Open Access

ARTICLE

Expression of caveolin-1 in rat Leydig cells

MARTA B. CASANOVA, LIVIA LUSTIG, EMILCE S. DIAZ, ELIANA H. PELLIZZARI*, SELVA B. CIGORRAGA*, BERTA DENDUCHIS

Centro de Investigaciones en Reproducción, Facultad de Medicina, Universidad de Buenos Aires.
* Centro de Investigaciones Endocrinológicas, Hospital de Niños “Ricardo Gutierrez”, Ciudad Autónoma de Buenos Aires, Argentina.
Address correspondence to: Dra. Berta Denduchis. Centro de Investigaciones en Reproducción. Facultad de Medicina, Universidad de Buenos Aires. Paraguay 2155, piso 10, C1121ABG Buenos Aires, ARGENTINA. E-mail: ciruba@fmed.uba.ar

BIOCELL 2006, 30(3), 431-438. https://doi.org/10.32604/biocell.2006.30.431

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-1 and 3β-hydroxysteroid dehydrogenase. Western blot analysis revealed a band of about 22 kDa molecular weight that was recognized with both caveolin-1 and tyrosinephosphocaveolin-1 antibodies. Caveolin-1 is one of a few proteins with a demonstrated ability to bind cholesterol in vivo. In this context, the presence of caveolin-1 in Leydig cells may be related to cholesterol traffic -a rate limiting step in steroid biosynthesis.

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