Laminin-211 in skeletal muscle function

Cell Adh Migr. 2013 Jan-Feb;7(1):111-21. doi: 10.4161/cam.22618. Epub 2012 Nov 15.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Basement Membrane / metabolism
  • Cell Survival
  • Dystroglycans / metabolism
  • Extracellular Matrix / metabolism
  • Humans
  • Laminin / genetics
  • Laminin / metabolism*
  • Mice
  • Muscle Contraction
  • Muscle Development*
  • Muscle, Skeletal / metabolism
  • Muscle, Skeletal / physiology*
  • Muscular Dystrophies / genetics
  • Muscular Dystrophies / metabolism
  • Muscular Dystrophies / pathology
  • Mutation
  • Protein Binding
  • Sarcolemma / metabolism
  • Sarcolemma / pathology
  • Signal Transduction

Substances

  • Laminin
  • laminin alpha 2
  • Dystroglycans