IHEM   20887
INSTITUTO DE HISTOLOGIA Y EMBRIOLOGIA DE MENDOZA DR. MARIO H. BURGOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Lysosomal proteins could be transported by alternative pathways in rat epididymal cells
Autor/es:
CARVELLI LORENA; BANNOUD NADIA; AGUILERA CAROLINA; MORALES CARLOS; SOSA ESCUDERO MIGUEL
Lugar:
Aguas de San Pedro- San Pablo
Reunión:
Congreso; Fifth International Conference on the Epididymis; 2010
Resumen:
The mammalian epididdymis is involved in the maturation of gametes ands its integrity and functionality depends on steroid hormones. The epididymal epithelium secretes protein into the lumen wich could be involved in sperm maturation. In the epididymis of mammals the secretions is enriched in acid hydrolase, an unsual fact, because these enzymes are normally confined to the lysosomal enviroment. In most celll types, the normal distribution of lysosomal enzymes is mediated by receptors that recognize mannnose-6-phosphate (MPRS). Two forms of these receptors have been decribed so far, cation-dependent (CD-MPR) and cation independent (CI-MPR). In some cell types, the CD-MPR participates in the secretion of lysosomal enzymes, while the CI-MPR is involved in the endocytosis of ligands. From previous results, we observed an increase in the expression and secretion of procathepsin D in rats deprived of androgens (castration), indicating that these events could be regulated by steroids hormones. Futhermore, it is well known tha the gene encoding Cathepsin D contains an element of response to estrogen, indicating that these hormones regulate the expression of these enzyme. Although procathepsin D is carried by the MPRs in most cells types, alternative routes have been proposed for transport to lysosomes. For example, in some cell types, procathepsin D complexes with prosaposin (a soluble lysosomal protein), wich are transported to lysosomes or realeased into the extracellular medium through the sortilin receptor.