The N-terminal globular domain of the laminin alpha1 chain binds to alpha1beta1 and alpha2beta1 integrins and to the heparan sulfate-containing domains of perlecan

FEBS Lett. 1998 Jul 3;430(3):217-21. doi: 10.1016/s0014-5793(98)00601-2.

Abstract

The N-terminal domains VI plus V (62 kDa) and V alone (43 kDa) of the laminin alpha1 chain were obtained as recombinant products and shown to be folded into a native form by electron microscopy and immunological assays. Domain VI alone, which corresponds to an LN module, did not represent an autonomously folding unit in mammalian cells, however. Fragment alpha1VI/V, but not fragment alpha1V, bound to purified alpha1beta1 and alpha2beta1 integrins, to heparin, and to heparan sulfate-substituted domains I and V of perlecan. This localized the binding activities to the LN module, which contains two basic sequences suitable for heparin interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Heparan Sulfate Proteoglycans*
  • Heparitin Sulfate / chemistry
  • Heparitin Sulfate / metabolism*
  • Humans
  • Integrin alpha1beta1
  • Integrins / metabolism*
  • Laminin / chemistry*
  • Laminin / genetics
  • Laminin / metabolism*
  • Laminin / ultrastructure
  • Mice
  • Microscopy, Electron
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Folding
  • Proteoglycans / chemistry
  • Proteoglycans / metabolism*
  • Receptors, Collagen
  • Recombinant Fusion Proteins

Substances

  • Heparan Sulfate Proteoglycans
  • Integrin alpha1beta1
  • Integrins
  • Laminin
  • Peptide Fragments
  • Proteoglycans
  • Receptors, Collagen
  • Recombinant Fusion Proteins
  • perlecan
  • laminin A
  • Heparitin Sulfate