Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2006-3-13
pubmed:abstractText
WARP is a novel member of the von Willebrand factor A domain superfamily of extracellular matrix proteins that is expressed by chondrocytes. WARP 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, WARP is highly specific for the chondrocyte pericellular microenvironment and co-localizes with perlecan, a prominent component of the chondrocyte pericellular region. WARP is present in the guanidine-soluble fraction of cartilage matrix extracts as a disulfide-bonded multimer, indicating that WARP is a strongly interacting component of the cartilage matrix. To investigate how WARP is integrated with the pericellular environment, we studied WARP binding to mouse perlecan using solid phase and surface plasmon resonance analysis. WARP 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 WARP 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7341-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16407285-Amino Acid Motifs, pubmed-meshheading:16407285-Animals, pubmed-meshheading:16407285-Cartilage, pubmed-meshheading:16407285-Cartilage, Articular, pubmed-meshheading:16407285-Cell Line, pubmed-meshheading:16407285-Chondrocytes, pubmed-meshheading:16407285-DNA, Complementary, pubmed-meshheading:16407285-Disulfides, pubmed-meshheading:16407285-Dose-Response Relationship, Drug, pubmed-meshheading:16407285-Extracellular Matrix, pubmed-meshheading:16407285-Extracellular Matrix Proteins, pubmed-meshheading:16407285-Heparan Sulfate Proteoglycans, pubmed-meshheading:16407285-Humans, pubmed-meshheading:16407285-Immunohistochemistry, pubmed-meshheading:16407285-Immunoprecipitation, pubmed-meshheading:16407285-In Situ Hybridization, pubmed-meshheading:16407285-Kinetics, pubmed-meshheading:16407285-Mice, pubmed-meshheading:16407285-Protein Binding, pubmed-meshheading:16407285-Protein Structure, Tertiary, pubmed-meshheading:16407285-RNA, Messenger, pubmed-meshheading:16407285-Recombinant Proteins, pubmed-meshheading:16407285-Surface Plasmon Resonance, pubmed-meshheading:16407285-Time Factors, pubmed-meshheading:16407285-Tissue Distribution, pubmed-meshheading:16407285-von Willebrand Factor
pubmed:year
2006
pubmed:articleTitle
WARP is a novel multimeric component of the chondrocyte pericellular matrix that interacts with perlecan.
pubmed:affiliation
Cell and Matrix Biology Research Unit, Murdoch Childrens Research Institute and Department of Paediatrics, University of Melbourne, Royal Children's Hospital, Flemington Road, Parkville, Victoria 3052, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't