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J. Biol. Chem., Vol. 263, Issue 32, 16984-16991, 11, 1988
S Cheifetz, JL Andres and J Massague
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.
The transforming growth factor-beta receptor type III is a membrane proteoglycan. Domain structure of the receptor
Department of Biochemistry, University of Massachusetts Medical School, Worcester 01655.
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