Hyaluronectin binds to laminin and blocks laminin-dependent process formation by astrocytes.
Neuroreport
; 6(15): 2037-40, 1995 Oct 23.
Article
in En
| MEDLINE
| ID: mdl-8580435
ABSTRACT
The interaction of hyaluronectin (HN), a hyaluronic acid-binding extracellular matrix (ECM) glycoprotein with two other ECM-associated molecules, laminin and fibronectin, was studied by ligand blot and solid phase ligand binding assays. Ligand blot analysis with biotin-labeled HN revealed a strong binding of HN to immobilized laminin and a weaker binding to fibronectin. Ligand binding studies indicated a concentration dependent, Ca(2+)-independent binding of HN to laminin. Binding of HN to laminin but not to fibronectin was resistant to increased salt concentrations indicating a non-electrostatic, protein-protein interaction of HN with laminin. The functional relevance of HN-laminin interaction was demonstrated by an inhibition of laminin-supported astroglial process formation by HN.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Astrocytes
/
Laminin
/
Hyaluronic Acid
Limits:
Animals
/
Humans
Language:
En
Journal:
Neuroreport
Journal subject:
NEUROLOGIA
Year:
1995
Document type:
Article
Affiliation country:
United States