The transforming growth factor-beta receptor type III is a membrane proteoglycan. Domain structure of the receptor.

Citation data:

The Journal of biological chemistry, ISSN: 0021-9258, Vol: 263, Issue: 32, Page: 16984-91

Publication Year:
1988
Usage 29
Abstract Views 29
Mentions 1
References 1
Citations 162
Citation Indexes 162
Repository URL:
https://escholarship.umassmed.edu/oapubs/888
PMID:
2903157
Author(s):
Cheifetz, Sela; Andres, Janet L.; Massague, Joan
Tags:
Biochemistry, Genetics and Molecular Biology; Affinity Labels; Animals; Cell Membrane; Chondroitin Lyases; Chromatography, Ion Exchange; Glycoside Hydrolases; Polysaccharide-Lyases; Rats; Receptors, Cell Surface; Receptors, Transforming Growth Factor beta; Trypsin; Tunicamycin; Life Sciences; Medicine and Health Sciences
article description
The transforming growth factor-beta (TGF-beta) receptor type III is a low abundance cell surface component that binds TGF-beta 1 and TGF-beta 2 with high affinity and specificity, and is present in many mammalian and avian cell types. Type III TGF-beta receptors affinity-labeled with 125I-TGF-beta migrate in sodium dodecyl sulfate-polyacrylamide electrophoresis gels as diffuse species of 250-350 kDa. Here we show that type III receptors deglycosylated by the action of trifluoromethanesulfonic acid yield affinity-labeled receptor cores of 110-130 kDa. This marked decrease in molecular weight is also achieved by combined treatment of type III receptors with heparitinase and chondroitinase ABC. Digestion of receptor-linked glycosaminoglycans by treatment of intact cell monolayers with heparitinase and chondroitinase does not prevent TGF-beta binding to the type III receptor core polypeptide and does not release the receptor polypeptide from the membrane. The type III TGF-beta receptor binds tightly to DEAE-Sephacel and coelutes with cellular proteoglycans at a characteristically high salt concentration. Thus, the type III TGF-beta receptor has the properties of a membrane proteoglycan that carries heparan and chondroitin sulfate glycosaminoglycan chains. The binding site for TGF-beta appears to reside in the 100-120-kDa core polypeptide of this receptor. The type III receptor is highly sensitive to cleavage by trypsin. Trypsin action releases the glycosaminoglycan-containing domain of the receptor leaving a 60-kDa membrane-associated domain that contains the cross-linked ligand. A model for the domain structure of the TGF-beta receptor type III is proposed based on these results.