Characterization of the membrane-bound protein kinase C and its substrate proteins in canine cardiac sarcolemma

1986 ◽  
Vol 886 (1) ◽  
pp. 152-161 ◽  
Author(s):  
Shaohua Yuan ◽  
Amar K. Sen
1992 ◽  
Vol 70 (1) ◽  
pp. 81-85 ◽  
Author(s):  
Yi Qu ◽  
Joseph Torchia ◽  
Thanh Duc Phan ◽  
Po Hsiung Wu ◽  
Amar Kumar Sen

The endogenous substrate proteins of rat cardiac protein kinase C type I, II, and III isozymic forms were studied in rat cardiac sarcolemma. The 19-, 21-, 29-, 35-, and 95-kDa proteins were phosphorylated by both types II and III, but not type I. The extent of phosphorylation by individual protein kinase C isozymic forms was additive and equal to the extent of phosphorylation observed when a mixture of isozymic forms was employed. The extent of phosphorylation of the 21-kDa protein by type III was much higher than that by type II. These results suggest that the protein kinase C isozymes have preferences for specific endogenous substrate proteins. The phosphorylation of these endogenous substrate proteins by protein kinase C isozymes probably plays a role in cardiac cell functions.Key words: cardiac sarcolemma, protein kinase C isozymes, phosphorylation, substrate proteins.


1990 ◽  
Vol 265 (8) ◽  
pp. 4583-4591 ◽  
Author(s):  
J D Pearson ◽  
D B DeWald ◽  
W R Mathews ◽  
N M Mozier ◽  
H A Zürcher-Neely ◽  
...  

1992 ◽  
Vol 267 (14) ◽  
pp. 10011-10017
Author(s):  
J Grabarek ◽  
M Raychowdhury ◽  
K Ravid ◽  
K.C. Kent ◽  
P.J. Newman ◽  
...  

1994 ◽  
Vol 203 (1) ◽  
pp. 311-318 ◽  
Author(s):  
T. Nanmori ◽  
W. Taguchi ◽  
M. Kinugasa ◽  
Y. Oji ◽  
S. Sahara ◽  
...  

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