Linked Life Data

3689368

Source:http://linkedlifedata.com/resource/pubmed/id/3689368

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-12-21
pubmed:abstractText
One mechanism by which drugs alter the function of enzymes is through chronic inhibition. To determine whether commonly used cancer chemotherapeutic agents could alter protein kinase C (PKC) and thereby modify the calcium-messenger system, we studied the effect of anthracyclines and vinca alkaloids on the activity of PKC. Doxorubicin, daunomycin, vincristine and vinblastine inhibited the activity of PKC by 50% at concentrations of 150, 120, 350 and 140 microM respectively. Furthermore, we demonstrated the potential for this interaction to occur in intact cells, since doxorubicin blocked the binding of the phorbol ester, PDBu, to its receptor, PKC. The mode of inhibition of PKC was due, at least in part, to interference with the activation of the enzyme by phosphatidylserine. The activity of PKC was increased 15 fold in a highly resistant human breast cancer line, but this increase in enzymic activity was not seen in all lines tested. These studies demonstrate that anthracyclines and vinca alkaloids inhibit PKC, and suggest that chronic antagonism could lead to changes in its activity and function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
718-25
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Inhibition of protein kinase C by antineoplastic agents: implications for drug resistance.
pubmed:affiliation
Department of Medicine, Yale University School of Medicine, New Haven, CT 06510.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't