Mouse myoblasts can fuse and form a normal sarcomere in the absence of beta1 integrin expression

J Cell Sci. 1998 Aug:111 ( Pt 16):2397-409. doi: 10.1242/jcs.111.16.2397.

Abstract

Antibody perturbation experiments suggested that migration, terminal differentiation and fusion of myoblasts are dependent on beta1 integrin expression. In addition, several studies have postulated that beta1 integrins have a role in the formation of sarcomeres. In the present report we have analysed skeletal myogenesis in wild-type/beta1-null chimeric mice and beta1-null embryoid bodies. Trunk and limbs of beta1-null chimeric mice contained muscle tissue composed of normal and beta1-null myoblasts indicating that all myotomic sublineages can form, migrate to their peripheral targets and fuse in the absence of beta1 integrin expression. Pure populations of beta1-null myoblasts and satellite cells isolated from beta1-null chimeric embryos and chimeric newborn mice, respectively, were able to differentiate in vitro and to fuse into multinucleated myotubes. Quantitative and qualitative comparisons between normal and beta1-null myoblasts revealed no apparent difference in their capacity to terminally differentiate and fuse. Furthermore, beta1-null myotubes developed sarcomeres which were indistinguishable from wild-type controls. When normal and beta1-null ES cells were differentiated into embryoid bodies, they contained fully differentiated myotubes with normal sarcomeres and normal deposition of costameric components. However, formation of beta1-null myotubes was delayed and was less efficient in beta1-null embryoid bodies than in wild-type controls. High expression of alphav integrin subunit at the tips of normal as well as beta1-null myotubes indicated that the lack of beta1 integrins did not result in a significant redistribution of alphav-containing receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Newborn
  • Antigens, CD / metabolism
  • Cell Differentiation
  • Cell Fusion / immunology
  • Cell Fusion / physiology
  • Cell Movement
  • Chimera
  • Cytoskeletal Proteins / metabolism
  • Dystroglycans
  • Immunohistochemistry
  • In Vitro Techniques
  • Integrin alpha Chains*
  • Integrin alphaV
  • Integrin beta1 / genetics
  • Integrin beta1 / physiology*
  • Membrane Glycoproteins / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Mice, Inbred DBA
  • Mice, Knockout
  • Microscopy, Electron
  • Muscle, Skeletal / cytology*
  • Muscle, Skeletal / immunology*
  • Sarcomeres / immunology*
  • Sarcomeres / ultrastructure*
  • Stem Cells / cytology
  • Stem Cells / immunology

Substances

  • Antigens, CD
  • Cytoskeletal Proteins
  • DAG1 protein, human
  • Integrin alpha Chains
  • Integrin alphaV
  • Integrin beta1
  • Membrane Glycoproteins
  • integrin alpha7
  • Dystroglycans