Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites

Biochim Biophys Acta. 1998 May 19;1384(2):189-96. doi: 10.1016/s0167-4838(98)00033-8.

Abstract

The primary structure of murine betaglycan, also known as transforming growth factor beta (TGF-beta) type III receptor, was deduced from the nucleotide sequence of a cDNA clone isolated from a heart library. Murine betaglycan is a single spanning membrane polypeptide of 850 amino acids which is highly similar to betaglycan of other species. Transfection of this cDNA into COS1 cells resulted in the expression of a membrane proteoglycan that binds TGF-beta and is recognized by antibodies raised against rat betaglycan. COS1 cells transfected with the double mutant Ser533Ala; Ser544Ala of the murine betaglycan cDNA produced a TGF-beta type III receptor devoid of glycosaminoglycan chains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Glycosaminoglycans / metabolism*
  • Mice
  • Molecular Sequence Data
  • Myocardium / metabolism
  • Proteoglycans / genetics*
  • Proteoglycans / metabolism
  • Receptors, Transforming Growth Factor beta / genetics*
  • Receptors, Transforming Growth Factor beta / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Glycosaminoglycans
  • Proteoglycans
  • Receptors, Transforming Growth Factor beta
  • betaglycan

Associated data

  • GENBANK/AF039601