Inhibition of glycogen synthase (casein) kinase-1 by different divalent metal ions
The specificity of glycogen synthase (casein) kinase-1 (CK-1) for different divalent metal ions was explored in this study. Of the eight metal ions (Mg, Mn, Zn, Cu, Ca, Ni, Co, Fe) tested only Mg/sup 2 +/ supported significant kinase activity. Several of the other metals, however, inhibited the Mg/sup 2 +/-stimulated kinase activity. Half-maximal inhibition by Zn, Mn, Co, Fe and Ni were observed at 50, 55, 110, 125 and 300 ..mu..M, respectively. Kinetic analyses using Zn/sup 2 +/ indicate that at a constant (ATP) Zn/sup 2 +/ increases the K/sub m/ for casein, the V/sub max/ being unaffected +/- Zn/sup 2 +/. At a constant (casein), Zn/sup 2 +/ decreased the V/sub max/ for ATP, the K/sub m/ remaining unchanged +/- Zn/sup 2 +/. The inhibition of CK-1 by the different metals is reversed by EGTA or EDTA. These results suggest that divalent metal ions such as Zn/sup 2 +/ and Mn/sup 2 +/ that do not support CK-1 activity may serve as inhibitors of the kinase in vivo.
- Research Organization:
- Univ. of Waterloo, Ontario
- OSTI ID:
- 6065413
- Report Number(s):
- CONF-870644-
- Journal Information:
- Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
- Country of Publication:
- United States
- Language:
- English
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CALCIUM COMPOUNDS
BIOLOGICAL EFFECTS
COBALT COMPOUNDS
COPPER COMPOUNDS
IRON COMPOUNDS
MAGNESIUM COMPOUNDS
MANGANESE COMPOUNDS
NICKEL COMPOUNDS
PHOSPHOTRANSFERASES
ENZYME ACTIVITY
ZINC COMPOUNDS
CATIONS
EDTA
EGTA
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CHARGED PARTICLES
CHELATING AGENTS
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GLYCOLS
HYDROXY COMPOUNDS
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ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
TRANSFERASES
TRANSITION ELEMENT COMPOUNDS
560300* - Chemicals Metabolism & Toxicology