WARP is a new member of the von Willebrand factor A-domain superfamily of extracellular matrix proteins

FEBS Lett. 2002 Apr 24;517(1-3):61-6. doi: 10.1016/s0014-5793(02)02579-6.

Abstract

We report a new member of the von Willebrand factor A-domain protein superfamily, WARP (for von Willebrand factor A-domain-related protein). 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cells, Cultured
  • Chondrocytes / metabolism*
  • Extracellular Matrix Proteins* / chemistry*
  • Extracellular Matrix Proteins* / isolation & purification
  • Fibroblasts / metabolism
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism*
  • Humans
  • Mice
  • Molecular Sequence Data
  • Osteoblasts / metabolism
  • RNA, Messenger / biosynthesis
  • Sequence Homology, Amino Acid
  • Transfection
  • von Willebrand Factor / chemistry*
  • von Willebrand Factor / metabolism

Substances

  • Extracellular Matrix Proteins
  • Glycoproteins
  • RNA, Messenger
  • VWA1 protein, human
  • WARP protein, mouse
  • von Willebrand Factor