Binding of protein kinase C to neutrophil membranes in the presence of Ca2+ and its activation by a Ca2+-requiring proteinase

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

Research output: Contribution to journalArticle

Abstract

In the presence of micromolar concentrations of Ca2+, both protein kinase C and a cytosolic Ca2+-requiring neutral proteinase of human neutrophils become associated with the neutrophil membrane. Binding to the membrane results in activation of the proteinase, which then catalyzes limited proteolysis of the kinase to produce a form that is fully active in the absence of Ca2+ and phospholipid. This irreversibly activated protein kinase is released from the membrane and may thus have access, in the intact cell, to intracellular protein substrates. In the absence of proteinase, Ca2+ promotes the binding of protein kinase C, but conversion to the Ca2+/phospholipid-independent form does not occur and the kinase remains associated with the membrane fraction.

Original languageEnglish
Pages (from-to)6435-6439
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume82
Issue number19
DOIs
Publication statusPublished - 1985

ASJC Scopus subject areas

  • Genetics
  • General

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