BINDING of SEX-HORMONE-BINDING GLOBULIN (SHBG) TO TESTICULAR MEMBRANES and SOLUBILIZED RECEPTORS

BINDING of SEX-HORMONE-BINDING GLOBULIN (SHBG) TO TESTICULAR MEMBRANES and SOLUBILIZED RECEPTORS

Autor Porto, C. S. Google Scholar
Abreu, L. C. Google Scholar
Gunsalus, G. L. Google Scholar
Bardin, C. W. Google Scholar
Instituição POPULAT COUNCIL
Universidade Federal de São Paulo (UNIFESP)
Resumo Sex-hormone-binding globulin (SHBG) binds to a specific protein on the surface of prostate, epididymis, and a human breast cancer cell line (MCF-7), and is internalized by these cells. the present study demonstrated specific binding of SHBG to receptor on membranes prepared from rat testes. the binding was saturable, specific, and time and temperature dependent. Scatchard analysis of these binding studies suggested that SHBG binds to a single class of sites on testicular membranes with a K(d) at 37-degrees-C of 5 X 10(-8) M and a binding capacity of 30 +/- 0.6 pmol/mg protein. These binding characteristics are similar to the SHBG receptor on human prostate and MCF-7 cells. Solubilization of the receptor resulted in a 5-fold increase in its binding capacity (158 +/- 0.3 pmol/mg protein) and a 10-fold decrease in binding affinity (K(d) at 37-degrees-C = 6.5 X 10(-7) M). the apparent molecular weight of the testicular SHBG receptor, as estimated by gel filtration, was M(r) = 174,000. Conclusion: a specific binding site for SHBG was identified on testicular membranes. This binding site has been tentatively identified as a SHBG receptor based on its physical properties in testicular membrane preparations and following solubilization.
Palavra-chave CELL RECEPTOR
SEX-HORMONE-BINDING GLOBULIN
ANDROGEN-BINDING PROTEIN
MEMBRANE
(RAT TESTIS)
Idioma Inglês
Data de publicação 1992-11-01
Publicado em Molecular and Cellular Endocrinology. Clare: Elsevier Sci Ireland Ltd, v. 89, n. 1-2, p. 33-38, 1992.
ISSN 0303-7207 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 33-38
Fonte http://dx.doi.org/10.1016/0303-7207(92)90208-N
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1992JX32600005
Endereço permanente http://repositorio.unifesp.br/handle/11600/25284

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