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Fibromodulin and lumican bind to the same region on collagen type I fibrils
Author(s) -
Svensson Liz,
Närlid Ingmar,
Oldberg Åke
Publication year - 2000
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/s0014-5793(00)01314-4
Subject(s) - lumican , decorin , proteoglycan , chemistry , fibril , extracellular matrix , aggrecan , biochemistry , glycoprotein , microbiology and biotechnology , biglycan , biology , medicine , alternative medicine , pathology , osteoarthritis , articular cartilage
Fibromodulin and lumican are closely related members of the extracellular matrix leucine‐rich repeat glycoprotein/proteoglycan family. Similar to decorin, another member of this protein family, they bind to fibrillar collagens and function in the assembly of the collagen network in connective tissues. We have studied the binding of recombinant fibromodulin, lumican and decorin, expressed in mammalian cells, to collagen type I. Using a collagen fibril formation/sedimentation assay we show that fibromodulin inhibits the binding of lumican, and vice versa. Fibromodulin and lumican do not affect the binding of decorin to collagen, nor does decorin inhibit the binding of fibromodulin or lumican. Binding competition experiments and Scatchard plot analysis indicate that fibromodulin binds to collagen type I with higher affinity than lumican.