| First Author | Ponce-Castañeda MV | Year | 1998 |
| Journal | Biochim Biophys Acta | Volume | 1384 |
| Issue | 2 | Pages | 189-96 |
| PubMed ID | 9659379 | Mgi Jnum | J:48601 |
| Mgi Id | MGI:1271001 | Doi | 10.1016/s0167-4838(98)00033-8 |
| Citation | Ponce-Castaneda MV, et al. (1998) Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites. Biochim Biophys Acta 1384(2):189-96 |
| abstractText | 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. |
