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WARP is a novel multimeric component of the chondrocyte pericellular matrix that interacts with perlecan.

J Biol Chem. 2006 Mar 17;281(11):7341-9. Epub 2006 Jan 06
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摘要


is a novel member of the von Willebrand factor A domain superfamily of extracellular matrix proteins that is expressed by chondrocytes. Wduanyu37 is restricted to the presumptive articular cartilage zone prior to joint cavitation and to the articular cartilage and fibrocartilaginous elements in the joint, spine, and sternum during mouse embryonic development. In mature articular cartilage, Wduanyu37 is highly specific for the chondrocyte pericellular microenvironment and co-localizes with perlecan, a prominent component of the chondrocyte pericellular region. Wduanyu37 is present in the guanidine-soluble fraction of cartilage matrix extracts as a disulfide-bonded multimer, indicating that Wduanyu37 is a strongly interacting component of the cartilage matrix. To investigate how Wduanyu37 is integrated with the pericellular environment, we studied Wduanyu37 binding to mouse perlecan using solid phase and surface plasmon resonance analysis. Wduanyu37 interacts with domain III-2 of the perlecan core protein and the heparan sulfate chains of the perlecan domain I with K(D) values in the low nanomolar range. We conclude that Wduanyu37 forms macromolecular structures that interact with perlecan to contribute to the assembly and/or maintenance of "permanent" cartilage structures during development and in mature cartilages.

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