Document Detail


Laminin-211 in skeletal muscle function.
MedLine Citation:
PMID:  23154401     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A chain is no stronger than its weakest link is an old idiom that holds true for muscle biology. As the name implies, skeletal muscle's main function is to move the bones. However, for a muscle to transmit force and withstand the stress that contractions give rise to, it relies on a chain of proteins attaching the cytoskeleton of the muscle fiber to the surrounding extracellular matrix. The importance of this attachment is illustrated by a large number of muscular dystrophies caused by interruption of the cytoskeletal-extracellular matrix interaction. One of the major components of the extracellular matrix is laminin, a heterotrimeric glycoprotein and a major constituent of the basement membrane. It has become increasingly apparent that laminins are involved in a multitude of biological functions, including cell adhesion, differentiation, proliferation, migration and survival. This review will focus on the importance of laminin-211 for normal skeletal muscle function.
Authors:
Johan Holmberg; Madeleine Durbeej
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2012-11-15
Journal Detail:
Title:  Cell adhesion & migration     Volume:  7     ISSN:  1933-6926     ISO Abbreviation:  Cell Adh Migr     Publication Date:    2013 Jan-Feb
Date Detail:
Created Date:  2013-01-08     Completed Date:  2013-06-14     Revised Date:  2014-01-10    
Medline Journal Info:
Nlm Unique ID:  101469464     Medline TA:  Cell Adh Migr     Country:  United States    
Other Details:
Languages:  eng     Pagination:  111-21     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Basement Membrane / metabolism
Cell Survival
Dystroglycans / metabolism
Extracellular Matrix / metabolism
Humans
Laminin / genetics,  metabolism*
Mice
Muscle Contraction
Muscle Development*
Muscle, Skeletal / metabolism,  physiology*
Muscular Dystrophies / genetics,  metabolism,  pathology
Mutation
Protein Binding
Sarcolemma / metabolism,  pathology
Signal Transduction
Chemical
Reg. No./Substance:
0/Laminin; 0/laminin alpha 2; 146888-27-9/Dystroglycans
Comments/Corrections

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