Fibroblast‐Derived J 1 Adhesion Glycoproteins Show Binding Properties to Extracellular Matrix Constituents Different from Those of Central Nervous System Origin

Rainer Probstmeier, Klaus Kühn, Melitta Schachner

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Abstract: The J 1 extracellular adhesion molecule from mouse brain consists of several immunochemically related glycoproteins of different molecular weights and distinct functional properties. Like the brain J 1 glycoproteins, the fibroblastderived J 1 glycoproteins interact with all collagen types tested (collagen G and type I–VI and IX), as measured by binding of 125I‐labeled J 1 glycoproteins to immobilized collagens. As tested for collagen type I, this binding can be inhibited more effectively by chondroitin sulfate than by heparin. After electrophoretic separation and transfer to nitrocellulose, fibroblast‐derived J 1 only binds to a limited number of collagen types (collagen types I, VI, and IX and G), whereas brainderived J 1 glycoproteins bind to all collagen types tested (collagen types I–VI and IX and G). These results show that fibroblast‐derived J 1 glycoproteins, although immunochemically related to J 1 glycoproteins from brain, differ from these in their binding specificities to extracellular matrix constituents.

Original languageEnglish (US)
Pages (from-to)1016-1019
Number of pages4
JournalJournal of neurochemistry
Volume54
Issue number3
DOIs
StatePublished - Mar 1990

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cellular and Molecular Neuroscience

Keywords

  • Adhesion
  • Chondroitin sulfate
  • Collagen
  • Extracellular matrix
  • Heparin
  • J 1 glycoproteins
  • Mouse.

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