Document Detail


Disruption of endoplasmic reticulum to Golgi transport leads to the accumulation of large aggregates containing beta-COP in pancreatic acinar cells.
MedLine Citation:
PMID:  8507897     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
When transport between the rough endoplasmic reticulum (ER) and Golgi complex is blocked by Brefeldin A (BFA) treatment or ATP depletion, the Golgi apparatus and associated transport vesicles undergo a dramatic reorganization. Because recent studies suggest that coat proteins such as beta-COP play an important role in the maintenance of the Golgi complex, we have used immunocytochemistry to determine the distribution of beta-COP in pancreatic acinar cells (PAC) in which ER to Golgi transport was blocked by BFA treatment or ATP depletion. In controls, beta-COP was associated with Golgi cisternae and transport vesicles as expected. Upon BFA treatment, PAC Golgi cisternae are dismantled and replaced by clusters of remnant vesicles surrounded by typical ER transitional elements that are generally assumed to represent the exit site of vesicular carriers for ER to Golgi transport. In BFA-treated PAC, beta-COP was concentrated in large (0.5-1.0 micron) aggregates closely associated with remnant Golgi membranes. In addition to typical ER transitional elements, we detected a new type of transitional element that consists of specialized regions of rough ER (RER) with ribosome-free ends that touched or extended into the beta-COP containing aggregates. In ATP-depleted PAC, beta-COP was not detected on Golgi membranes but was concentrated in similar large aggregates found on the cis side of the Golgi stacks. The data indicate that upon arrest of ER to Golgi transport by either BFA treatment or energy depletion, beta-COP dissociates from PAC Golgi membranes and accumulates as large aggregates closely associated with specialized ER elements. The latter may correspond to either the site of entry or exit for vesicles recycling between the Golgi and the RER.
Authors:
L C Hendricks; M McCaffery; G E Palade; M G Farquhar
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular biology of the cell     Volume:  4     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  1993 Apr 
Date Detail:
Created Date:  1993-07-13     Completed Date:  1993-07-13     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  413-24     Citation Subset:  IM    
Affiliation:
Division of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Animals
Brefeldin A
Coatomer Protein
Cyclopentanes / pharmacology
Cytoplasm / chemistry,  metabolism
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum / drug effects,  metabolism*
Female
Golgi Apparatus / drug effects,  metabolism*
Immunohistochemistry
Male
Membrane Proteins / analysis,  metabolism*
Mice
Microscopy, Electron
Microtubule-Associated Proteins / analysis,  metabolism*
Pancreas / drug effects,  metabolism*,  ultrastructure
Rats
Rats, Sprague-Dawley
Grant Support
ID/Acronym/Agency:
CA-46128/CA/NCI NIH HHS; DK-17780/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Coatomer Protein; 0/Cyclopentanes; 0/Membrane Proteins; 0/Microtubule-Associated Proteins; 20350-15-6/Brefeldin A; 56-65-5/Adenosine Triphosphate
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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