(-)-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
Pancreatic Neoplasms D010190 77 associated lipids
Mammary Neoplasms, Experimental D008325 67 associated lipids
Lung Neoplasms D008175 171 associated lipids
Liver Diseases D008107 31 associated lipids
Hemolysis D006461 131 associated lipids
Glioblastoma D005909 27 associated lipids
Body Weight D001835 333 associated lipids
Adenocarcinoma D000230 166 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?


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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
Pan CY et al. Enhancement of inward Ca(2+) currents in bovine chromaffin cells by green tea polyphenol extracts. 2002 Neurochem. Int. pmid:11738479
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de Mejía EG and Ramírez-Mares MV Leaf extract from Ardisia compressa protects against 1-nitropyrene-induced cytotoxicity and its antioxidant defense disruption in cultured rat hepatocytes. 2002 Toxicology pmid:12204551
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Lu H et al. Enzymology of methylation of tea catechins and inhibition of catechol-O-methyltransferase by (-)-epigallocatechin gallate. 2003 Drug Metab. Dispos. pmid:12695345
Levine L Does the release of arachidonic acid from cells play a role in cancer chemoprevention? 2003 FASEB J. pmid:12724337
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Bellosta S et al. Inhibition of metalloproteinase-9 activity and gene expression by polyphenolic compounds isolated from the bark of Tristaniopsis calobuxus (Myrtaceae). 2003 Cell. Mol. Life Sci. pmid:12943230
Yeh CW et al. Suppression of fatty acid synthase in MCF-7 breast cancer cells by tea and tea polyphenols: a possible mechanism for their hypolipidemic effects. 2003 Pharmacogenomics J. pmid:12931129
Facchini A et al. Effect of green tea extract on the induction of ornithine decarboxylase and the activation of extracellular signal-regulated kinase in bladder carcinoma ECV304 cells. 2003 Nutr Cancer pmid:14769544
Lin YS et al. Factors affecting the levels of tea polyphenols and caffeine in tea leaves. 2003 J. Agric. Food Chem. pmid:12643643
Lill G et al. Complex effects of different green tea catechins on human platelets. 2003 FEBS Lett. pmid:12832052
Jeon SY et al. Green tea catechins as a BACE1 (beta-secretase) inhibitor. 2003 Bioorg. Med. Chem. Lett. pmid:14592472
Yoshimura Y et al. Evaluation of the NO scavenging activity of procyanidin in grape seed by use of the TMA-PTIO/NOC 7 ESR system. 2003 J. Agric. Food Chem. pmid:14558755
Koh SH et al. Epigallocatechin gallate protects nerve growth factor differentiated PC12 cells from oxidative-radical-stress-induced apoptosis through its effect on phosphoinositide 3-kinase/Akt and glycogen synthase kinase-3. 2003 Brain Res. Mol. Brain Res. pmid:14559356
Kumagai A et al. Tumor chemopreventive activity of 3-O-acylated (--)-epigallocatechins. 2003 Bioorg. Med. Chem. pmid:14604677
Kundu JK et al. Inhibition of phorbol ester-induced COX-2 expression by epigallocatechin gallate in mouse skin and cultured human mammary epithelial cells. 2003 J. Nutr. pmid:14608118
Ramírez-Mares MV and de Mejía EG Comparative study of the antioxidant effect of ardisin and epigallocatechin gallate in rat hepatocytes exposed to benomyl and 1-nitropyrene. 2003 Food Chem. Toxicol. pmid:12963005
Weber JM et al. Inhibition of adenovirus infection and adenain by green tea catechins. 2003 Antiviral Res. pmid:12742577
Yang LL et al. Antitumor principle constituents of Myrica rubra Var. acuminata. 2003 J. Agric. Food Chem. pmid:12720379
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Taylor AW et al. Hop (Humulus lupulus L.) proanthocyanidins characterized by mass spectrometry, acid catalysis, and gel permeation chromatography. 2003 J. Agric. Food Chem. pmid:12822954
Morikawa T et al. Structures of new friedelane-type triterpenes and eudesmane-type sesquiterpene and aldose reductase inhibitors from Salacia chinensis. 2003 J. Nat. Prod. pmid:14510595
Suzuki M et al. Epimerization of tea catechins and O-methylated derivatives of (-)-epigallocatechin-3-O-gallate: relationship between epimerization and chemical structure. 2003 J. Agric. Food Chem. pmid:12517118