IHEM   20887
INSTITUTO DE HISTOLOGIA Y EMBRIOLOGIA DE MENDOZA DR. MARIO H. BURGOS
Unidad Ejecutora - UE
artículos
Título:
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: possible implications in secretion of lysosomal enzymes.
Autor/es:
CARVELLI LORENA; BANNOUD NADIA; AGUILERA CAROLINA; MORALES CARLOS; SOSA ESCUDERO MIGUEL
Revista:
JOURNAL OF CELLULAR BIOCHEMISTRY
Editorial:
WILEY-LISS, DIV JOHN WILEY & SONS INC
Referencias:
Lugar: New York; Año: 2010 vol. 110 p. 1101 - 1110
ISSN:
0730-2312
Resumen:
It is believed that the mammalian epididymis participates in the maturation of the sperm due to its secretory activity. High concentrations of several secreted acid hydrolases are found in the epididymal lumen. Moreover, some of these enzymes are secreted by the epididymal epithelium in an androgen-dependent fashion. In this study, we attempted to discern whether mannose-6-phosphate receptors (MPRs) regulate transport and secretion of lysosomal enzymes in the rat epididymis, and if these events are altered when the animals are subjected to hormonal manipulation. We observed that expression of cation-dependent MPR (CD-MPR) and cation-independent MPR (CI-MPR) increased significantly in caudal epididymis of castrated rats by immunoblot. This increase was corroborated by quantitation of MPRs, by binding assays. This change could be due to androgen deprivation, as a similar effect was observed after treatment with the anti-androgenic drug flutamide. Furthermore, we observed that the CD-MPR was redistributed to the apical area of the epithelium on castrated rats by immunohistochemistry, which is compatible with the redistribution of the receptors toward lighter fractions in a Percoll gradient. Consistent with a possible involvement of the CD-MPR in the secretion, we observed an increase in pro-cathepsin D levels in epididymal fluid after castration. We conclude that the CD-MPR might be regulated by hormones and that this receptor might be involved in the secretion of specific enzymes into the rat epididymis