Heparin-activated protein kinase from rabbit muscle: Relationship to enzymes of the glycogen synthase kinase-3 category

Zafeer Ahmad, Fook Thean Lee, Anna A. DePaoli-Roach, Peter J. Roach

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

A heparin-activated protein kinase has been previously identified in rabbit skeletal muscle extracts (Z. Ahmad et al. (1985) FEBS Lett. 179, 96-100). Further study has indicated that this enzyme phosphorylates rabbit muscle glycogen synthase in the same tryptic peptide(s) as the protein kinase FA/GSK-3 (glycogen synthase kinase-3) and is able to activate the ATP-Mg2+-dependent protein phosphatase. These results indicate similarities in properties between the two protein kinases. Exposure of the heparinactivated enzyme to trypsin resulted in loss of heparin activation, from 3-fold to 1.3-fold. One hypothesis suggested by this result is that the enzyme FA/GSK-3 could be a derivative of the heparin-activated enzyme that has lost heparin sensitivity. The conceptual importance of this hypothesis is that it may provide a clue to the mode of regulation of this important class of protein kinases.

Original languageEnglish (US)
Pages (from-to)329-335
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume250
Issue number2
DOIs
StatePublished - Nov 1 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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