017/5615647

Abstract

Epigallocatechin-3-gallate (EGCG), a component extracted from green tea, has been proved to have multiple effects on human pathological and physiological processes, and its mechanisms are discrepant in cancer, vascularity, bone regeneration, and nervous system. Although there are multiple benefits associated with EGCG, more and more challenges are still needed to get through. For example, EGCG shows low bioactivity via oral administration. This review focuses on effects of EGCG, including anti-cancer, antioxidant, anti-inflammatory, anticollagenase, and antifibrosis effects, to express the potential of EGCG and necessity of further studies in this field.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 21, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Introduction

Green tea is one of the most popular drinks in the area of China and Japan, whose main chemical components are tea polyphenols (30% dry weight). Polyphenols share various therapeutic effects against pathological conditions including cancer, inflammation, diabetes, and cardiovascular diseases. Recently, scientific interest in polyphenols has been rapidly increased. Tea polyphenols in green tea possess lots of catechins including catechin, epicatechin (EC), epicatechin-3-gallate (ECG), epigallocatechin (EGC), and epigallocatechin-3-gallate (EGCG). Among these components, EGCG is the most abundant tea polyphenol. Moreover, it is reported that the galloyl moiety of tea catechins plays crucial roles in benefits of tea catechins, especially in lipid lowering effect. Compared to other tea catechins, galloyl moiety of catechins (EGCG and ECG) possesses the most biological activities including angiogenesis. Peoples believe that drinking green tea is beneficial to health and it has been demonstrated that EGCG is with inhibitory effects in many aspects of abnormal changes, such as antioxidant, anticancer, anti-inflammatory, anticollagenase, and antifibrosis effects, appearing in its wide functional range (Figure 1). It can be speculated that EGCG, to some extent, has the effect of protecting organs or tissues from a pile of diseases. Moreover, EGCG has promotional effect on osteogenesis. Although the researches concerning EGCG are still on the road accompanied with quite a few controversies, EGCG is more likely to be beneficial to health.

2.1. Anticancer Effect

For all the time, the anticancer property of EGCG is the focal point of researches. On one hand, EGCG can inhibit tumorigenesis by inhibiting carcinogen activity. There are findings suggesting that EGCG prevents diethylnitrosamine-induced obesity-related liver tumorigenesis by inhibiting the IGF/IGF-1R axis, improving hyperinsulinemia, and attenuating chronic inflammation. On the other hand, it can restrain tumor proliferation by acting against angiogenesis. Shankar et al. found that EGCG inhibits pancreatic cancer orthotopic tumor growth, angiogenesis, and metastasis that are associated with inhibition of PI3K/AKT and ERK pathways and activation of FKHRL1/FOXO3a. Moreover, it can inhibit tumor migration and penetration and induce tumor cell death via several mechanisms including caspase-dependent apoptosis, caspase-independent apoptosis, lysosomal membrane permeabilization-mediated cell death, and autophagy. It is widely accepted that hepatocyte growth factor (HGF) is involved in tumor migration and invasion, and EGCG has the capacity to suppress its activity. In fact, most of the anticancer effects of EGCG play a role via several signal transduction pathways including JAK/STAT, MAPK, PI3K/AKT, Wnt, and Notch. From the above, it can be easily found that the mechanism of anticancer effect of EGCG is considerably multiple and complicated.

What may be concerned is if this antigrowth effect is also found in normal cells. Park et al. examined the discrepancy of EGCG effects to normal rat osteoblasts (NRO) and human osteosarcoma (MG-63 and Saos-2). It turned out that after EGCG treatment of micromolar concentrations, the growth and alkaline phosphatase activity of both osteosarcoma cells are inhibited with morphological alterations and G0/G1-phase arrest of the cell cycle, while the NRO is not affected basically. The internal mechanism of the different effects EGCG has on both types of cells remains to be illuminated.

2.2. Antioxidant Effect

Antioxidation is a process of vital importance to the health of human body. On the basis of the chemical structure of EGCG, we sort it into antioxidant. The phenol rings in EGCG structure act as electron traps and scavengers of free radicals, inhibit the formation of reactive oxygen species, and reduce the harm caused by oxidative stress. It is reported that EGCG can effectively inhibit oxidative stress-induced protein tyrosine nitration induced by oxidative stress in blood platelet, and as an antioxidant it can improve the function of mitochondria. However, there are some studies pointing out that EGCG of high concentration can cause self-oxidization and function as the prooxidant by producing hydroxyl radicals, hydrogen peroxide, and quinonoid intermediates causing cytotoxicity. For example, Chen et al. found that the catechol-quinone produced by self-oxidation of EGCG and EGC can cross-link with erythrocyte membrane proteins as a cross-linking agent, thus leading to the membrane protein aggregates; herein a galloyl moiety is the essential group of catechins to have the prooxidative effect. Meanwhile in factual physiological concentration (1-2 μM up to 10 μM), EGCG can produce small quantities of reactive oxygen species to activate several signal pathways and then arouse corresponding cellular protective mechanism, thus mainly presenting its antioxidant effects. The complicated biological effects of EGCG may be linked to its products of the metabolism.

2.3. Anti-Inflammatory Effect

Features of inflammatory response are the symptoms of a large number of immune cell aggregation at the inflammatory sites, release of proinflammatory cytokines, and reactive oxygen/nitrogen (ROS/RNS). ROS/RNS are relative to the activation of transcription factor NF-κB and activator protein- (AP-) 1. After activation, NF-jB and AP-1 will transfer from the cytoplasm to the nucleus and upregulate a variety of inflammatory gene expressions, which will give rise to the exacerbated inflammatory response and tissue injury. The anti-inflammatory mechanism is intimate to the process of signal transduction.

EGCG inhibits the transfection of NF-κB and AP-1 to downregulate the expression of iNOS and COX-2 mainly by scavenging NO, peroxynitrite, and other ROS/RNS and decreases the production of inflammatory factors to show the anti-inflammatory effects. IL-8 can stimulate neutrophil aggregation and promote the activation of reactive oxygen species, and it has been pointed out that EGCG could inhibit the IL-8 production of respiratory passage epithelium cell, thereby reducing the severity of respiratory passage inflammatory response. In addition, Tang et al. argued that EGCG downregulates the expression of proinflammatory genes mediated by P2X4 receptor by blocking the JAK1/2 tyrosine kinase signaling pathway in vascular endothelial cells. EGCG plays a crucial role in the regulation of the relative gene expression and transcription, which can account for its anti-inflammatory property.

2.4. Anticollagenase Effect

Collagen is a paramount component of the extracellular matrix and of biological characteristics including biodegradability and biocompatibility, which have been widely studied in quite many fields. Specific three-helix structure of collagen and stability of collagen structure are closely related to its biological functions. And collagenase can specifically hydrolyze three-dimensional helix structure collagen, destroying its stability, thus affecting its biological function. EGCG-treated collagen can effectively resist the degradation of collagenase and maintain three-helix structure in the 37°C. However, mechanisms explaining that EGCG can stabilize the collagen and resist collagenase are still in a controversy. Madhan et al. found that, after EGCG treatment, 95% collagen can resist the degradation of collagenase. They harbor the idea that hydrogen bonding between EGCG and collagenase and hydrophobic interaction inhibit the activity of collagenase, and they observed second structure change of collagenase with round two dichroism spectropolarimeter. But Jackson et al. indicate that EGCG closed collagenase-active site of collagen by being closely conjugated with collagen, which was examined by high performance liquid chromatography and thus resist hydrolysis of collagenase. Therefore, there is a great need of further experiment to explore the intrinsic mechanism explaining that the EGCG can stabilize the collagen structure and resist collagenase degradation.

2.5. Antifibrosis Effect

EGCG plays the role of antifibrosis mainly by blocking the transfer of NF-κB from the cytoplasm to the nucleus to downregulate the expression of certain genes. Hepatic fibrosis is a severe complication of chronic liver diseases, which can eventually lead to cirrhosis and even liver failure and liver cancer. Hepatic stellate cells are the major sources of extracellular matrix in chronic liver disease, which will be of excessive proliferation and excessive secretion of extracellular matrix during the development of hepatic fibrosis, thus aggravating the liver fibrosis. It is reported that EGCG can inhibit the activation and proliferation of hepatic stellate cells and synthesis of collagen, in a rat model. PDGF and IGF play essential roles in the process of liver fibrosis, as EGCG can inhibit the expression of PDGFR and IGF-1R mRNAs, thereby reducing liver fibrosis. In addition, increased expression and activity of MMP-2 are one of the main causes of liver fibrosis, while EGCG can reduce its activity and possess the antifibrosis effect via downregulation of the expression of MMP-2 mRNA. Myocardial fibrosis is mainly due to the increased CTGF in the heart, the promotion of myocardial fibroblast cell proliferation, and excessive secretion of extracellular matrix. Some research shows that, in rat cardiac fibroblasts after AngII stimulation, EGCG could significantly reduce the synthesis of collagen and fibronectin expression and inhibit the cell proliferation. The internal mechanism is that EGCG, by preventing NF-κB transfer to the nucleus and downregulating CTGF gene expression, achieves the effect of antifibrosis. Additionally, the long-term peritoneal dialysis can lead to peritoneal histological aberrance, causing the formation of peritoneal fibrosis. It has been demonstrated that EGCG can also inhibit the NF-κB to reverse the peritoneal fibrosis process. From the information presented above, it can be found that both intracellular reactions and extracellular components can be the aiming targets of EGCG, thus realizing its multiple mechanisms of inhibiting the abnormal changes of the body. Now that the inhibitory effects have been studied, it has promotional influences aiming to make contribution to the health as well.

2.6. Osteogenesis Promotion

Osteoporosis is a severe disease characterized by a decrease in bone density and a degeneration in bone fibrous. Epidemiological studies in several countries have found that when more green tea is consumed, the risk of osteoporosis will be lower. Studies have also proved that, EGCG and bone metabolism are closely linked. It can induce the apoptosis of osteoclasts and inhibit the formation of osteoclasts by blocking the generation of NF-κB and IL-1b, can also reduce bone absorption by inhibiting osteoclast formation, and promote the formation of mineralized bone nodules. The treatment of osteoporosis based on mesenchymal stem cell has captured increasing attention. Bone marrow-derived mesenchymal stem cells possess the ability of self-renewal and differentiation and are considered as ideal cell sources of the treatment of osteoporosis in this way. Jin et al. studied the osteogenic effect of EGCG on hBMSCs by examining cell proliferation, ALP activity, and the expression of related osteogenic markers. The result manifested that EGCG at concentrations of 5 μM significantly promoted the differentiation of hBMSCs into bone cells. It provides the basis for the clinical application of EGCG to rescue osteoporosis by stem cells. Moreover, not only the therapy of stem cells but biomaterials have potential to repair osteoporosis; for example, TCP is one of the ideal scaffolds for bone remodeling. It is bioactive and biodegradable and is capable of space maintaining to improve osteogenesis. Animal experiments indicate that a-TCP combining EGCG can significantly stimulate the bone regeneration in skull defects of rats, which means the combination of a-TCP and EGCG may be a material having potential to promote bone regeneration. From the above, it can be concluded that EGCG is a promising drug in the treatments or precautions. The properties of EGCG especially the antioxidant and anti-inflammatory ones can present these functions, found during some researches in specific tissues. For specific situations and perhaps the comprehension of several effects mentioned above, we discuss these functions in the next part.

2.7. Autoxidation

It is reported that tea polyphenols can be oxidized by superoxide anion (O2∙−) radicals, which influence the stability. EGCG is not stable and can be oxidized on both the B and the D ring. The main oxidation site of EGCG during autoxidation is the B ring, but the preferred site for O2∙− oxidation followed by structural degradation is the D ring. The autoxidation of EGCG further leads to the formation of reactive oxygen species, which are involved in the biological activities such as telomerase inhibition. A mechanism for the autoxidation of EGCG was based on the formation of EGCG quinone, EGCG dimer quinone, and other related compounds. For example, EGCG can inhibit the angiotensin-converting enzyme (ACE) activity through oxidation into an electrophilic quinone, which may be related to the treatment of cardiovascular diseases. Moreover, the formation of autoxidized products also contributes to the inhibition of fibrillation. In addition, EGCG are found to form covalent adducts with cysteinyl thiol residues in proteins through autoxidation to subsequently modulate protein function, which can be applied to treat human gastric cancer. The stability and autoxidation of EGCG are also associated with several factors including pH, temperature, metal ion, antioxidant levels, oxygen levels, concentration of EGCG, and other ingredients in tea. It is reported that EGCG is more prone to undergo autoxidation at alkaline pH, and the instability is related to their electrophilic reactivity.

3.1. Cancer Treatment

Although the anticancer effect of EGCG in vitro is obvious and aimed at cancerous cells, its effect in vivo and the application in clinical treatment are restricted by several factors. On one hand, the anticancer property of EGCG depends on its high dose, while in normal life the intake quantity of EGCG of our drinking green tea is intensely small and the bioavailability in vivo is low as well. On the other hand, notwithstanding the fact that more and more studies are indicative that EGCG as traditional adjuvant in cancer therapy can reduce the deleterious side effects and get addictive or synergistic effects, EGCG can also cut down the effects of drugs at some extent which limits its clinical application. Therefore, more profound researches are still required in the application of EGCG into clinic.

3.2. Oral Disease Treatment

The application of EGCG in the field of oral treatment mainly utilizes its anti-inflammatory effect and inhibiting bone absorption ability. One of the well-known reasons for tooth extraction is pulpal necrosis from bacterial infection, which may induce an inflammatory response and bone resorption at the periapical area of the tooth. Hong et al. studied the healing process of extraction socket with the transplantation of collagenated bovine bone mineral (CBBM) soaked with EGCG, under the condition of injury of the dental periapical of dogs. A research indicated that after the treatment of EGCG, reduced inflammatory response and reduced alveolar bone absorption were observed. Similarly as the dog as the experimental object, Shin et al. found that the experimental group with EGCG is more beneficial to dehiscence defect healing with increased bone remodeling. Additionally, Cho et al. demonstrated that oral administrated EGCG also possesses therapeutic effects on periodontitis triggered by ligation through in vivo experiments.

Moreover, EGCG cross-linked collagen membranes have potentials in guided bone regeneration (GBR). GBR is an effective procedure to augment deficient volume of alveolar bone for success of dental implant surgeries, where collagen membranes are usually used. To improve the mechanical properties of pure collagen membranes, cross-linking agents are widely used. EGCG can be a potential cross-linking agent for collagen membranes due to its anticollagenase effect. Therefore, some studies have also focused on the EGCG-modified collagen membranes. Chu et al. fabricated a novel EGCG-modified collagen membrane with desirable mechanical properties and improved cell adhesion of osteoblasts. However, collagen membranes with the highest concentration of EGCG did not exhibit satisfactory result of cell viability. Previous studies have loaded growth factors on collagen membranes to improve the outcome of GBR, and polyethylene glycol (PEG) can be used to improve biocompatibility and decrease cytotoxicity of the added growth factors or drugs. Therefore, PEG was also added onto the EGCG-modified collagen membranes and the results proved that EGCG-modified collagen membranes with PEG modification possessed better biocompatibility and improved cell viability of osteoblasts than those without PEG. To further improve the outcome of bone regeneration, nanosized hydroxylapatite (nano-HA) can also be loaded onto EGCG-modified collagen membranes, which obtained favorable new bone regeneration. However, the results showed that nano-HA-collagen membranes group exhibited less bone regenerative ability than the control group. It is supposed that the imbalance of FBR elicited by implantation of collagen membranes may lead to the loss of bone. Moreover, the new generation of GBR membranes not only should serve as barrier membranes, but also are capable of modulating FBR for bone regeneration after implantation. EGCG-modified collagen membranes can also downregulate the secretion of inflammatory factors. Therefore, EGCG-modified collagen membranes also have great potentials to be immune modulating materials. Further studies on EGCG-modified collagen membranes are still needed.

3.3. Nervous System Protection

Neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), and Huntington's disease (HD), are led by protein misfolding resulting from amyloid protein which is a fibrous polymer rich in β sheets, formed by the self-assembly of proteins of different sequences, structures, and functions. EGCG could conjugate directly with natural peptides not folded to inhibit the formation of toxic intermediate products of α-synaptic nucleoprotein and amyloid protein β and form a nontoxic and disordered oligomer of these two proteins, so as to exert protective effects on nerves. In addition, protein aggregation is generally related to the reduced endogenous antioxidants, inflammation and increased iron ions, NO levels, and other related factors. The presence of ROS and RNS will intensify protein misfolding. Experimental studies have emphasized that EGCG could serve as an antioxidant and inhibit the transformation of nitrate and peroxynitrite into NO, thus decreasing ischemic neuronal damage and protecting nerve. Besides the effect on neurodegenerative diseases, EGCG is shown to inhibit the microglia mediated inflammatory response and reduce the damage of the central nervous system triggered by infrasound. In addition, EGCG can promote the healing of extrusion-damaged sciatic nerve, which may be accomplished by changing the expression of the gene controlling apoptosis.

3.4. Vascular System Protection

Endothelial cells play crucial roles in some physiological processes, including the regulation of vascular tension, coagulation, and permeability. Endothelial cells dysfunction is an essential initial cause of the occurrence of cardiovascular diseases like atherosclerosis. EGCG protects the cardiovascular system and resists all kinds of cardiovascular diseases via its antioxidant and anti-inflammatory function. When atherosclerosis occurs, it accompanies the activation of endothelial cells, the increase of some cytokines, and the expression of adhesion molecule. Ludwig et al. found that EGCG can downregulate vascular cell adhesion protein-1 (VCAM-1) in human umbilical vein endothelial cell, while VCAM-1 plays an important role in atherosclerosis. Perfusion is after myocardial infarct; taking EGCG can reduce neutrophil aggregation and the release of IL-6 and TNF-α in order to minimize the endothelial injury induced by ROS. Lorenz et al. found that, after taking green tea, endothelial cells were activated by posttranscriptional regulation (eNOS), resulting in the aortic diastole of rat. The aiming object of EGCG is not limited to endothelial cells. The study found that the proliferation and migration of vascular smooth muscle cell could be inhibited by EGCG, which can induce cell cycle arrest. Cho et al. observed the effect of the scaffold with EGCG on vascular smooth muscle cells and platelets and they found that the scaffold with sustained release of EGCG could inhibit the migration, invasion, and adhesion of VSMCs and activation of platelet. It means that the polymers releasing EGCG can be used to fabricate the EGCG scaffolds and thus prevent vascular restenosis and thrombosis after stent implantation. Although the protective effects of EGCG on the cardiovascular system are proved in numerous experiments, how to apply the EGCG to the corresponding position is still a challenge.

4. Future Perspectives

EGCG shows various effects in different cell types in vitro and vivo. Notwithstanding the fact that the properties of the EGCG have been gradually clarified, there still exist quite a few controversies, for example, mechanism of EGCG in collagen stabilization. For the aspect of application, EGCG combined with other drugs for anticancer treatment can possess a synergistic and protective effect. Moreover, EGCG-collagen membranes have great potentials in GBR surgeries. However, EGCG still encounters lots of challenges for clinical application. Oral administration or venous injection of EGCG has low bioavailability, and effects are easily influenced by concentration, derivatives, and other factors. It still needs solutions as to how to deliver EGCG effectively to target sites and protect anticancer drugs from degradation.

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    Goo H. C., Hwang Y.-S., Choi Y. R., Cho H. N., Suh H. Development of collagenase-resistant collagen and its interaction with adult human dermal fibroblasts. Biomaterials. 2003;24(28):5099-5113.

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    Madhan B., Krishnamoorthy G., Rao J. R., Nair B. U. Role of green tea polyphenols in the inhibition of collagenolytic activity by collagenase. International Journal of Biological Macromolecules. 2007;41(1):16-22.

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    Jackson J. K., Zhao J., Wong W., Burt H. M. The inhibition of collagenase induced degradation of collagen by the galloyl-containing polyphenols tannic acid, epigallocatechin gallate and epicatechin gallate. Journal of Materials Science: Materials in Medicine. 2010;21(5):1435-1443.

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    Fattovich G., Stroffolini T., Zagni I., Donato F. Hepatocellular carcinoma in cirrhosis: incidence and risk factors. Gastroenterology. 2004;127(supplement 1):S35-S50.

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  46. 46.

    Friedman S. L., Bansal M. B. Reversal of hepatic fibrosis—fact or fantasy? Hepatology. 2006;43(2, supplement 1):S82-S88.

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    Friedman S. L. Molecular mechanisms of hepatic fibrosis and principles of therapy. Journal of Gastroenterology. 1997;32(3):424-430.

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    Friedman S. L. Cytokines and fibrogenesis. Seminars in Liver Disease. 1999;19(2):129-140.

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    Nakamuta M., Higashi N., Kohjima M., et al. Epigallocatechin-3-gallate, a polyphenol component of green tea, suppresses both collagen production and collagenase activity in hepatic stellate cells. International Journal of Molecular Medicine. 2005;16(4):677-681.

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    Higashi N., Kohjima M., Fukushima M., et al. Epigallocatechin-3-gallate, a green-tea polyphenol, suppresses Rho signaling in TWNT-4 human hepatic stellate cells. Journal of Laboratory and Clinical Medicine. 2005;145(6):316-322.

    Not in our library10.1016/j.lab.2005.03.017

  51. 51.

    Sakata R., Ueno T., Nakamura T., Sakamoto M., Torimura T., Sata M. Green tea polyphenol epigallocatechin-3-gallate inhibits platelet-derived growth factor-induced proliferation of human hepatic stellate cell line LI90. Journal of Hepatology. 2004;40(1):52-59.

    Not in our library10.1016/s0168-8278(03)00477-x

  52. 52.

    Yasuda Y., Shimizu M., Sakai H., et al. (−)-Epigallocatechin gallate prevents carbon tetrachloride-induced rat hepatic fibrosis by inhibiting the expression of the PDGFRβ and IGF-1R. Chemico-Biological Interactions. 2009;182(2-3):159-164.

    Not in our library10.1016/j.cbi.2009.07.015

  53. 53.

    Zhen M.-C., Wang Q., Huang X.-H., et al. Green tea polyphenol epigallocatechin-3-gallate inhibits oxidative damage and preventive effects on carbon tetrachloride-induced hepatic fibrosis. Journal of Nutritional Biochemistry. 2007;18(12):795-805.

    Not in our library10.1016/j.jnutbio.2006.12.016

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    Weber K. T., Sun Y., Tyagi S. C., Cleutjens J. P. M. Collagen network of the myocardium: Function, structural remodeling and regulatory mechanisms. Journal of Molecular and Cellular Cardiology. 1994;26(3):279-292.

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    Cai Y., Yu S.-S., Chen T.-T., et al. EGCG inhibits CTGF expression via blocking NF-κB activation in cardiac fibroblast. Phytomedicine. 2013;20(2):106-113.

    Not in our library10.1016/j.phymed.2012.10.002

  56. 56.

    Kitamura M., Nishino T., Obata Y., et al. Epigallocatechin gallate suppresses peritoneal fibrosis in mice. Chemico-Biological Interactions. 2012;195(1):95-104.

    Not in our library10.1016/j.cbi.2011.11.002

  57. 57.

    Nakagawa H., Wachi M., Kato M., et al. Fenton reaction is primarily involved in a mechanism of (–)-epigallocatechin-3-gallate to induce osteoclastic cell death. Biochemical and Biophysical Research Communications. 2002;292(1):94-101.

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  58. 58.

    Yun J.-H., Pang E.-K., Kim C.-S., et al. Inhibitory effects of green tea polyphenol (−)-epigallocatechin gallate on the expression of matrix metalloproteinase-9 and on the formation of osteoclasts. Journal of Periodontal Research. 2004;39(5):300-307.

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  59. 59.

    Vali B., Rao L. G., El-Sohemy A. Epigallocatechin-3-gallate increases the formation of mineralized bone nodules by human osteoblast-like cells. Journal of Nutritional Biochemistry. 2007;18(5):341-347.

    Not in our library10.1016/j.jnutbio.2006.06.005

  60. 60.

    Gangji V., Hauzeur J. P., Matos C., de Maertelaer V., Toungouz M., Lambermont M. Treatment of osteonecrosis of the femoral head with implantation of autologous bone-marrow cells: a pilot study. Journal of Bone and Joint Surgery—American Volume. 2004;86(6):1153-1160.

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  61. 61.

    Caplan A. I. Adult mesenchymal stem cells for tissue engineering versus regenerative medicine. Journal of Cellular Physiology. 2007;213(2):341-347.

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    Pittenger M. F., Mackay A. M., Beck S. C., et al. Multilineage potential of adult human mesenchymal stem cells. Science. 1999;284(5411):143-147.

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    Kamitakahara M., Ohtsuki C., Miyazaki T. Review paper: Behavior of ceramic biomaterials derived from tricalcium phosphate in physiological condition. Journal of Biomaterials Applications. 2008;23(3):197-212.

    Not in our library10.1177/0885328208096798

  64. 64.

    Kihara H., Shiota M., Yamashita Y., Kasugai S. Biodegradation process of α-TCP particles and new bone formation in a rabbit cranial defect model. Journal of Biomedical Materials Research—Part B Applied Biomaterials. 2006;79(2):284-291.

    Not in our library10.1002/jbm.b.30540

  65. 65.

    Nyan M., Sato D., Kihara H., MacHida T., Ohya K., Kasugai S. Effects of the combination with α-tricalcium phosphate and simvastatin on bone regeneration. Clinical Oral Implants Research. 2009;20(3):280-287.

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  66. 66.

    Sang S., Lee M.-J., Hou Z., Ho C.-T., Yang C. S. Stability of tea polyphenol (−)-epigallocatechin-3-gallate and formation of dimers and epimers under common experimental conditions. Journal of Agricultural and Food Chemistry. 2005;53(24):9478-9484.

    Not in our library10.1021/jf0519055

  67. 67.

    Hong J., Lu H., Meng X., Ryu J.-H., Hara Y., Yang C. S. Stability, cellular uptake, biotransformation, and efflux of tea polyphenol (−)-epigallocatechin-3-gallate in HT-29 human colon adenocarcinoma cells. Cancer Research. 2002;62(24):7241-7246.

    Not in our library

  68. 68.

    Hou Z., Sang S., You H., et al. Mechanism of action of (−)-epigallocatechin-3-gallate: auto-oxidation-dependent inactivation of epidermal growth factor receptor and direct effects on growth inhibition in human esophageal cancer KYSE 150 cells. Cancer Research. 2005;65(17):8049-8056.

    Not in our library10.1158/0008-5472.can-05-0480

  69. 69.

    Naasani I., Oh-hashi F., Oh-hara T., et al. Blocking telomerase by dietary polyphenols is a major mechanism for limiting the growth of human cancer cells in vitro and in vivo. Cancer Research. 2003;63(4):824-830.

    Not in our library

  70. 70.

    Sang S., Yang I., Buckley B., Ho C.-T., Yang C. S. Autoxidative quinone formation in vitro and metabolite formation in vivo from tea polyphenol (−)-epigallocatechin-3-gallate: studied by real-time mass spectrometry combined with tandem mass ion mapping. Free Radical Biology and Medicine. 2007;43(3):362-371.

    Not in our library10.1016/j.freeradbiomed.2007.04.008

  71. 71.

    Liu Z., Nakashima S., Nakamura T., Munemasa S., Murata Y., Nakamura Y. (−)-Epigallocatechin-3-gallate inhibits human angiotensin-converting enzyme activity through an autoxidation-dependent mechanism. Journal of Biochemical & Molecular Toxicology. 2017.

    Not in our library10.1002/jbt.21932

  72. 72.

    Ghosh S., Pandey N. K., Dasgupta S. (−)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme. International Journal of Biological Macromolecules. 2013;54(1):90-98.

    Not in our library10.1016/j.ijbiomac.2012.11.031

  73. 73.

    Ishii T., Mori T., Tanaka T., et al. Covalent modification of proteins by green tea polyphenol (−)-epigallocatechin-3-gallate through autoxidation. Free Radical Biology and Medicine. 2008;45(10):1384-1394.

    Not in our library10.1016/j.freeradbiomed.2008.07.023

  74. 74.

    Tanaka T., Ishii T., Mizuno D., et al. (−)-Epigallocatechin-3-gallate suppresses growth of AZ521 human gastric cancer cells by targeting the DEAD-box RNA helicase p68. Free Radical Biology and Medicine. 2011;50(10):1324-1335.

    Not in our library10.1016/j.freeradbiomed.2011.01.024

  75. 75.

    Mori T., Ishii T., Akagawa M., Nakamura Y., Nakayama T. Covalent binding of tea catechins to protein thiols: The relationship between stability and electrophilic reactivity. Bioscience, Biotechnology and Biochemistry. 2010;74(12):2451-2456.

    Not in our library10.1271/bbb.100509

  76. 76.

    Lecumberri E., Dupertuis Y. M., Miralbell R., Pichard C. Green tea polyphenol epigallocatechin-3-gallate (EGCG) as adjuvant in cancer therapy. Clinical Nutrition. 2013;32(6):894-903.

    Not in our library10.1016/j.clnu.2013.03.008

  77. 77.

    Lin S., Kok S., Kuo M. Y., et al. Sequential expressions of MMP-1, TIMP-1, IL-6, and COX-2 genes in induced periapical lesions in rats. European Journal of Oral Sciences. 2002;110(3):246-253.

    Not in our library10.1034/j.1600-0447.2002.11227.x

  78. 78.

    Wang C.-Y., Tani-Ishii N., Stashenko P. Bone-resorptive cytokine gene expression in periapical lesions in the rat. Oral Microbiology and Immunology. 1997;12(2):65-71.

    Not in our library10.1111/j.1399-302x.1997.tb00619.x

  79. 79.

    Hong J.-Y., Yon J., Lee J.-S., et al. Effects of epigallocatechin-3-gallate on the healing of extraction sockets with a periapical lesion: A pilot study in dogs. Journal of Biomedical Materials Research Part B: Applied Biomaterials. 2015;103(4):727-734.

    Not in our library10.1002/jbm.b.33238

  80. 80.

    Shin Y.-S., Seo J.-Y., Oh S.-H., et al. The effects of ErhBMP-2-/EGCG-coated BCP bone substitute on dehiscence around dental implants in dogs. Oral Diseases. 2014;20(3):281-287.

    Not in our library10.1111/odi.12109

  81. 81.

    Cho A.-R., Kim J.-H., Lee D.-E., et al. The effect of orally administered epigallocatechin-3-gallate on ligature-induced periodontitis in rats. Journal of Periodontal Research. 2013;48(6):781-789.

    Not in our library10.1111/jre.12071

  82. 82.

    Wang H., Boyapati L. ‘PASS’ principles for predictable bone regeneration. Implant Dentistry. 2006;15(1):8-17.

    Not in our library10.1097/01.id.0000204762.39826.0f

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    Tonelli P., Duvina M., Barbato L., et al. Bone regeneration in dentistry. Clinical Cases in Mineral and Bone Metabolism. 2011;8(3):24-28.

    Not in our library

  84. 84.

    Kostopoulos L., Karring T. Augmentation of the rat mandible using guided tissue regeneration. Clinical Oral Implants Research. 1994;5(2):75-82.

    Not in our library10.1034/j.1600-0501.1994.050203.x

  85. 85.

    Dahlin C., Sennerby L., Lekholm U., Linde A., Nyman S. Generation of new bone around titanium implants using a membrane technique: an experimental study in rabbits. The International Journal of Oral & Maxillofacial Implants. 1989;4(1):19-25.

    Not in our library

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    Chu C., Deng J., Xiang L., et al. Evaluation of epigallocatechin-3-gallate (EGCG) cross-linked collagen membranes and concerns on osteoblasts. Materials Science and Engineering C. 2016;67:386-394.

    Not in our library10.1016/j.msec.2016.05.021

  87. 87.

    Chu C., Deng J., Liu L., et al. Nanoparticles combined with growth factors: recent progress and applications. RSC Advances. 2016;6(93):90856-90872.

    Not in our library10.1039/c6ra13636b

  88. 88.

    Chu C., Deng J., Hou Y., et al. Application of PEG and EGCG modified collagen-base membrane to promote osteoblasts proliferation. Materials Science and Engineering C. 2017;76:31-36.

    Not in our library10.1016/j.msec.2017.02.157

  89. 89.

    Chu C., Deng J., Man Y., Qu Y. Evaluation of nanohydroxyapaptite (nano-HA) coated epigallocatechin-3-gallate (EGCG) cross-linked collagen membranes. Materials Science and Engineering C. 2017;78:258-264.

    Not in our library10.1016/j.msec.2017.04.069

  90. 90.

    Chu C., Deng J., Sun X., Qu Y., Man Y. Collagen membrane and immune response in guided bone regeneration: recent progress and perspectives. Tissue Engineering Part B: Reviews. 2017.

    Not in our library10.1089/ten.teb.2016.0463

  91. 91.

    Taylor J. P., Hardy J., Fischbeck K. H. Toxic proteins in neurodegenerative disease. Science. 2002;296(5575):1991-1995.

    Not in our library10.1126/science.1067122

  92. 92.

    Sacchettini J. C., Kelly J. W. Therapeutic strategies for human amyloid diseases. Nature Reviews Drug Discovery. 2002;1(4):267-275.

    Not in our library10.1038/nrd769

  93. 93.

    Dobson C. M. Protein folding and misfolding. Nature. 2003;426(6968):884-890.

    Not in our library10.1038/nature02261

  94. 94.

    Rochet J.-C., Lansbury P. T. Amyloid fibrillogenesis: Themes and variations. Current Opinion in Structural Biology. 2000;10(1):60-68.

    Not in our library10.1016/s0959-440x(99)00049-4

  95. 95.

    Ehrnhoefer D. E., Bieschke J., Boeddrich A., et al. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nature Structural and Molecular Biology. 2008;15(6):558-566.

    Not in our library10.1038/nsmb.1437

  96. 96.

    Berg D., Gerlach M., Youdim M. B. H., et al. Brain iron pathways and their relevance to Parkinson's disease. Journal of Neurochemistry. 2001;79(2):225-236.

    Not in our library10.1046/j.1471-4159.2001.00608.x

  97. 97.

    Gerlach M., Ben-Shachar D., Riederer P., Youdim M. B. H. Altered brain metabolism of iron as a cause of neurodegenerative diseases? Journal of Neurochemistry. 1994;63(3):793-807.

    Not in our library10.1046/j.1471-4159.1994.63030793.x

  98. 98.

    Fahn S., Cohen G. The oxidant stress hypothesis in Parkinson's disease: evidence supporting it. Annals of Neurology. 1992;32(6):804-812.

    Not in our library10.1002/ana.410320616

  99. 99.

    Riederer P., Sofic E., Rausch W. D., et al. Transition metals, ferritin, glutathione, and ascorbic acid in parkinsonian brains. Journal of Neurochemistry. 1989;52(2):515-520.

    Not in our library10.1111/j.1471-4159.1989.tb09150.x

  100. 100.

    Senior K. New genes reveal major role for iron in neurodegeneration. The Lancet. 2001;358(9278):p. 302.

    Not in our library10.1016/s0140-6736(01)05522-2

  101. 101.

    Cai J., Jing D., Shi M., et al. Epigallocatechin gallate (EGCG) attenuates infrasound-induced neuronal impairment by inhibiting microglia-mediated inflammation. Journal of Nutritional Biochemistry. 2014;25(7):716-725.

    Not in our library10.1016/j.jnutbio.2014.02.012

  102. 102.

    Renno W. M., Al-Maghrebi M., Alshammari A., George P. (−)-Epigallocatechin-3-gallate (EGCG) attenuates peripheral nerve degeneration in rat sciatic nerve crush injury. Neurochemistry International. 2013;62(3):221-231.

    Not in our library10.1016/j.neuint.2012.12.018

  103. 103.

    Ludwig A., Lorenz M., Grimbo N., et al. The tea flavonoid epigallocatechin-3-gallate reduces cytokine-induced VCAM-1 expression and monocyte adhesion to endothelial cells. Biochemical and Biophysical Research Communications. 2004;316(3):659-665.

    Not in our library10.1016/j.bbrc.2004.02.099

  104. 104.

    Aneja R., Hake P. W., Burroughs T. J., Denenberg A. G., Wong H. R., Zingarelli B. Epigallocatechin, a green tea polyphenol, attenuates myocardial ischemia reperfusion injury in rats. Molecular Medicine. 2004;10(1–6):55-62.

    Not in our library10.2119/2004-00032.aneja

  105. 105.

    Lorenz M., Wessler S., Follmann E., et al. A constituent of green tea, epigallocatechin-3-gallate, activates endothelial nitric oxide synthase by a phosphatidylinositol-3-OH-kinase-, cAMP-dependent protein kinase-, and Akt-dependent pathway and leads to endothelial-dependent vasorelaxation. The Journal of Biological Chemistry. 2004;279(7):6190-6195.

    Not in our library10.1074/jbc.m309114200

  106. 106.

    Han D.-W., Lim H. R., Baek H. S., et al. Inhibitory effects of epigallocatechin-3-O-gallate on serum-stimulated rat aortic smooth muscle cells via nuclear factor-κB down-modulation. Biochemical and Biophysical Research Communications. 2006;345(1):148-155.

    Not in our library10.1016/j.bbrc.2006.04.072

  107. 107.

    Cho H. H., Han D.-W., Matsumura K., Tsutsumi S., Hyon S.-H. The behavior of vascular smooth muscle cells and platelets onto epigallocatechin gallate-releasing poly(l-lactide-co-ε-caprolactone) as stent-coating materials. Biomaterials. 2008;29(7):884-893.

    Not in our library10.1016/j.biomaterials.2007.10.052

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