ISSN:
1040-452X
Keywords:
Betaglycan
;
Binding proteins
;
Cell surface proteins
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
Notes:
The nature and role of cell surface proteins that bind members of the TGF-β family has been investigated. TGF-β, activins, and BMPs each bind to receptors of 55 kDa (type I) and 70 kDa (type II). In the TGF-β system, these receptors are implicated in the mediation of multiple responses. A member of the type II receptor family has been cloned that encodes four alternatively spliced versions of a transmembrane serine/threonine kinase receptor related to the recently cloned mouse activin receptor and C-elegans daf-1 gene. Inhibitors of serine/threonine kinase activity block transcriptional and growth inhibitory responses to TGF-β. In addition to the signaling receptors, many cell types express the TGF-β binding proteoglycan betaglycan. Betaglycan has been purified, molecularly cloned, and shown to bind TGF-β via its core protein and basic fibroblast growth factor via its heparan sulfate chains. In addition to receptors I and II and betaglycan, some cells express a newly identified set of membrane proteins that specifically bind either TGF-β1 or TGF-β2. Three of the four isoform-restricted binding proteins are bound to the membrane via phospholipid anchors. Like betaglycan, these proteins might function to regulate the interaction between TGF-β and their target cells. © 1992 Wiley-Liss, Inc.
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/mrd.1080320204
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