Laminin-211 in skeletal muscle function.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3218932
- author
- Holmberg, Johan K LU and Durbeej-Hjalt, Madeleine LU
- organization
- publishing date
- 2012
- 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
- 2016-04-04 07:10:41
- date last changed
- 2018-11-21 20:48:13
@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.}},
url = {{http://www.ncbi.nlm.nih.gov/pubmed/23154401?dopt=Abstract}},
volume = {{7}},
year = {{2012}},
}