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PMID: 2339114 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 10 ·1990-05-00 ·Pages 3705-7

Pontremoli S, Michetti M, Melloni E, Sparatore B, Salamino F, Horecker BL

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.

MeSH Terms
Antibodies, Monoclonal Humans In Vitro Techniques Molecular Weight N-Formylmethionine Leucyl-Phenylalanine/pharmacology Neutrophils/drug effects,enzymology Protein Kinase C/blood,isolation & purification Tetradecanoylphorbol Acetate/pharmacology
Chemicals
Antibodies, Monoclonal N-Formylmethionine Leucyl-Phenylalanine Protein Kinase C Tetradecanoylphorbol Acetate
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Pontremoli S
Institute of Biological Chemistry, University of Genoa, Italy.
Michetti M
Melloni E
Sparatore B
Salamino F
Horecker B L
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.87.10.3705
Published
1990-05-00
Pages
3705-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC53971
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.87.10.3705 PMC Full Text View journal details
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