Literature DB >> 8422258

Calcium-independent activation of protein kinase C by the dianionic form of phosphatidic acid.

G A Senisterra1, L C van Gorkom, R M Epand.   

Abstract

Phosphatidic acid in the form of small unilamellar vesicles has a dissociation constant of about 8.3 as determined by 31P nuclear magnetic resonance (NMR) spectroscopy. The activation of protein kinase C (PKC) by monovalent phosphatidic acid or phosphatidylserine occurs only in the presence of Ca2+. However, PKC activity on membranes of divalent anionic phosphatidic acid is independent of Ca2+ concentration.

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Year:  1993        PMID: 8422258     DOI: 10.1006/bbrc.1993.1006

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Cell-free activation of neutrophil NADPH oxidase by a phosphatidic acid-regulated protein kinase.

Authors:  L C McPhail; D Qualliotine-Mann; K A Waite
Journal:  Proc Natl Acad Sci U S A       Date:  1995-08-15       Impact factor: 11.205

2.  Time-course changes in content and fatty acid composition of phosphatidic acid from rat thymocytes during concanavalin A stimulation.

Authors:  S el Bawab; O Macovschi; M Lagarde; A F Prigent
Journal:  Biochem J       Date:  1995-05-15       Impact factor: 3.857

  2 in total

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