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. 1990 May;87(10):3705–3707. doi: 10.1073/pnas.87.10.3705

Identification of the proteolytically activated form of protein kinase C in stimulated human neutrophils.

S Pontremoli 1, M Michetti 1, E Melloni 1, B Sparatore 1, F Salamino 1, B L Horecker 1
PMCID: PMC53971  PMID: 2339114

Abstract

The proteolytically activated form of protein kinase C has been identified in human neutrophils by using a monoclonal antibody that recognizes both the native kinase and the catalytically active proteolytic fragment (protein kinase M). Stimulation with fMet-Leu-Phe results in the conversion of approximately 30% of native protein kinase C to protein kinase M, with little evidence of further degradation. Stimulation with phorbol 12-myristate 13-acetate, on the other hand, causes only a transient formation of protein kinase M, with complete loss of total kinase activity. These differences are related to the differences in biochemical responses, reported earlier, in neutrophils exposed to these two activators.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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