Microsomal cAMP-independent histone H1 kinase activity in plasmacytoma, Morris hepatoma and normal liver.

Abstract

A protein kinase activity with high specificity for histone H1 was isolated from mouse plasmacytoma, Morris hepatoma and normal mouse liver and compared by ion exchange chromatography after DEAE-cellulose, hydroxylapatite and Sephadex G-200 chromatography. This cAMP-independent histone H1 kinase is not affected by the heat-stable cAMP-dependent protein kinase inhibitor. It has the following particular properties: it prefers GTP to ATP as substrate and was found to be present with a great activity only in neoplastic tissues. No phosphatase activity was detected in the partially purified histone H1 kinase fraction from normal and neoplastic cells. These results suggest either an increase amount of histone H1 kinase and/or of its activator in neoplastic cells, or the presence of a strong inhibitor in normal cells. This histone H1 kinase appears to be analogous to the chromatin bound kinase which phosphorylates histone H1 at the NH2 and COOH terminal regions. We might suggest an implication of this kinase in the regulation of cell division.

• Authors: M Schmitt, C Quirin-Stricker, J Kempf
• Journal: Biochimie (Biochimie) Vol. 64 Issue 1 Pg. 13-20 (Jan 1982) ISSN: 0300-9084 [Print] France
• PMID: 6279172 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Histones
• Guanosine Triphosphate
• Adenosine Triphosphate
• Cyclic AMP
• Protein Kinases
• Protamine Kinase

Topics

• Adenosine Triphosphate (metabolism)
• Animals
• Cyclic AMP (pharmacology)
• Guanosine Triphosphate (metabolism)
• Histones (metabolism)
• Liver Neoplasms, Experimental (enzymology)
• Mice
• Mice, Inbred BALB C
• Microsomes, Liver (enzymology)
• Phosphorylation
• Plasmacytoma (enzymology)
• Protamine Kinase (metabolism)
• Protein Kinases (metabolism)
• Rats
• Substrate Specificity