Linked Life Data

17230588

Source:http://linkedlifedata.com/resource/pubmed/id/17230588

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-2-6
pubmed:abstractText
Oligomeric procyanidins were found to inhibit the protein tyrosine kinase activity of the epidermal growth factor receptor (EGFR). The inhibitory potency was found to increase with the degree of oligomerisation (PA2 > PC1 >> PB1 = PB2 = PB3 = PB4 >> (-)-epicatechin). To address the question whether the interference with the activity of isolated EGFR preparations also plays a role within intact cells, effects on the phosphorylation status of the EGFR, as a measure of its activity, were determined in human colon carcinoma cells. Treatment of HT29 cells with the trimeric procyanidin PC1 resulted in a decrease of the EGFR autophosphorylation already at low micromolar concentrations. A respective procyanidin tetramer (PA2) failed to affect substantially the receptor phosphorylation status by up to 50 microM, indicating that the effectiveness of oligomeric procyanidins against EGFR activity within intact cells might be limited with increasing degree of polymerisation. Nevertheless, oligomeric procyanidins were identified as potential inhibitors of the EGFR, which might be of interest with respect to chemoprevention. However, PC1 and PA2 were also identified as potent inhibitors of the catalytic activity of human topoisomerase I and II, demanding further studies to elucidate whether the interference of procyanidins with topoisomerases might impair DNA integrity, thus limiting their usefulness in terms of chemoprevention.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1613-4125
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
192-200
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The epidermal growth factor receptor and human topoisomerases represent potential cellular targets of oligomeric procyanidins.
pubmed:affiliation
Institute of Applied Biosciences, Section of Food Toxicology, University of Karlsruhe TH, Kaiserstrasse 12, Karlsruhe, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't