[HTML][HTML] Fibromodulin and lumican bind to the same region on collagen type I fibrils

L Svensson, I Närlid, Å Oldberg - FEBS letters, 2000 - Elsevier
L Svensson, I Närlid, Å Oldberg
FEBS letters, 2000Elsevier
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 …
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.
Elsevier