Detection of post-translational sulfation of alpha(5)beta(1) integrin and its role in integrin-fibronectin binding

Detection of post-translational sulfation of alpha(5)beta(1) integrin and its role in integrin-fibronectin binding

Author Veiga, Silvio Sanches Autor UNIFESP Google Scholar
Elias, Maria Carolina Quartim Barbos Autor UNIFESP Google Scholar
Gremski, W. Google Scholar
Porcionatto, Marimélia Aparecida Autor UNIFESP Google Scholar
Nader, Helena Bonciani Autor UNIFESP Google Scholar
Brentani, Ricardo Renzo Autor UNIFESP Google Scholar
Institution INST LUDWIG PESQUISAS CANC
UNIV FED PARANA
Universidade Federal de São Paulo (UNIFESP)
Abstract Fibronectins are glycoproteins of the extracellular matrix composed of two 220-kDa polypeptide chains named A and B bound by two disulfide bridges, Both chains when digested with proteolytic enzymes give rise to six different domains named I to VI that are involved in the ligand properties of this molecule. Fibronectins bind fibrin, collagen, glycosaminoglycan residues and several integrins. In this study, using metabolic radiolabeling alpha(5) beta(1) integrin with sodium sulfate, an immunoprecipitation reaction, inhibition of sulfate incorporation and a fibronectin-binding assay, we were able to detect this integrin as a sulfated molecule and this sulfation appears to regulate the integrin-fibronectin binding.
Keywords alpha(5)beta(1) integrin
fibronectin
integrin sulfation
Language English
Date 1996-09-01
Published in Brazilian Journal Of Medical And Biological Research. Sao Paulo: Assoc Bras Divulg Cientifica, v. 29, n. 9, p. 1235-1238, 1996.
ISSN 0100-879X (Sherpa/Romeo, impact factor)
Publisher Assoc Bras Divulg Cientifica
Extent 1235-1238
Access rights Closed access
Type Article
Web of Science ID WOS:A1996VF23100019
URI http://repositorio.unifesp.br/11600/43116

Show full item record




File

File Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Search


Browse

Statistics

My Account