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WARP is a new member of the von Willebrand factor A‐domain superfamily of extracellular matrix proteins
Author(s) -
Fitzgerald Jamie,
Tay Ting Su,
Bateman John F.
Publication year - 2002
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(02)02579-6
Subject(s) - fibronectin , glycoprotein , von willebrand factor , complementary dna , egf like domain , signal peptide , extracellular matrix , biology , peptide sequence , chemistry , microbiology and biotechnology , biochemistry , gene , immunology , platelet
We report a new member of the von illebrand factor A‐domain protein superfamily, WARP (for von illebrand factor ‐domain‐ elated rotein). The full‐length mouse WARP cDNA is 2.3 kb in size and predicts a protein of 415 amino acids which contains a signal sequence, a VA‐like domain, two fibronectin type III‐like repeats, and a short proline‐ and arginine‐rich segment. WARP mRNA was expressed predominantly in chondrocytes and in vitro expression experiments in transfected 293 cells indicated that WARP is a secreted glycoprotein that forms disulphide‐bonded oligomers. We conclude that WARP is a new member of the von Willebrand factor A‐domain (VA‐domain) superfamily of extracellular matrix proteins which may play a role in cartilage structure and function.