The 38 kDa Ca2+/membrane-binding protein of pig granulocytes needs a high Ca2+ concentration to be phosphorylated by protein kinase C

Gyöngyi Farkas, L. Buday, Ferenc Antoni, A. Faragó

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The 38 kDa Ca2+/membrane-binding protein reported to be the dominant substrate of protein kinase C in the extracts of pig neutrophil granulocytes was purified partially and its phosphorylation was investigated. In pig granulocytes type II protein kinase C was the major isoform, while type III isoenzyme was present only as a minor activity. Phosphorylation of the 38 kDa protein was performed with rat brain protein kinase C. Each of the three isoenzymes purified from rat brain was able to phosphorylate this protein, though on the conditions used in our experiments it was phosphorylated most intensively by type II protein kinase C. A phospholipid-dependent, but Ca2+-independent, form of protein kinase C was demonstrated with the aid of a synthetic oligopeptide substrate. Phosphorylation of the 38 kDa protein by the Ca2+-independent enzyme proceeded exclusively in the presence of Ca2+. The Ca2+ concentration necessary for the phosphorylation of the 38 kDa protein by either form of protein kinase C was by orders of magnitude higher than that required for the activation of protein kinase C.

Original languageEnglish
Pages (from-to)81-86
Number of pages6
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1091
Issue number1
DOIs
Publication statusPublished - Jan 10 1991

Fingerprint

Granulocytes
Protein Kinase C
Carrier Proteins
Membrane Proteins
Swine
Phosphorylation
Isoenzymes
Proteins
Oligopeptides
Brain
Phospholipids
Protein Isoforms
Neutrophils
Enzymes

Keywords

  • (Granulocytes)
  • (Pig)
  • Calcium ion/membrane binding protein, 38 kDa
  • Isoenzyme
  • Lipocortin phosphorylation
  • Phospholipid-dependent calcium-independent protein kinase
  • Protein kinase C

ASJC Scopus subject areas

  • Biophysics
  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

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title = "The 38 kDa Ca2+/membrane-binding protein of pig granulocytes needs a high Ca2+ concentration to be phosphorylated by protein kinase C",
abstract = "The 38 kDa Ca2+/membrane-binding protein reported to be the dominant substrate of protein kinase C in the extracts of pig neutrophil granulocytes was purified partially and its phosphorylation was investigated. In pig granulocytes type II protein kinase C was the major isoform, while type III isoenzyme was present only as a minor activity. Phosphorylation of the 38 kDa protein was performed with rat brain protein kinase C. Each of the three isoenzymes purified from rat brain was able to phosphorylate this protein, though on the conditions used in our experiments it was phosphorylated most intensively by type II protein kinase C. A phospholipid-dependent, but Ca2+-independent, form of protein kinase C was demonstrated with the aid of a synthetic oligopeptide substrate. Phosphorylation of the 38 kDa protein by the Ca2+-independent enzyme proceeded exclusively in the presence of Ca2+. The Ca2+ concentration necessary for the phosphorylation of the 38 kDa protein by either form of protein kinase C was by orders of magnitude higher than that required for the activation of protein kinase C.",
keywords = "(Granulocytes), (Pig), Calcium ion/membrane binding protein, 38 kDa, Isoenzyme, Lipocortin phosphorylation, Phospholipid-dependent calcium-independent protein kinase, Protein kinase C",
author = "Gy{\"o}ngyi Farkas and L. Buday and Ferenc Antoni and A. Farag{\'o}",
year = "1991",
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T1 - The 38 kDa Ca2+/membrane-binding protein of pig granulocytes needs a high Ca2+ concentration to be phosphorylated by protein kinase C

AU - Farkas, Gyöngyi

AU - Buday, L.

AU - Antoni, Ferenc

AU - Faragó, A.

PY - 1991/1/10

Y1 - 1991/1/10

N2 - The 38 kDa Ca2+/membrane-binding protein reported to be the dominant substrate of protein kinase C in the extracts of pig neutrophil granulocytes was purified partially and its phosphorylation was investigated. In pig granulocytes type II protein kinase C was the major isoform, while type III isoenzyme was present only as a minor activity. Phosphorylation of the 38 kDa protein was performed with rat brain protein kinase C. Each of the three isoenzymes purified from rat brain was able to phosphorylate this protein, though on the conditions used in our experiments it was phosphorylated most intensively by type II protein kinase C. A phospholipid-dependent, but Ca2+-independent, form of protein kinase C was demonstrated with the aid of a synthetic oligopeptide substrate. Phosphorylation of the 38 kDa protein by the Ca2+-independent enzyme proceeded exclusively in the presence of Ca2+. The Ca2+ concentration necessary for the phosphorylation of the 38 kDa protein by either form of protein kinase C was by orders of magnitude higher than that required for the activation of protein kinase C.

AB - The 38 kDa Ca2+/membrane-binding protein reported to be the dominant substrate of protein kinase C in the extracts of pig neutrophil granulocytes was purified partially and its phosphorylation was investigated. In pig granulocytes type II protein kinase C was the major isoform, while type III isoenzyme was present only as a minor activity. Phosphorylation of the 38 kDa protein was performed with rat brain protein kinase C. Each of the three isoenzymes purified from rat brain was able to phosphorylate this protein, though on the conditions used in our experiments it was phosphorylated most intensively by type II protein kinase C. A phospholipid-dependent, but Ca2+-independent, form of protein kinase C was demonstrated with the aid of a synthetic oligopeptide substrate. Phosphorylation of the 38 kDa protein by the Ca2+-independent enzyme proceeded exclusively in the presence of Ca2+. The Ca2+ concentration necessary for the phosphorylation of the 38 kDa protein by either form of protein kinase C was by orders of magnitude higher than that required for the activation of protein kinase C.

KW - (Granulocytes)

KW - (Pig)

KW - Calcium ion/membrane binding protein, 38 kDa

KW - Isoenzyme

KW - Lipocortin phosphorylation

KW - Phospholipid-dependent calcium-independent protein kinase

KW - Protein kinase C

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