Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum

Autores
Pierre, Alice; Racine, Chrystèle; Rey, Rodolfo Alberto; Fanchin, Renato; Taieb, Joëlle; Cohen Tannoudji, Joëlle; Carmillo, Paul; Pepinsky, R. Blake; Cate, Richard L.; Di Clemente, Nathalie
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Context: Anti-Müllerian hormone (AMH) is an important clinical marker for diagnosing and assessing the reproductive status and/or disorders in men and women. Most studies have not distinguished between levels of inactive AMH precursor and the cleaved noncovalent complex that binds the AMH type II receptor (AMHRII) and initiates signaling. Objective: The objective of the study was to measure the levels of AMH cleavage and bioactivity in human body fluids. Design, Setting, and Patients: AMH cleavage levels and bioactivity were measured in the serum of six boys and in the follicular fluid and serum of nine control women and 13 women with the polycystic ovary syndrome (PCOS). Main Outcome Measures: AMH cleavage levels were measured by capturing AMH with an anti- AMH antibody, followed by Western blotting. The bioactivity of cleaved AMH was assessed with an ELISA that measures the levels of AMH capable of binding AMHRII. Results: PCOS women have an elevated level of AMH cleavage in their follicular fluid (24% vs 8% in controlwomen),andmostofthecleavedAMHcanbindAMHRII.Higherlevels of cleavage areobserved in female (60%) and male (79%) serum, but very little of the cleaved AMH can bind AMHRII. Conclusions: These results support an autocrine role for AMH in the pathophysiology of PCOS in the follicle. In addition,theyindicate thatAMHundergoesinteractions or structuralchangesaftercleavage that prevent receptor binding, meaning, unexpectedly, that the level of cleaved AMH in biological fluids does not always reflect the level of bioactive AMH.
Fil: Pierre, Alice. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Racine, Chrystèle. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Rey, Rodolfo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina
Fil: Fanchin, Renato. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Taieb, Joëlle. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Cohen Tannoudji, Joëlle. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Carmillo, Paul. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Pepinsky, R. Blake. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Cate, Richard L.. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Di Clemente, Nathalie. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Materia
AMH
Cleavage
PCOS
testis
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:11336/86111
Acceder
id CONICETDig_a383e912c8213854b267f0bc80e66c9f
oai_identifier_str oai:ri.conicet.gov.ar:11336/86111
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serumPierre, AliceRacine, ChrystèleRey, Rodolfo AlbertoFanchin, RenatoTaieb, JoëlleCohen Tannoudji, JoëlleCarmillo, PaulPepinsky, R. BlakeCate, Richard L.Di Clemente, NathalieAMHCleavagePCOStestishttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Context: Anti-Müllerian hormone (AMH) is an important clinical marker for diagnosing and assessing the reproductive status and/or disorders in men and women. Most studies have not distinguished between levels of inactive AMH precursor and the cleaved noncovalent complex that binds the AMH type II receptor (AMHRII) and initiates signaling. Objective: The objective of the study was to measure the levels of AMH cleavage and bioactivity in human body fluids. Design, Setting, and Patients: AMH cleavage levels and bioactivity were measured in the serum of six boys and in the follicular fluid and serum of nine control women and 13 women with the polycystic ovary syndrome (PCOS). Main Outcome Measures: AMH cleavage levels were measured by capturing AMH with an anti- AMH antibody, followed by Western blotting. The bioactivity of cleaved AMH was assessed with an ELISA that measures the levels of AMH capable of binding AMHRII. Results: PCOS women have an elevated level of AMH cleavage in their follicular fluid (24% vs 8% in controlwomen),andmostofthecleavedAMHcanbindAMHRII.Higherlevels of cleavage areobserved in female (60%) and male (79%) serum, but very little of the cleaved AMH can bind AMHRII. Conclusions: These results support an autocrine role for AMH in the pathophysiology of PCOS in the follicle. In addition,theyindicate thatAMHundergoesinteractions or structuralchangesaftercleavage that prevent receptor binding, meaning, unexpectedly, that the level of cleaved AMH in biological fluids does not always reflect the level of bioactive AMH.Fil: Pierre, Alice. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; FranciaFil: Racine, Chrystèle. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; FranciaFil: Rey, Rodolfo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; ArgentinaFil: Fanchin, Renato. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; FranciaFil: Taieb, Joëlle. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; FranciaFil: Cohen Tannoudji, Joëlle. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; FranciaFil: Carmillo, Paul. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; ArgentinaFil: Pepinsky, R. Blake. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; ArgentinaFil: Cate, Richard L.. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; FranciaFil: Di Clemente, Nathalie. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; FranciaEndocrine Society2016-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/86111Pierre, Alice; Racine, Chrystèle; Rey, Rodolfo Alberto; Fanchin, Renato; Taieb, Joëlle; et al.; Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum; Endocrine Society; Journal of Clinical Endocrinology and Metabolism; 101; 12; 12-2016; 4618-46270021-972XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1210/jc.2016-1742info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jcem/article/101/12/4618/2765023info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:46:11Zoai:ri.conicet.gov.ar:11336/86111instacron: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:34982025-09-03 09:46:12.446CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
title Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
spellingShingle Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
Pierre, Alice
AMH
Cleavage
PCOS
testis
title_short Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
title_full Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
title_fullStr Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
title_full_unstemmed Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
title_sort Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum
dc.creator.none.fl_str_mv Pierre, Alice
Racine, Chrystèle
Rey, Rodolfo Alberto
Fanchin, Renato
Taieb, Joëlle
Cohen Tannoudji, Joëlle
Carmillo, Paul
Pepinsky, R. Blake
Cate, Richard L.
Di Clemente, Nathalie
author Pierre, Alice
author_facet Pierre, Alice
Racine, Chrystèle
Rey, Rodolfo Alberto
Fanchin, Renato
Taieb, Joëlle
Cohen Tannoudji, Joëlle
Carmillo, Paul
Pepinsky, R. Blake
Cate, Richard L.
Di Clemente, Nathalie
author_role author
author2 Racine, Chrystèle
Rey, Rodolfo Alberto
Fanchin, Renato
Taieb, Joëlle
Cohen Tannoudji, Joëlle
Carmillo, Paul
Pepinsky, R. Blake
Cate, Richard L.
Di Clemente, Nathalie
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv AMH
Cleavage
PCOS
testis
topic AMH
Cleavage
PCOS
testis
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Context: Anti-Müllerian hormone (AMH) is an important clinical marker for diagnosing and assessing the reproductive status and/or disorders in men and women. Most studies have not distinguished between levels of inactive AMH precursor and the cleaved noncovalent complex that binds the AMH type II receptor (AMHRII) and initiates signaling. Objective: The objective of the study was to measure the levels of AMH cleavage and bioactivity in human body fluids. Design, Setting, and Patients: AMH cleavage levels and bioactivity were measured in the serum of six boys and in the follicular fluid and serum of nine control women and 13 women with the polycystic ovary syndrome (PCOS). Main Outcome Measures: AMH cleavage levels were measured by capturing AMH with an anti- AMH antibody, followed by Western blotting. The bioactivity of cleaved AMH was assessed with an ELISA that measures the levels of AMH capable of binding AMHRII. Results: PCOS women have an elevated level of AMH cleavage in their follicular fluid (24% vs 8% in controlwomen),andmostofthecleavedAMHcanbindAMHRII.Higherlevels of cleavage areobserved in female (60%) and male (79%) serum, but very little of the cleaved AMH can bind AMHRII. Conclusions: These results support an autocrine role for AMH in the pathophysiology of PCOS in the follicle. In addition,theyindicate thatAMHundergoesinteractions or structuralchangesaftercleavage that prevent receptor binding, meaning, unexpectedly, that the level of cleaved AMH in biological fluids does not always reflect the level of bioactive AMH.
Fil: Pierre, Alice. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Racine, Chrystèle. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Rey, Rodolfo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina
Fil: Fanchin, Renato. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Taieb, Joëlle. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Cohen Tannoudji, Joëlle. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Carmillo, Paul. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Pepinsky, R. Blake. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Cate, Richard L.. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Di Clemente, Nathalie. Inserm; Francia. Université Paris Diderot - Paris 7; Francia. Centre National de la Recherche Scientifique; Francia
description Context: Anti-Müllerian hormone (AMH) is an important clinical marker for diagnosing and assessing the reproductive status and/or disorders in men and women. Most studies have not distinguished between levels of inactive AMH precursor and the cleaved noncovalent complex that binds the AMH type II receptor (AMHRII) and initiates signaling. Objective: The objective of the study was to measure the levels of AMH cleavage and bioactivity in human body fluids. Design, Setting, and Patients: AMH cleavage levels and bioactivity were measured in the serum of six boys and in the follicular fluid and serum of nine control women and 13 women with the polycystic ovary syndrome (PCOS). Main Outcome Measures: AMH cleavage levels were measured by capturing AMH with an anti- AMH antibody, followed by Western blotting. The bioactivity of cleaved AMH was assessed with an ELISA that measures the levels of AMH capable of binding AMHRII. Results: PCOS women have an elevated level of AMH cleavage in their follicular fluid (24% vs 8% in controlwomen),andmostofthecleavedAMHcanbindAMHRII.Higherlevels of cleavage areobserved in female (60%) and male (79%) serum, but very little of the cleaved AMH can bind AMHRII. Conclusions: These results support an autocrine role for AMH in the pathophysiology of PCOS in the follicle. In addition,theyindicate thatAMHundergoesinteractions or structuralchangesaftercleavage that prevent receptor binding, meaning, unexpectedly, that the level of cleaved AMH in biological fluids does not always reflect the level of bioactive AMH.
publishDate 2016
dc.date.none.fl_str_mv 2016-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/86111
Pierre, Alice; Racine, Chrystèle; Rey, Rodolfo Alberto; Fanchin, Renato; Taieb, Joëlle; et al.; Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum; Endocrine Society; Journal of Clinical Endocrinology and Metabolism; 101; 12; 12-2016; 4618-4627
0021-972X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/86111
identifier_str_mv Pierre, Alice; Racine, Chrystèle; Rey, Rodolfo Alberto; Fanchin, Renato; Taieb, Joëlle; et al.; Most cleaved anti-müllerian hormone binds its receptor in human follicular fluid but little is competent in serum; Endocrine Society; Journal of Clinical Endocrinology and Metabolism; 101; 12; 12-2016; 4618-4627
0021-972X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1210/jc.2016-1742
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jcem/article/101/12/4618/2765023
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/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Endocrine Society
publisher.none.fl_str_mv Endocrine Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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
_version_ 1842268777164570624
score 13.13397

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