Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-β receptor system Journal Article


Authors: López-Casillas, F.; Cheifetz, S.; Doody, J.; Andres, J. L.; Lane, W. S.; Massagué, J.
Article Title: Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-β receptor system
Abstract: We describe the primary structure of rat betaglycan, a polymorphic membrane-anchored proteoglycan with high affinity for transforming growth factor-β (TGF-β). As deduced from its cDNA sequence, the 853 amino acid core protein of betaglycan has an extracellular domain with clustered sites for potential attachment of glycosaminoglycan chains. These chains are dispensable for TGF-β binding to the core protein. The transmembrane region and the short cytoplasmic tail of betaglycan are very similar to these regions in human endoglin, an endothelial cell membrane glycoprotein involved in intercellular recognition. The ectodomain of betaglycan can be released as a soluble proteoglycan; a potential cleavage site near the transmembrane region is identical to the highly regulated cleavage site of the membrane-anchored transforming growth factor-α precursor. The unique features of betaglycan suggest important roles in cell interaction with TGF-β. © 1991.
Keywords: nonhuman; comparative study; animal; animal tissue; gene expression; transforming growth factor beta; membrane proteins; animalia; cloning, molecular; dna; amino acid sequence; molecular sequence data; rna, messenger; sequence alignment; membrane glycoproteins; rat; transforming growth factor beta receptor; receptors, transforming growth factor beta; base sequence; dna sequence; rats; fetus; beta glucan; blotting, northern; gene structure; receptors, cell surface; solubility; growth factor receptor; proteoglycans; proteoglycan; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.
Journal Title: Cell
Volume: 67
Issue: 4
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 1991-11-15
Start Page: 785
End Page: 795
Language: English
DOI: 10.1016/0092-8674(91)90073-8
PUBMED: 1657406
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 27 September 2019 -- Source: Scopus
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  1. Joan Massague
    389 Massague
  2. Jacqueline F Doody
    13 Doody