Inhibition of T Cell Activation by Protein Kinase C Pseudosubstrates
| Autor: | A. Alavi-Nassab, J. Freire-Moar, C.W. Turchk, P. Barja |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
CD3 Complex
Molecular Sequence Data Immunology Gene Expression Peptide In Vitro Techniques Biology Lymphocyte Activation Jurkat cells Isozyme Cell Line Humans Amino Acid Sequence RNA Messenger Lymphotoxin-alpha Protein Kinase C Protein kinase C DNA Primers chemistry.chemical_classification Base Sequence Receptors Interleukin-2 Molecular biology Enzyme assay Enzyme chemistry Biochemistry Enzyme inhibitor biology.protein Tetradecanoylphorbol Acetate Signal transduction Peptides |
| Zdroj: | Cellular Immunology. 153:28-38 |
| ISSN: | 0008-8749 |
| DOI: | 10.1006/cimm.1994.1003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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