Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus
International audience Egg yolk constitutes the main storage compartment of the avian egg and the first nutritional source that supports embryonic growth. Most egg yolk components are synthesized by the liver of laying hens at sexual maturity and are secreted into the blood to be further transferred...
Published in: | Poultry Science |
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Online Access: | https://hal.inrae.fr/hal-02644821 https://hal.inrae.fr/hal-02644821/document https://hal.inrae.fr/hal-02644821/file/REHAULT-GODBERT_1 https://doi.org/10.3382/ps.2011-01910 |
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ftccsdartic:oai:HAL:hal-02644821v1 2023-05-15T13:40:57+02:00 Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus Bourin, Marie-Christine Gautron, Joël Berges, Magali Nys, Yves, Réhault-Godbert, Sophie Unité de Recherches Avicoles (URA) Institut National de la Recherche Agronomique (INRA) OVO-mining, ANR-09-BLAN-0136 2012 https://hal.inrae.fr/hal-02644821 https://hal.inrae.fr/hal-02644821/document https://hal.inrae.fr/hal-02644821/file/REHAULT-GODBERT_1 https://doi.org/10.3382/ps.2011-01910 en eng HAL CCSD Poultry Science Association info:eu-repo/semantics/altIdentifier/doi/10.3382/ps.2011-01910 hal-02644821 https://hal.inrae.fr/hal-02644821 https://hal.inrae.fr/hal-02644821/document https://hal.inrae.fr/hal-02644821/file/REHAULT-GODBERT_1 doi:10.3382/ps.2011-01910 PRODINRA: 170009 WOS: 000307680300026 info:eu-repo/semantics/OpenAccess ISSN: 0032-5791 Poultry Science https://hal.inrae.fr/hal-02644821 Poultry Science, Poultry Science Association, 2012, 91 (9), pp.2288-93. ⟨10.3382/ps.2011-01910⟩ liver chicken aspartic proteinase egg yolk enzyme foie poulet oeuf [SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology info:eu-repo/semantics/article Journal articles 2012 ftccsdartic https://doi.org/10.3382/ps.2011-01910 2021-08-07T23:02:52Z International audience Egg yolk constitutes the main storage compartment of the avian egg and the first nutritional source that supports embryonic growth. Most egg yolk components are synthesized by the liver of laying hens at sexual maturity and are secreted into the blood to be further transferred into the ovarian oocyte (yolky follicle) by receptor-mediated endocytosis. Egg yolk proteins are secreted as precursors and must undergo proteolytic processing to be bioactive. It is assumed that chicken cathepsin D, an aspartic protease; is a key enzyme in this process. Very recently, a novel aspartic protease, namely "similar to nothepsin," has been identified in the egg yolk. Previous experiments conducted in Antarctic fish have shown that the expression of nothepsin is tissue- and sex-specific. To gain insight into the specificities of expression of both cathepsin D and "similar to nothepsin" in Gallus gallus, we compared their distribution in various tissues, in male and females. Cathepsin D is ubiquitously expressed in all tissues examined, including liver of both male and female adults, and its expression is stable during sexual maturation. In contrast, "similar to nothepsin" expression is unique to the liver of adult females and is sex steroid-dependent as it increases gradually in the liver of hens during sexual maturation. The sexual dimorphic expression of the "similar to nothepsin" gene suggests that the activity of this protein is regulated by the steroid environment of laying hens and is specifically adapted for inclusion in the yolk. Further studies are needed to assess whether "similar to nothepsin" assists cathepsin D in the proteolytic processing of egg yolk proteins during follicular growth. Article in Journal/Newspaper Antarc* Antarctic Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Antarctic Poultry Science 91 9 2288 2293 |
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Open Polar |
collection |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
English |
topic |
liver chicken aspartic proteinase egg yolk enzyme foie poulet oeuf [SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology |
spellingShingle |
liver chicken aspartic proteinase egg yolk enzyme foie poulet oeuf [SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology Bourin, Marie-Christine Gautron, Joël Berges, Magali Nys, Yves, Réhault-Godbert, Sophie Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus |
topic_facet |
liver chicken aspartic proteinase egg yolk enzyme foie poulet oeuf [SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology |
description |
International audience Egg yolk constitutes the main storage compartment of the avian egg and the first nutritional source that supports embryonic growth. Most egg yolk components are synthesized by the liver of laying hens at sexual maturity and are secreted into the blood to be further transferred into the ovarian oocyte (yolky follicle) by receptor-mediated endocytosis. Egg yolk proteins are secreted as precursors and must undergo proteolytic processing to be bioactive. It is assumed that chicken cathepsin D, an aspartic protease; is a key enzyme in this process. Very recently, a novel aspartic protease, namely "similar to nothepsin," has been identified in the egg yolk. Previous experiments conducted in Antarctic fish have shown that the expression of nothepsin is tissue- and sex-specific. To gain insight into the specificities of expression of both cathepsin D and "similar to nothepsin" in Gallus gallus, we compared their distribution in various tissues, in male and females. Cathepsin D is ubiquitously expressed in all tissues examined, including liver of both male and female adults, and its expression is stable during sexual maturation. In contrast, "similar to nothepsin" expression is unique to the liver of adult females and is sex steroid-dependent as it increases gradually in the liver of hens during sexual maturation. The sexual dimorphic expression of the "similar to nothepsin" gene suggests that the activity of this protein is regulated by the steroid environment of laying hens and is specifically adapted for inclusion in the yolk. Further studies are needed to assess whether "similar to nothepsin" assists cathepsin D in the proteolytic processing of egg yolk proteins during follicular growth. |
author2 |
Unité de Recherches Avicoles (URA) Institut National de la Recherche Agronomique (INRA) OVO-mining, ANR-09-BLAN-0136 |
format |
Article in Journal/Newspaper |
author |
Bourin, Marie-Christine Gautron, Joël Berges, Magali Nys, Yves, Réhault-Godbert, Sophie |
author_facet |
Bourin, Marie-Christine Gautron, Joël Berges, Magali Nys, Yves, Réhault-Godbert, Sophie |
author_sort |
Bourin, Marie-Christine |
title |
Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus |
title_short |
Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus |
title_full |
Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus |
title_fullStr |
Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus |
title_full_unstemmed |
Sex- and tissue-specific expression of “similar to nothepsin” and cathepsin D in relation to egg yolk formation in Gallus gallus |
title_sort |
sex- and tissue-specific expression of “similar to nothepsin” and cathepsin d in relation to egg yolk formation in gallus gallus |
publisher |
HAL CCSD |
publishDate |
2012 |
url |
https://hal.inrae.fr/hal-02644821 https://hal.inrae.fr/hal-02644821/document https://hal.inrae.fr/hal-02644821/file/REHAULT-GODBERT_1 https://doi.org/10.3382/ps.2011-01910 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
ISSN: 0032-5791 Poultry Science https://hal.inrae.fr/hal-02644821 Poultry Science, Poultry Science Association, 2012, 91 (9), pp.2288-93. ⟨10.3382/ps.2011-01910⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.3382/ps.2011-01910 hal-02644821 https://hal.inrae.fr/hal-02644821 https://hal.inrae.fr/hal-02644821/document https://hal.inrae.fr/hal-02644821/file/REHAULT-GODBERT_1 doi:10.3382/ps.2011-01910 PRODINRA: 170009 WOS: 000307680300026 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.3382/ps.2011-01910 |
container_title |
Poultry Science |
container_volume |
91 |
container_issue |
9 |
container_start_page |
2288 |
op_container_end_page |
2293 |
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1766143819471912960 |