Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/43116
Title: Detection of post-translational sulfation of alpha(5)beta(1) integrin and its role in integrin-fibronectin binding
Authors: Veiga, Silvio Sanches [UNIFESP]
Elias, Maria Carolina Quartim Barbos [UNIFESP]
Gremski, W.
Porcionatto, Marimélia Aparecida [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
INST LUDWIG PESQUISAS CANC
UNIV FED PARANA
Universidade Federal de São Paulo (UNIFESP)
Keywords: alpha(5)beta(1) integrin
fibronectin
integrin sulfation
Issue Date: 1-Sep-1996
Publisher: Assoc Bras Divulg Cientifica
Citation: Brazilian Journal Of Medical And Biological Research. Sao Paulo: Assoc Bras Divulg Cientifica, v. 29, n. 9, p. 1235-1238, 1996.
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.
URI: http://repositorio.unifesp.br/11600/43116
ISSN: 0100-879X
Appears in Collections:Artigo

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