Cell spreading on laminin substrate involves Con A-binding proteins

Reprod Nutr Dev. 1990;30(3):397-401. doi: 10.1051/rnd:19900312.

Abstract

Concanavalin A (Con A), a tetravalent lectin, was shown to impair 8 chick embryo fibroblast (8 d CEF) spreading on a laminin (LM) substrate but not on a fibronectin substrate (FN), suggesting that cell surface Con A binding proteins could be involved in 8 d CEF spreading on a LM substrate. The interaction of Con A-binding proteins with Con A is dependent upon the carbohydrate moieties of the isolated glycoproteins; since they interact strongly with Con A-Sepharose and are eluted with 0.3 Mol/l alpha-methylmannopyranoside, the isolated Con A binding-proteins inhibit 8 d CEF adhesion to a Con A substrate to the same extent as alpha-methylmannopyranoside. Furthermore, the isolated Con A binding proteins specifically inhibit in a dose-dependent manner 8 d CEF spreading on LM but not on FN.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Cell Adhesion / drug effects
  • Chick Embryo
  • Concanavalin A / pharmacology
  • Fibroblasts / cytology*
  • Fibroblasts / drug effects
  • Glycoproteins / physiology
  • Laminin*
  • Methylmannosides / pharmacology
  • Receptors, Concanavalin A / pharmacology
  • Receptors, Concanavalin A / physiology*

Substances

  • Glycoproteins
  • Laminin
  • Methylmannosides
  • Receptors, Concanavalin A
  • concanavalin A-binding glycoproteins
  • Concanavalin A
  • methylmannoside