Beta 1 integrins mediate chondrocyte interaction with type I collagen, type II collagen, and fibronectin

Exp Cell Res. 1993 Apr;205(2):276-85. doi: 10.1006/excr.1993.1087.

Abstract

Chondrocytes isolated from the cephalic region of sterna from 14-day-old chick embryos used beta 1 integrins and required either Mg2+ or Mn2+ for attachment to plates coated with type I collagen, type II collagen, and fibronectin. beta 1 integrin was concentrated in adhesion plaques of the chondrocytes plated on type I collagen, type II collagen, and fibronectin substrates. Chondrocytes expressed at least 3 alpha-subunits, including alpha 3, alpha 5, and putative alpha 2. alpha 5, but not alpha 3, had a higher molecular weight in chondrocytes than in fibroblasts. Levels of alpha 3 and alpha 5 were about 25-30% of that in fibroblasts. When the chondrocytes were cultured in the presence of ascorbate in suspension, the cells aggregated into clusters. This aggregation was dependent on beta 1 integrin and type II collagen.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cartilage / metabolism*
  • Cell Adhesion
  • Chick Embryo
  • Collagen / metabolism*
  • Cytoskeletal Proteins / metabolism
  • Extracellular Matrix Proteins / metabolism
  • Fibronectins / metabolism*
  • In Vitro Techniques
  • Integrins / metabolism*
  • Molecular Sequence Data
  • Morphogenesis
  • Peptides / metabolism
  • Receptors, Cell Surface / metabolism

Substances

  • Cytoskeletal Proteins
  • Extracellular Matrix Proteins
  • Fibronectins
  • Integrins
  • Peptides
  • Receptors, Cell Surface
  • Collagen