Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites.
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.
Ponce-Castañeda
M V
MV
Departmento de Biología Celular, Universidad Nacional Autónoma de México, México City.
Esparza-López
J
J
Vilchis-Landeros
M M
MM
Mendoza
V
V
López-Casillas
F
F
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D006025:Glycosaminoglycans / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D009206:Myocardium / Q000378:metabolism; D011509:Proteoglycans / Q000235:genetics* / Q000378:metabolism; D018125:Receptors, Transforming Growth Factor beta / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D006025:Glycosaminoglycans; D011509:Proteoglycans; D018125:Receptors, Transforming Growth Factor beta; C071736:betaglycan