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PMID: 3025869 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Phosphorylation by protein kinase C of a 20-kDa cytoskeletal polypeptide enhances its susceptibility to digestion by calpain.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 84 ·No. 2 ·1987-01-00 ·Pages 398-401

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

Abstract

Incubation of the cytoskeletal fraction from human neutrophils with the proteolytically activated form of protein kinase C results in the phosphorylation of several components, including a 20-kDa polypeptide, probably consisting of myosin light chains. The 20-kDa polypeptide is also specifically phosphorylated by activated protein kinase C in a solubilized 20-kDa/80-kDa complex that was obtained after sonication of the insoluble cytoskeletal fraction. Phosphorylation of this polypeptide, in either the insoluble cytoskeletal fraction or the soluble 20-kDa/80-kDa complex, greatly enhances its susceptibility to digestion by the Ca2+-requiring proteinase (calpain, EC 3.4.22.17) of human neutrophils. Thus, signals that activate calpain by mobilizing intracellular calcium would lead to proteolytic activation of protein kinase C, phosphorylation of cytoskeletal proteins, and remodeling of the cytoskeleton by proteolysis of at least one cytoskeletal component.

MeSH Terms
Calpain/blood Cytoskeletal Proteins/metabolism Humans Kinetics Molecular Weight Neutrophils/enzymology Phosphoproteins/isolation & purification Phosphorylation Protein Kinase C/blood
Chemicals
Cytoskeletal Proteins Phosphoproteins Protein Kinase C Calpain
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Pontremoli S
Melloni E
Michetti M
Sparatore B
Salamino F
Sacco O
Horecker B L
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37 references, click to expand
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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.84.2.398
Published
1987-01-00
Pages
398-401
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC304214
Subset
IM
Corrections
ErratumIn
-
External Links
PubMed source DOI: 10.1073/pnas.84.2.398 PMC Full Text View journal details
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