(-)-Epigallocatechin

(-)-Epigallocatechin is a lipid of Polyketides (PK) class. The involved functions are known as Protective Agents, inhibitors, Process, Drug Kinetics and Fermentation. (-)-epigallocatechin often locates in Hepatic, Blood, Membrane, Back and apical membrane. The associated genes with (-)-Epigallocatechin are ADRBK1 gene and FASTK Gene. The related lipids are 1,2-dilinolenoyl-3-(4-aminobutyryl)propane-1,2,3-triol. The related experimental models are Rodent Model and Transgenic Model.

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Introduction

To understand associated biological information of (-)-Epigallocatechin, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with (-)-Epigallocatechin?

There are no associated biomedical information in the current reference collection.

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with (-)-Epigallocatechin

MeSH term MeSH ID Detail
Hemolysis D006461 131 associated lipids
Adenocarcinoma D000230 166 associated lipids
Lung Neoplasms D008175 171 associated lipids
Pancreatic Neoplasms D010190 77 associated lipids
Mammary Neoplasms, Experimental D008325 67 associated lipids
Body Weight D001835 333 associated lipids
Liver Diseases D008107 31 associated lipids
Glioblastoma D005909 27 associated lipids
Total 8

PubChem Associated disorders and diseases

What pathways are associated with (-)-Epigallocatechin

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with (-)-Epigallocatechin?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with (-)-Epigallocatechin?


Related references are published most in these journals:

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What lipids are associated with (-)-Epigallocatechin?

Related references are published most in these journals:

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What genes are associated with (-)-Epigallocatechin?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with (-)-Epigallocatechin?

Rodent Model

Rodent Model are used in the study 'Dietary (-)-epicatechin as a potent inhibitor of βγ-secretase amyloid precursor protein processing.' (Cox CJ et al., 2015) and Rodent Model are used in the study 'Effects of dosing condition on the oral bioavailability of green tea catechins after single-dose administration of Polyphenon E in healthy individuals.' (Chow HH et al., 2005).

Transgenic Model

Transgenic Model are used in the study 'Dietary (-)-epicatechin as a potent inhibitor of βγ-secretase amyloid precursor protein processing.' (Cox CJ et al., 2015).

Related references are published most in these journals:

Model Cross reference Weighted score Related literatures
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NCBI Entrez Crosslinks

All references with (-)-Epigallocatechin

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Authors Title Published Journal PubMed Link
Ludwig A et al. The tea flavonoid epigallocatechin-3-gallate reduces cytokine-induced VCAM-1 expression and monocyte adhesion to endothelial cells. 2004 Biochem. Biophys. Res. Commun. pmid:15033450
Long LH and Halliwell B The effects of oxaloacetate on hydrogen peroxide generation from ascorbate and epigallocatechin gallate in cell culture media: potential for altering cell metabolism. 2012 Biochem. Biophys. Res. Commun. pmid:22166196
Narukawa M et al. Evaluation of the bitterness of green tea catechins by a cell-based assay with the human bitter taste receptor hTAS2R39. 2011 Biochem. Biophys. Res. Commun. pmid:21272567
Bertoldi M et al. Green tea polyphenols: novel irreversible inhibitors of dopa decarboxylase. 2001 Biochem. Biophys. Res. Commun. pmid:11374875
Abe I et al. Green tea polyphenols: novel and potent inhibitors of squalene epoxidase. 2000 Biochem. Biophys. Res. Commun. pmid:10679280
Manalo DJ et al. Inactivation of prolyl hydroxylase domain (PHD) protein by epigallocatechin (EGCG) stabilizes hypoxia-inducible factor (HIF-1α) and induces hepcidin (Hamp) in rat kidney. 2011 Biochem. Biophys. Res. Commun. pmid:22138393
Bain J et al. The specificities of protein kinase inhibitors: an update. 2003 Biochem. J. pmid:12534346
Hong J et al. Effects of purified green and black tea polyphenols on cyclooxygenase- and lipoxygenase-dependent metabolism of arachidonic acid in human colon mucosa and colon tumor tissues. 2001 Biochem. Pharmacol. pmid:11705450
Chen D et al. Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. 2005 Biochem. Pharmacol. pmid:15857617
Baek WK et al. Inhibitory modulation of ATP-sensitive potassium channels by gallate-ester moiety of (-)-epigallocatechin-3-gallate. 2005 Biochem. Pharmacol. pmid:16216226
Ochiai H et al. Epigallocatechin-3-gallate is an inhibitor of Na+, K(+)-ATPase by favoring the E1 conformation. 2009 Biochem. Pharmacol. pmid:19539611
Feng W et al. Green tea catechins are potent sensitizers of ryanodine receptor type 1 (RyR1). 2010 Biochem. Pharmacol. pmid:20471964
Miyata M et al. The crystal structure of the green tea polyphenol (-)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site. 2010 Biochemistry pmid:20565072
Kamihira-Ishijima M et al. Inhibitory mechanism of pancreatic amyloid fibril formation: formation of the complex between tea catechins and the fragment of residues 22-27. 2012 Biochemistry pmid:23205879
Nakane H and Ono K Differential inhibitory effects of some catechin derivatives on the activities of human immunodeficiency virus reverse transcriptase and cellular deoxyribonucleic and ribonucleic acid polymerases. 1990 Biochemistry pmid:1693287
Kong LX and Zeng CM Effects of Seeding on Lysozyme Amyloid Fibrillation in the Presence of Epigallocatechin and Polyethylene Glycol. 2017 Biochemistry Mosc. pmid:28320299
Ikeda I et al. Tea catechins decrease micellar solubility and intestinal absorption of cholesterol in rats. 1992 Biochim. Biophys. Acta pmid:1643098
Annabi B et al. Green tea polyphenol (-)-epigallocatechin 3-gallate inhibits MMP-2 secretion and MT1-MMP-driven migration in glioblastoma cells. 2002 Biochim. Biophys. Acta pmid:11853893
Mochizuki M et al. Kinetic analysis and mechanistic aspects of autoxidation of catechins. 2002 Biochim. Biophys. Acta pmid:11853955
Sugita-Konishi Y et al. Epigallocatechin gallate and gallocatechin gallate in green tea catechins inhibit extracellular release of Vero toxin from enterohemorrhagic Escherichia coli O157:H7. 1999 Biochim. Biophys. Acta pmid:10572924