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PMID: 9659379 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites.

Biochimica et biophysica acta ·Vol. 1384 ·No. 2 ·1998-05-19 ·Pages 189-96

Ponce-Castañeda MV, Esparza-López J, Vilchis-Landeros MM, Mendoza V, López-Casillas F

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Binding Sites Glycosaminoglycans/metabolism Mice Molecular Sequence Data Myocardium/metabolism Proteoglycans/genetics,metabolism Receptors, Transforming Growth Factor beta/genetics,metabolism Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Glycosaminoglycans Proteoglycans Receptors, Transforming Growth Factor beta betaglycan
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ponce-Castañeda M V
Departmento de Biología Celular, Universidad Nacional Autónoma de México, México City.
Esparza-López J
Vilchis-Landeros M M
Mendoza V
López-Casillas F
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1998-05-19
Pages
189-96
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Databases
GENBANK
AF039601
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