Preparation and Characterization of Calmodulin-Dependent Protein Kinase IV (CaM-Kinase IV) Free of CaM-Kinase IV Kinase from Rat Cerebral Cortex1

1995 ◽  
Vol 117 (1) ◽  
pp. 85-90 ◽  
Author(s):  
Isamu Kameshita ◽  
Hitoshi Fujisawa
Keyword(s):  
Protein Kinase ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Cam Kinase Iv

scholarly journals Activation mechanisms for Ca2+/calmodulin-dependent protein kinase IV. Identification of a brain CaM-kinase IV kinase.

1994 ◽  
Vol 269 (46) ◽  
pp. 28640-28647
Author(s):  
H Tokumitsu ◽  
D A Brickey ◽  
J Glod ◽  
H Hidaka ◽  
J Sikela ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Activation Mechanisms ◽  
Dependent Protein ◽  
Cam Kinase Iv

scholarly journals Characterization of Ca2+/calmodulin-dependent protein kinase in rat pancreatic islets

1993 ◽  
Vol 289 (3) ◽  
pp. 795-800 ◽  
Author(s):  
S J Hughes ◽  
H Smith ◽  
S J H Ashcroft
Keyword(s):  
Protein Kinase ◽  
Glycogen Synthase ◽  
Elongation Factor ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Elongation Factor 2 ◽  
Dependent Protein ◽  
Endogenous Substrates

We have attempted to identify islet Ca2+/calmodulin-dependent protein kinase (CaM kinase) by comparing its activity with purified brain CaM kinase II. Islet CaM kinase, in the presence of calmodulin and Ca2+, phosphorylated major endogenous substrates of 102, 57 and 53 kDa and also exogenous glycogen synthase; brain CaM kinase II phosphorylated glycogen synthase and peptides of 57 and 53 kDa. Alloxan (1 mM) inhibited the phosphorylation of glycogen synthase and the 102, 57 and 53 kDa islet peptides by islet CaM kinase; the phosphorylation of glycogen synthase and the 57 and 53 kDa substrates by brain CaM kinase II was also inhibited by alloxan. The Ca2+ and calmodulin-dependencies of phosphorylation of the endogenous islet substrates differed. In the presence of 400 nM calmodulin, half-maximal phosphorylation was attained at Ca2+ concentrations of 80 +/- 9, 401 +/- 61 and 459 +/- 59 nM for the 102, 57 and 53 kDa substrates respectively. In the presence of 10 microM Ca2+, half-maximal phosphorylation was attained at calmodulin concentrations of 9 +/- 2, 38 +/- 2.5 and 37 +/- 2 nM for the 102, 57 and 53 kDa substrates respectively. Differential centrifugation located the 102 kDa substrate in the post-100,000 g supernatant and the 57 and 53 kDa substrates in the particulate fraction. These data suggest that islet CaM kinase is similar to, if not identical with, brain CaM kinase II, but that phosphorylation of the endogenous 102 kDa substrate occurs by a distinct kinase which shows different sensitivities to Ca2+ and calmodulin. This kinase probably corresponds to CaM kinase III and the 102 kDa peptide to elongation factor 2 (EF-2), since the 102 kDa peptide was shown to undergo ADP-ribosylation in the presence of diphtheria toxin and NAD+.

Sign in / Sign up

Export Citation Format

Share Document