Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability

Mutations in multiple genes of the growth hormone/IGF-I axis have been identified in syndromes marked by growth failure. However, no pathogenic human mutations have been reported in the six high-affinity IGF-binding proteins (IGFBPs) or their regulators, such as the met alloproteinase pregnancy-asso...

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Autores: Dauber, Andrew, Muñoz-Calvo, María T., Barrios, Vicente, Domené, Horacio M., Kloverpris, Soren, Serra-Juhé, Clara, Desikan, Vardhini, Pozo Román, Jesús, Muzumdar, Radhika, Martos Moreno, Gabriel Ángel, Hawkins, Federico G., Jasper, Héctor G., Conover, Cheryl A., Frystyk, Jan, Yakar, Shoshana, Hwa, Vivian, Chowen, Julie Ann, Oxvig, Claus, Rosenfeld, Ron G., Pérez-Jurado, Luis A., Argente Oliver, Jesús
Tipo de recurso: artículo
Fecha de publicación:2016
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/677926
Acceso en línea:http://hdl.handle.net/10486/677926
https://dx.doi.org/10.15252/emmm.201506106
Access Level:acceso abierto
Palabra clave:Bone
Delayed growth
Growth hormone
IGF bioavailability
IGF-binding proteins
Medicina
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spelling Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availabilityDauber, AndrewMuñoz-Calvo, María T.Barrios, VicenteDomené, Horacio M.Kloverpris, SorenSerra-Juhé, ClaraDesikan, VardhiniPozo Román, JesúsMuzumdar, RadhikaMartos Moreno, Gabriel ÁngelHawkins, Federico G.Jasper, Héctor G.Conover, Cheryl A.Frystyk, JanYakar, ShoshanaHwa, VivianChowen, Julie AnnOxvig, ClausRosenfeld, Ron G.Pérez-Jurado, Luis A.Argente Oliver, JesúsBoneDelayed growthGrowth hormoneIGF bioavailabilityIGF-binding proteinsMedicinaMutations in multiple genes of the growth hormone/IGF-I axis have been identified in syndromes marked by growth failure. However, no pathogenic human mutations have been reported in the six high-affinity IGF-binding proteins (IGFBPs) or their regulators, such as the met alloproteinase pregnancy-associated plasma protein A2 (PAPP-A2) that is hypothesized to increase IGF-I bioactivity by specific proteolytic cleavage of IGFBP-3 and -5. Multiple members of two unrelated families presented with progressive growth failure, moderate microcephaly, thin long bones, mildly decreased bone density and elevated circulating total IGF-I, IGFBP-3, and -5, acid labile subunit, and IGF-II concentrations. Two different homozygous mutations in PAPPA2, p.D643fs25* and p.Ala1033Val, were associated with this novel syndrome of growth failure. In vitro analysis of IGFBP cleavage demonstrated that both mutations cause a complete absence of PAPP-A2 proteolytic activity. Size-exclusion chromatography showed a significant increase in IGF-I bound in its ternary complex. Free IGF-I concentrations were decreased. These patients provide important insights into the regulation of longitudinal growth in humans, documenting the critical role of PAPP-A2 in releasing IGF-I from its BPs.Research reported in this publication was supported by Fondos de Investigación Sanitaria and fondos FEDER (Grants PI100747 and PI1302195 to JA, PI1302481 to LAPJ), Ministerio de Ciencia e Innovación (Grants BFU2011–27492 and BFU2014-51836-C2-2-R to JAC), Centro de Investigación Biomédica en Red Fisiopatología de Obesidad y Nutrición (CIBEROBN), Instituto de Salud Carlos III (JA), Fundación Endocrinología y Nutrición (JA), the Catalan Government (2014SGR1468 and ICREA Acadèmica to LAPJ), the Eunice Kennedy Shriver National Institute of Child Health & Human Development of the National Institutes of Health (Award Number K23HD07335 to AD), The Danish Council for Independent Research (FNU), and the Novo Nordisk Foundation (CO). A CIBER for Rare Diseases (CIBERER) fellowship supported CSJWiley-Blackwell Publishing LtdWiley - V C H Verlag GmbH & Co. KGaADepartamento de PediatríaFacultad de MedicinaInstituto de Investigación del Hospital de La Princesa (IP)20162016-04-01research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10486/677926https://dx.doi.org/10.15252/emmm.201506106reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:repositorio.uam.es:10486/6779262026-06-23T12:46:27Z
dc.title.none.fl_str_mv Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
title Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
spellingShingle Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
Dauber, Andrew
Bone
Delayed growth
Growth hormone
IGF bioavailability
IGF-binding proteins
Medicina
title_short Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
title_full Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
title_fullStr Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
title_full_unstemmed Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
title_sort Mutations in pregnancy-associated plasma protein A2 cause short stature due to low IGF-I availability
dc.creator.none.fl_str_mv Dauber, Andrew
Muñoz-Calvo, María T.
Barrios, Vicente
Domené, Horacio M.
Kloverpris, Soren
Serra-Juhé, Clara
Desikan, Vardhini
Pozo Román, Jesús
Muzumdar, Radhika
Martos Moreno, Gabriel Ángel
Hawkins, Federico G.
Jasper, Héctor G.
Conover, Cheryl A.
Frystyk, Jan
Yakar, Shoshana
Hwa, Vivian
Chowen, Julie Ann
Oxvig, Claus
Rosenfeld, Ron G.
Pérez-Jurado, Luis A.
Argente Oliver, Jesús
author Dauber, Andrew
author_facet Dauber, Andrew
Muñoz-Calvo, María T.
Barrios, Vicente
Domené, Horacio M.
Kloverpris, Soren
Serra-Juhé, Clara
Desikan, Vardhini
Pozo Román, Jesús
Muzumdar, Radhika
Martos Moreno, Gabriel Ángel
Hawkins, Federico G.
Jasper, Héctor G.
Conover, Cheryl A.
Frystyk, Jan
Yakar, Shoshana
Hwa, Vivian
Chowen, Julie Ann
Oxvig, Claus
Rosenfeld, Ron G.
Pérez-Jurado, Luis A.
Argente Oliver, Jesús
author_role author
author2 Muñoz-Calvo, María T.
Barrios, Vicente
Domené, Horacio M.
Kloverpris, Soren
Serra-Juhé, Clara
Desikan, Vardhini
Pozo Román, Jesús
Muzumdar, Radhika
Martos Moreno, Gabriel Ángel
Hawkins, Federico G.
Jasper, Héctor G.
Conover, Cheryl A.
Frystyk, Jan
Yakar, Shoshana
Hwa, Vivian
Chowen, Julie Ann
Oxvig, Claus
Rosenfeld, Ron G.
Pérez-Jurado, Luis A.
Argente Oliver, Jesús
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Pediatría
Facultad de Medicina
Instituto de Investigación del Hospital de La Princesa (IP)
dc.subject.none.fl_str_mv Bone
Delayed growth
Growth hormone
IGF bioavailability
IGF-binding proteins
Medicina
topic Bone
Delayed growth
Growth hormone
IGF bioavailability
IGF-binding proteins
Medicina
description Mutations in multiple genes of the growth hormone/IGF-I axis have been identified in syndromes marked by growth failure. However, no pathogenic human mutations have been reported in the six high-affinity IGF-binding proteins (IGFBPs) or their regulators, such as the met alloproteinase pregnancy-associated plasma protein A2 (PAPP-A2) that is hypothesized to increase IGF-I bioactivity by specific proteolytic cleavage of IGFBP-3 and -5. Multiple members of two unrelated families presented with progressive growth failure, moderate microcephaly, thin long bones, mildly decreased bone density and elevated circulating total IGF-I, IGFBP-3, and -5, acid labile subunit, and IGF-II concentrations. Two different homozygous mutations in PAPPA2, p.D643fs25* and p.Ala1033Val, were associated with this novel syndrome of growth failure. In vitro analysis of IGFBP cleavage demonstrated that both mutations cause a complete absence of PAPP-A2 proteolytic activity. Size-exclusion chromatography showed a significant increase in IGF-I bound in its ternary complex. Free IGF-I concentrations were decreased. These patients provide important insights into the regulation of longitudinal growth in humans, documenting the critical role of PAPP-A2 in releasing IGF-I from its BPs.
publishDate 2016
dc.date.none.fl_str_mv 2016
2016-04-01
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10486/677926
https://dx.doi.org/10.15252/emmm.201506106
url http://hdl.handle.net/10486/677926
https://dx.doi.org/10.15252/emmm.201506106
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley-Blackwell Publishing Ltd
Wiley - V C H Verlag GmbH & Co. KGaA
publisher.none.fl_str_mv Wiley-Blackwell Publishing Ltd
Wiley - V C H Verlag GmbH & Co. KGaA
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
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