Chondroitin sulphate modification in the alpha4 chain of human recombinant laminin-8 (alpha4beta1gamma1)

Matrix Biol. 2002 Oct;21(6):483-6. doi: 10.1016/s0945-053x(02)00052-5.

Abstract

We have produced human laminin-8 (alpha4beta1gamma1) using recombinant technology. Approximately half of the recombinant laminin-8 (rLN-8) molecules were found to have a chondroitin sulphate modification in the alpha4 chain. The substituted and non-substituted forms were separated and tested for cell adhesion activity. Lower cell adhesion promoting activity was seen for the substituted form, but the integrin receptor utilization was similar. We also found the human rLN-8 to behave identically in cell adhesion assays compared to a human/mouse hybrid variant of rLN-8.

Publication types

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

MeSH terms

  • Animals
  • Cell Adhesion / physiology
  • Cell Line
  • Chondroitin Sulfates / chemistry*
  • Humans
  • Integrin alpha6beta1 / metabolism
  • Laminin / biosynthesis*
  • Laminin / chemistry*
  • Laminin / physiology
  • Mice
  • Protein Multimerization
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Integrin alpha6beta1
  • Laminin
  • Recombinant Proteins
  • laminin 8
  • Chondroitin Sulfates