Detection of post-translational sulfation of alpha-5 beta-1 integrin and its role in integrin-fibronectin binding.
Braz J Med Biol Res
; 29(9): 1235-8, 1996 Sep.
Article
em En
| MEDLINE
| ID: mdl-9181068
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 of 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.
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Base de dados:
MEDLINE
Assunto principal:
Fibronectinas
/
Receptores de Fibronectina
Idioma:
En
Ano de publicação:
1996
Tipo de documento:
Article