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Cell surface acetylcholinesterase molecules on multinucleated myotubes are clustered over the nucleus of origin.
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MedLine Citation:
PMID:  1469054     Owner:  NLM     Status:  MEDLINE    
Multinucleated skeletal muscle fibers are compartmentalized with respect to the expression and organization of several intracellular and cell surface proteins including acetylcholinesterase (AChE). Mosaic muscle fibers formed from homozygous myoblasts expressing two allelic variants of AChE preferentially translate and assemble the polypeptides in the vicinity of the nucleus encoding the mRNA (Rotundo, R. L. 1990. J. Cell Biol. 110:715-719). To determine whether the locally synthesized AChE molecules are targeted to specific regions of the myotube surface, primary quail myoblasts were mixed with mononucleated cells of the mouse muscle C2/C12 cell line and allowed to fuse, forming heterospecific mosaic myotubes. Cell surface enzyme was localized by immunofluorescence using an avian AChE-specific monoclonal antibody. HOECHST 33342 was used to distinguish between quail and mouse nuclei in myotubes. Over 80% of the quail nuclei exhibited clusters of cell surface AChE in mosaic quail-mouse myotubes, whereas only 4% of the mouse nuclei had adjacent quail AChE-positive regions of membrane, all of which were located next to a quail nucleus. In contrast, membrane proteins such as Na+/K+ ATPase, which are not restricted to specific regions of the myotube surface, are free to diffuse over the entire length of the fiber. These studies indicate that the AChE molecules expressed in multinucleated muscle fibers are preferentially transported and localized to regions of surface membrane overlying the nucleus of origin. This targeting could play an important role in establishing and maintaining specialized cell surface domains such as the neuromuscular and myotendinous junctions.
S G Rossi; R L Rotundo
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of cell biology     Volume:  119     ISSN:  0021-9525     ISO Abbreviation:  J. Cell Biol.     Publication Date:  1992 Dec 
Date Detail:
Created Date:  1993-01-27     Completed Date:  1993-01-27     Revised Date:  2013-05-31    
Medline Journal Info:
Nlm Unique ID:  0375356     Medline TA:  J Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1657-67     Citation Subset:  IM    
Department of Cell Biology and Anatomy, University of Miami School of Medicine, Florida 33101.
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MeSH Terms
Acetylcholinesterase / biosynthesis,  drug effects,  isolation & purification*
Biological Transport
Cell Compartmentation
Cell Fusion
Cell Membrane / drug effects,  enzymology
Cell Nucleus / ultrastructure
Cell Polarity*
Cells, Cultured
Collagenases / pharmacology
Fluorescent Antibody Technique
Gene Expression
Membrane Proteins / drug effects,  isolation & purification
Muscles / cytology,  enzymology*,  ultrastructure
Protein Conformation
Grant Support
Reg. No./Substance:
0/Membrane Proteins; EC; EC 3.4.24.-/Collagenases

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

Full Text
Journal Information
Journal ID (nlm-ta): J Cell Biol
Journal ID (publisher-id): J. Cell Biol.
ISSN: 0021-9525
ISSN: 1540-8140
Publisher: The Rockefeller University Press
Article Information
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Print publication date: Day: 2 Month: 12 Year: 1992
Volume: 119 Issue: 6
First Page: 1657 Last Page: 1667
ID: 2289756
Publisher Id: 93107165
PubMed Id: 1469054

Cell surface acetylcholinesterase molecules on multinucleated myotubes are clustered over the nucleus of origin

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