Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-2-22
pubmed:abstractText
PKC pseudosubstrate consensus sequences can be found in the amino terminal region of all the different PKC isoenzymes characterized to date. Here we have used four peptides corresponding to the putative pseudosubstrate sequences from the PKC isoenzymes alpha, gamma, delta, and epsilon. These peptides showed PKC inhibitory activity when tested in a PKC-specific enzyme assay at concentrations of 25 to 100 microM, similar to what has been reported for the myristylated peptide KRTLR. Although the presence of a myristyl group at the amino terminal end of any of these peptides is not essential for their inhibitory activity, myristylation increased the inhibitory activity significantly. By contrast, the myristylated control peptide (GALRQQKNVHEVKN) was not active even at a 100 microM concentration. All of the PKC inhibitory peptides were also able to block PKC activity in a cell assay as demonstrated by their ability to inhibit the induction of IL-2R and TNF-beta expression in Jurkat cells. Finally, we confirmed a previous report of the inhibitory activity of the myristylated peptide KRTLR and showed that other related peptides (N-m-RLTRK, N-m-RRLKT) are also active in these assays.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0008-8749
pubmed:author
pubmed:issnType
Print
pubmed:volume
153
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
28-38
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Inhibition of T cell activation by protein kinase C pseudosubstrates.
pubmed:affiliation
Department of Molecular Immunology, Syntex Discovery Research, Palo Alto, California 94304.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't