Expression of caveolin-1 in rat Leydig cells
Biocell
;
30(3): 431-438, dec. 2006. ilus
Artículo
en Inglés
| LILACS
| ID: lil-491542
ABSTRACT
Caveolin-1, the first member of caveolin family reported, is recognized as the structural component of caveola, a plasma membrane invagination or vesicles that are a subcompartment distinct from clathrin-coated pits. This protein is also known to be involved in cholesterol trafficking. The aim of this study was to determine the expression of caveolin-1 in adult rat Leydig cells. Testis sections incubated with an antibody to caveolin-1 showed, by immunohistochemistry, a moderate number of Leydig cells with different degrees of immunoreaction and a strong reaction in endothelial cells and in the lamina propia of seminiferous tubules.Caveolin- 1 was detected in the cell cytoplasm with a granular pattern and on the cell surface of Leydig cells cultured 24 h on uncoated, laminin-1 or type IV collagen coated coverslips. We also observed a milder reaction in 3 h cultures. Immunoreaction was also detected in Leydig cells with an antibody to tyrosine-phosphorylated caveolin-1. By double immunofluorescent technique, we observed co-localization of caveolin- I and 313-hydroxysteroid dehydrogenase. Western blot analysis revealed a band of about 22 kDa molecular weight that was recognized with both caveolin-1 and tyrosine-phosphocaveolin-1 antibodies. Caveolin-l is one of a few proteins with ademonstrated ability to bind cholesterol in vivo. In this context, the presence of caveolin- in Leydig cells may be related to cholesterol traffic--a rate limiting step in steroid biosynthesis.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Western Blotting
/
Colesterol
/
Caveolina 1
/
Células Intersticiales del Testículo
Límite:
Animales
Idioma:
Inglés
Revista:
Biocell
Asunto de la revista:
Clulas
Año:
2006
Tipo del documento:
Artículo
País de afiliación:
Argentina
Institución/País de afiliación:
Universidad de Buenos Aires/AR
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