scholarly journals Identification and Characterization of Carboxyl Ester Hydrolase as a Phospholipid Hydrolyzing Enzyme of Zymogen Granule Membranes from Rat Exocrine Pancreas

1995 ◽  
Vol 270 (8) ◽  
pp. 3780-3787 ◽  
Author(s):  
Matthew Withiam-Leitch ◽  
Ronald P. Rubin ◽  
Svetlana E. Koshlukova ◽  
John M. Aletta
Keyword(s):  
Exocrine Pancreas ◽  
Zymogen Granule ◽  
Ester Hydrolase ◽  
Rat Exocrine Pancreas ◽  
Carboxyl Ester Hydrolase ◽  
Identification And Characterization

Nonparallel secretion of GP-2 from exocrine pancreas implies luminal coupling between acinar and duct cells

1994 ◽  
Vol 267 (1) ◽  
pp. G40-G51 ◽  
Author(s):  
S. D. Freedman ◽  
K. Sakamoto ◽  
G. A. Scheele
Keyword(s):  
Exocrine Pancreas ◽  
Acinar Cells ◽  
Zymogen Granule ◽  
Zymogen Granules ◽  
Pancreatic Acini ◽  
Glycosyl Phosphatidylinositol ◽  
Cellular Processes ◽  
Rat Exocrine Pancreas

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.

Biosynthesis, segregation, and secretion of exportable proteins by the exocrine pancreas

1980 ◽  
Vol 238 (6) ◽  
pp. G467-G477
Author(s):  
G. A. Scheele
Keyword(s):  
Gel Electrophoresis ◽  
Exocrine Pancreas ◽  
Secretory Process ◽  
Secretory Proteins ◽  
Two Dimensional Gel Electrophoresis ◽  
Pancreatic Exocrine ◽  
Exocrine Cell ◽  
Identification And Characterization ◽  
Intracellular Pathway

Recent findings that contribute to an understanding of the secretory process in the pancreatic exocrine cell are reviewed. These include 1) the separation, identification, and characterization of secreted proteins by two-dimensional gel electrophoresis, 2) the intracellular route and timetable of movement of secretory proteins from one intracellular compartment to another, 3) the evidence that suggests that all enzymes and zymogens secreted by the pancreas are segregated and transported within a single intracellular pathway, and 4) the mechanism by which presecretory proteins are thought to be transported across the lipid bilayer of the rough endoplasmic reticulum (the transport peptide hypothesis).

Sign in / Sign up

Export Citation Format

Share Document