Multiple forms of glycogen synthase kinase: isolation of forms which are independent of cyclic AMP.
Rabbit renal cortex was found to contain three types of glycogen synthase kinase (GSK). Cylic AMP-dependent protein kinase (GSK-C) accounted for only a small fraction of the total GSK activity. The predominant type of GSK (GSK-P) could be adsorbed to phosphocellulose, but not to DEAE cellulose. The other major type (GSK-D) could be adsorbed to DEAE cellulose and exhibited several peaks when eluted with a linear NaC1 gradient. GSK-P and GSK-D were not affected by cyclic AMP or by the heat-stable protein inhibitor of cyclic AMP-dependent protein kinase. This suggests that cyclic AMP-independent mechanisms may play a major role in regulation of GSK. Neither GSK-P nor GSK-D were associated with the major peak of histone, kinase, casein kinase, protamine kinase or phosvitin kinase. Therefore it cannot be assumed that these protein kinase activities can be used to monitor GSK activity.
D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007672:Kidney Cortex / Q000201:enzymology*; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits
D007527:Isoenzymes; D000242:Cyclic AMP; D011494:Protein Kinases