Hyaluronectin binds to laminin and blocks laminin-dependent process formation by astrocytes.
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.
Namboodiri
M S
MS
Department of Neurology, Medical University of South Carolina, Charleston 29425, USA.
Zhang
P
P
Bhat
N R
NR
D000818:Animals; D001253:Astrocytes / Q000378:metabolism*; D002478:Cells, Cultured / Q000378:metabolism; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism*; D007797:Laminin / Q000378:metabolism*; D011869:Radioligand Assay; D051381:Rats
D007797:Laminin; D006820:Hyaluronic Acid