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Laminin-211 in skeletal muscle function.

Holmberg, Johan K LU and Durbeej-Hjalt, Madeleine LU (2012) In Cell Adhesion and Migration 7(1).
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cell Adhesion and Migration
volume
7
issue
1
publisher
Landes Bioscience
external identifiers
  • wos:000313567700016
  • pmid:23154401
ISSN
1933-6918
language
English
LU publication?
yes
id
a643fd16-5687-4372-8df6-463b789bc65b (old id 3218932)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/23154401?dopt=Abstract
date added to LUP
2012-12-03 19:45:02
date last changed
2016-04-16 05:40:33
@article{a643fd16-5687-4372-8df6-463b789bc65b,
  abstract     = {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.},
  author       = {Holmberg, Johan K and Durbeej-Hjalt, Madeleine},
  issn         = {1933-6918},
  language     = {eng},
  number       = {1},
  publisher    = {Landes Bioscience},
  series       = {Cell Adhesion and Migration},
  title        = {Laminin-211 in skeletal muscle function.},
  volume       = {7},
  year         = {2012},
}