Protein Phosphatase Inhibitors Potentiate Ca2+/Calmodulin-Dependent Protein Kinase II Activity in Rat Pancreatic Acinar Cells

1996 ◽  
Vol 225 (2) ◽  
pp. 520-524 ◽  
Author(s):  
Jason Hwang ◽  
M.Julia Bragado ◽  
Rui-Dong Duan ◽  
John A. Williams





1996 ◽  
Vol 44 (11) ◽  
pp. 1243-1250 ◽  
Author(s):  
L M Matovcik ◽  
A R Maranto ◽  
C J Soroka ◽  
F S Gorelick ◽  
J Smith ◽  
...  

The Type 3 inositol 1,4,5-trisphosphate (InsP3) receptor is expressed at high levels in gastrointestinal tissues. This receptor has 16 potential phosphorylation sites for calcium/calmodulin-dependent protein kinase II (CaM kinase II). To determine if the Type 3 InsP3 receptor is likely to be a physiologic substrate for CaM kinase II, localizations of the Type 3 InsP3 receptor and CaM kinase II were compared in tissues of the gastrointestinal tract. Cellular and subcellular localizations were determined by immunofluorescence microscopy in rat intestine, pancreas, and stomach, and in isolated rabbit gastric glands. Both proteins were found in the apical region of intestinal enterocytes, pancreatic acinar cells, and gastric parietal, chief, and surface mucous cells. CaM kinase II was found throughout the entire intracellular canalicular F-actin domain of parietal cells, whereas the type 3 InsP3 receptor was restricted to the neck region. Thus, in several gastrointestinal tissues the Type 3 InsP3 receptor is specifically localized to a portion of the apical cytoskeletal domain in which resides the calcium-responsive effector CaM kinase II.





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