Literature DB >> 9659379

Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites.

M V Ponce-Castañeda1, J Esparza-López, M M Vilchis-Landeros, V Mendoza, F López-Casillas.   

Abstract

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.

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Year:  1998        PMID： 9659379     DOI： 10.1016/s0167-4838(98)00033-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  5 in total

1.  Recombinant soluble betaglycan is a potent and isoform-selective transforming growth factor-beta neutralizing agent.

Authors:  M M Vilchis-Landeros; J L Montiel; V Mendoza; G Mendoza-Hernández; F López-Casillas
Journal:  Biochem J       Date:  2001-04-01       Impact factor: 3.857

Review 2.  Roles for the type III TGF-beta receptor in human cancer.

Authors:  Catherine E Gatza; Sun Young Oh; Gerard C Blobe
Journal:  Cell Signal       Date:  2010-02-12       Impact factor: 4.315

3.  Heart and liver defects and reduced transforming growth factor beta2 sensitivity in transforming growth factor beta type III receptor-deficient embryos.

Authors:  Kaye L Stenvers; Melinda L Tursky; Kenneth W Harder; Nicole Kountouri; Supavadee Amatayakul-Chantler; Dianne Grail; Clayton Small; Robert A Weinberg; Andrew M Sizeland; Hong-Jian Zhu
Journal:  Mol Cell Biol       Date:  2003-06       Impact factor: 4.272

4.  Betaglycan has two independent domains required for high affinity TGF-beta binding: proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor.

Authors:  Valentín Mendoza; M Magdalena Vilchis-Landeros; Guillermo Mendoza-Hernández; Tao Huang; Maria M Villarreal; Andrew P Hinck; Fernando López-Casillas; Jose-Luis Montiel
Journal:  Biochemistry       Date:  2009-12-15       Impact factor: 3.162

5.  Glucocorticoids recruit Tgfbr3 and Smad1 to shift transforming growth factor-β signaling from the Tgfbr1/Smad2/3 axis to the Acvrl1/Smad1 axis in lung fibroblasts.

Authors:  Julian T Schwartze; Simone Becker; Elpidoforos Sakkas; Łukasz A Wujak; Gero Niess; Jakob Usemann; Frank Reichenberger; Susanne Herold; István Vadász; Konstantin Mayer; Werner Seeger; Rory E Morty
Journal:  J Biol Chem       Date:  2013-12-17       Impact factor: 5.157
  5 in total

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