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Inhibition of glycogen synthase (casein) kinase-1 by different divalent metal ions

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6065413
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-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 46:6
Country of Publication:
United States
Language:
English