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Disruption of perlecan binding and matrix assembly by post‐translational or genetic disruption of dystroglycan function
Author(s) -
Kanagawa Motoi,
Michele Daniel E.,
Satz Jakob S.,
Barresi Rita,
Kusano Hajime,
Sasaki Takako,
Timpl Rupert,
Henry Michael D.,
Campbell Kevin P.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.07.059
Subject(s) - perlecan , dystroglycan , chemistry , microbiology and biotechnology , function (biology) , matrix (chemical analysis) , genetics , biology , extracellular matrix , laminin , proteoglycan , chromatography
Dystroglycan is a cell‐surface matrix receptor that requires LARGE‐dependent glycosylation for laminin binding. Although the interaction of dystroglycan with laminin has been well characterized, less is known about the role of dystroglycan glycosylation in the binding and assembly of perlecan. We report reduced perlecan‐binding activity and mislocalization of perlecan in the LARGE‐deficient Large myd mouse. Cell‐surface ligand clustering assays show that laminin polymerization promotes perlecan assembly. Solid‐phase binding assays provide evidence for the first time of a trimolecular complex formation of dystroglycan, laminin and perlecan. These data suggest functional disruption of the trimolecular complex in glycosylation‐deficient muscular dystrophy.