Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes
- Autores
- Carvelli, Flavia Lorena; Bannoud, Nadia; Aguilera, Andrea Carolina; Morales, Carlos R.; Sosa Escudero, Miguel Angel
- Año de publicación
- 2010
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Fil: Carvelli, Flavia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Bannoud, Nadia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Aguilera, Andrea Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Morales, Carlos R.. McGill University; Canadá
Fil: Sosa Escudero, Miguel Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina - Materia
-
EPIDIDYMIS
LYSOSOMAL ENZYMES
CATION-DEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR
CASTRATION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/281032
Ver los metadatos del registro completo
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Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymesCarvelli, Flavia LorenaBannoud, NadiaAguilera, Andrea CarolinaMorales, Carlos R.Sosa Escudero, Miguel AngelEPIDIDYMISLYSOSOMAL ENZYMESCATION-DEPENDENT MANNOSE-6-PHOSPHATE RECEPTORCASTRATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1It 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.Fil: Carvelli, Flavia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Bannoud, Nadia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Aguilera, Andrea Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Morales, Carlos R.. McGill University; CanadáFil: Sosa Escudero, Miguel Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaWiley-liss, div John Wiley & Sons Inc.2010-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/281032Carvelli, Flavia Lorena; Bannoud, Nadia; Aguilera, Andrea Carolina; Morales, Carlos R.; Sosa Escudero, Miguel Angel; Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes; Wiley-liss, div John Wiley & Sons Inc.; Journal of Cellular Biochemistry; 110; 5; 8-2010; 1101-11100730-2312CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1002/jcb.22622info:eu-repo/semantics/altIdentifier/doi/10.1002/jcb.22622info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-26T10:04:13Zoai:ri.conicet.gov.ar:11336/281032instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-02-26 10:04:13.388CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes |
| title |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes |
| spellingShingle |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes Carvelli, Flavia Lorena EPIDIDYMIS LYSOSOMAL ENZYMES CATION-DEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR CASTRATION |
| title_short |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes |
| title_full |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes |
| title_fullStr |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes |
| title_full_unstemmed |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes |
| title_sort |
Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes |
| dc.creator.none.fl_str_mv |
Carvelli, Flavia Lorena Bannoud, Nadia Aguilera, Andrea Carolina Morales, Carlos R. Sosa Escudero, Miguel Angel |
| author |
Carvelli, Flavia Lorena |
| author_facet |
Carvelli, Flavia Lorena Bannoud, Nadia Aguilera, Andrea Carolina Morales, Carlos R. Sosa Escudero, Miguel Angel |
| author_role |
author |
| author2 |
Bannoud, Nadia Aguilera, Andrea Carolina Morales, Carlos R. Sosa Escudero, Miguel Angel |
| author2_role |
author author author author |
| dc.subject.none.fl_str_mv |
EPIDIDYMIS LYSOSOMAL ENZYMES CATION-DEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR CASTRATION |
| topic |
EPIDIDYMIS LYSOSOMAL ENZYMES CATION-DEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR CASTRATION |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
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. Fil: Carvelli, Flavia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina Fil: Bannoud, Nadia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina Fil: Aguilera, Andrea Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina Fil: Morales, Carlos R.. McGill University; Canadá Fil: Sosa Escudero, Miguel Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina |
| description |
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. |
| publishDate |
2010 |
| dc.date.none.fl_str_mv |
2010-08 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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http://hdl.handle.net/11336/281032 Carvelli, Flavia Lorena; Bannoud, Nadia; Aguilera, Andrea Carolina; Morales, Carlos R.; Sosa Escudero, Miguel Angel; Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes; Wiley-liss, div John Wiley & Sons Inc.; Journal of Cellular Biochemistry; 110; 5; 8-2010; 1101-1110 0730-2312 CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/281032 |
| identifier_str_mv |
Carvelli, Flavia Lorena; Bannoud, Nadia; Aguilera, Andrea Carolina; Morales, Carlos R.; Sosa Escudero, Miguel Angel; Castration induces changes in the cation-dependent mannose-6-phosphate receptor in rat epididymis: Possible implications in secretion of lysosomal enzymes; Wiley-liss, div John Wiley & Sons Inc.; Journal of Cellular Biochemistry; 110; 5; 8-2010; 1101-1110 0730-2312 CONICET Digital CONICET |
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eng |
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eng |
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Wiley-liss, div John Wiley & Sons Inc. |
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Wiley-liss, div John Wiley & Sons Inc. |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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