Document Detail


Folimycin (concanamycin A), a specific inhibitor of V-ATPase, blocks intracellular translocation of the glycoprotein of vesicular stomatitis virus before arrival to the Golgi apparatus.
MedLine Citation:
PMID:  8242793     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Folimycin (concanamycin A) specifically inhibited vacuolar-type ATPase as far as examined. Folimycin blocked excretion of the glycoprotein (G protein) of vesicular stomatitis virus into the medium and, instead, G protein was accumulated intracellularly. The intracellularly accumulated G protein electrophoresed a little faster than mature one. The N-glycan of the G protein was endoglycosidase H-sensitive, and terminal galactose and N-acetylglucosamine were not detected essentially on sequential digestion with exoglycosidases, indicating that processings known to occur in the Golgi apparatus do not take place in the presence of folimycin. The oligosaccharide chain of the G protein was determined to have a composition of Man8GlcNAc2 as analyzed by Bio-Gel P-4 column chromatography and high-performance liquid chromatography following digestion with alpha- and then with beta-mannosidase. Activities of mannosidase I and glycosyltransferases prepared from baby hamster kidney cells were not inhibited as far as examined, indicating that the incompleteness of the N-glycosidic chain in folimycin-treated cells is not caused by inhibition of processing enzymes. Taken together these observations suggest that folimycin blocks the intracellular translocation of G protein before the step of trimming by mannosidase I which is confined to the cis compartment of the Golgi. The intracellular localization of G protein as revealed by fluorescence microscopy was in good accordance with this assumption.
Authors:
M Muroi; N Shiragami; K Nagao; M Yamasaki; A Takatsuki
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell structure and function     Volume:  18     ISSN:  0386-7196     ISO Abbreviation:  Cell Struct. Funct.     Publication Date:  1993 Jun 
Date Detail:
Created Date:  1994-01-06     Completed Date:  1994-01-06     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  7608465     Medline TA:  Cell Struct Funct     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  139-49     Citation Subset:  IM    
Affiliation:
Department of Agricultural Chemistry, University of Tokyo, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anti-Bacterial Agents / pharmacology*
Biological Transport / drug effects
Cells, Cultured
Cricetinae
Glycosyltransferases / drug effects
Golgi Apparatus / metabolism
Macrolides*
Mannosidases / drug effects
Membrane Glycoproteins*
Microscopy, Fluorescence
Polysaccharides / metabolism
Proton-Translocating ATPases / antagonists & inhibitors
Rats
Saccharomyces cerevisiae
Vacuoles / enzymology
Vesicular stomatitis Indiana virus / drug effects*,  metabolism
Viral Envelope Proteins / drug effects*,  metabolism
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/G protein, vesicular stomatitis virus; 0/Macrolides; 0/Membrane Glycoproteins; 0/Polysaccharides; 0/Viral Envelope Proteins; 80890-47-7/concanamycin A; EC 2.4.-/Glycosyltransferases; EC 3.2.1.-/Mannosidases; EC 3.2.1.113/mannosyl-oligosaccharide 1,2-alpha-mannosidase; EC 3.6.3.14/Proton-Translocating ATPases

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


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