An assessment of the role of protein kinase and zymogen granule phosphorylation during secretion by the rat exocrine pancreas

1979 ◽  
Vol 583 (4) ◽  
pp. 422-433 ◽  
Author(s):  
Douglas S. Lewis ◽  
Robert A. Ronzio
1994 ◽  
Vol 267 (1) ◽  
pp. G40-G51 ◽  
Author(s):  
S. D. Freedman ◽  
K. Sakamoto ◽  
G. A. Scheele

The in vivo and in vitro secretion of glycoprotein-2 (GP-2), a glycosyl phosphatidylinositol (GPI)-anchored protein from the rat exocrine pancreas, was characterized. GP-2 was secreted in a nonparallel manner compared with amylase, a marker of secretory enzymes. Attenuated GP-2 secretion correlated with hormones that stimulated exocytosis in acinar cells. Augmented GP-2 secretion correlated with hormones that stimulated fluid and bicarbonate secretion from ductal elements. Immunofluorescence studies identified an enriched pool of GP-2 tightly bound to the apical membranes of acinar cells in addition to zymogen granules. This non-zymogen granule pool appears to represent the source of GP-2 released from acinar cells in a nonparallel manner. With the use of dispersed pancreatic acini largely devoid of ductal elements, GP-2 release was found to be augmented by alkaline pH. Thus GP-2 secretion appears to be modulated by two discrete cellular processes: 1) delivery of prereleased GP-2 within zymogen granules to the ductal lumen by exocytic mechanisms and 2) enzymatic release of GPI-anchored GP-2 from the luminal membranes, a kinetic process that appears to be regulated by secretin- or carbachol-induced secretion of bicarbonate.


Pathobiology ◽  
1990 ◽  
Vol 58 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Sambasiva Rao ◽  
Anjana V. Yeldandi ◽  
Janardan K. Reddy

Pancreas ◽  
1990 ◽  
Vol 5 (5) ◽  
pp. 598-605 ◽  
Author(s):  
Yoshimitsu Ogami ◽  
Toshinari Kimura ◽  
Hajime Nawata

2010 ◽  
Vol 48 (08) ◽  
Author(s):  
N Azoitei ◽  
GV Pusapati ◽  
A Kleger ◽  
C Brunner ◽  
F Genze ◽  
...  

2013 ◽  
Vol 51 (08) ◽  
Author(s):  
A Becher ◽  
A Staab ◽  
F Genze ◽  
S Bobrovich ◽  
N Azoitei ◽  
...  
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