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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/281032

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv 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
dc.language.none.fl_str_mv eng
language eng
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dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley-liss, div John Wiley & Sons Inc.
publisher.none.fl_str_mv Wiley-liss, div John Wiley & Sons Inc.
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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