Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells

Autores
Loreti, Rosana Nazareth; Ambao, Veronica Ana; Andreone, Luz; Trigo, Romina; Bussmann, Ursula Agnes; Campo, Stella Maris
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Granulosa cell inhibin A and B production is regulated by FSH and gonadal factors. This gonadotrophin is released as a mixture of glycoforms, which induce different biological responses in vivo and in vitro. Our aim was to determine the effect of recombinant human FSH glycosylation variants on inhibin A and B production by rat granulosa cells. Preparative isoelectrofocusing was used to isolate more acidic/sialylated (pH<4.00) and less acidic/sialylated (pH>5.00) rhFSH charge analogues. Concanavalin-A was used to isolate unbound and firmly bound rhFSH glycoforms on the basis of their oligosaccharide complexity. Granulosa cells, obtained from oestrogen-primed immature rats, were cultured with either native rhFSH or its glycosylation variants. Inhibin A and B were determined using specific ELISAs. Results were expressed as mean±SEM. Under basal conditions inhibin A was the predominant dimer produced (inhibin A: 673±55; inhibin B: 80±4 pg/mL). More acidic/sialylated charge analogues stimulated inhibin B production when compared to inhibin A at all doses studied; in contrast, less acidic/sialylated charge analogues stimulated inhibin A production and elicited no effect on inhibin B. Glycoforms bearing complex oligosaccharides showed a potent stimulatory effect on inhibin B when compared to inhibin A production (i.e. dose 1ng/mL: 4.9±0.5vs0.9±0.1 fold stimulation, P<0.001). Glycoforms bearing hybrid type oligosaccharides favoured inhibin A production (i.e. dose 4ng/mL 2.9±0.1vs1.6±0.1 fold stimulation, P<0.05). These results show that the sialylation degree as well as the complexity of oligosaccharides present in the rhFSH molecule may be considered additional factors that differentially regulate dimeric inhibin production by rat granulosa cells.
Fil: Loreti, Rosana Nazareth. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina. 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: Ambao, Veronica Ana. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Andreone, Luz. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Trigo, Romina. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Bussmann, Ursula Agnes. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Campo, Stella Maris. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Materia
Fsh
Sialylation
Inhibin
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:11336/1403
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/1403
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cellsLoreti, Rosana NazarethAmbao, Veronica AnaAndreone, LuzTrigo, RominaBussmann, Ursula AgnesCampo, Stella MarisFshSialylationInhibinhttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Granulosa cell inhibin A and B production is regulated by FSH and gonadal factors. This gonadotrophin is released as a mixture of glycoforms, which induce different biological responses in vivo and in vitro. Our aim was to determine the effect of recombinant human FSH glycosylation variants on inhibin A and B production by rat granulosa cells. Preparative isoelectrofocusing was used to isolate more acidic/sialylated (pH<4.00) and less acidic/sialylated (pH>5.00) rhFSH charge analogues. Concanavalin-A was used to isolate unbound and firmly bound rhFSH glycoforms on the basis of their oligosaccharide complexity. Granulosa cells, obtained from oestrogen-primed immature rats, were cultured with either native rhFSH or its glycosylation variants. Inhibin A and B were determined using specific ELISAs. Results were expressed as mean±SEM. Under basal conditions inhibin A was the predominant dimer produced (inhibin A: 673±55; inhibin B: 80±4 pg/mL). More acidic/sialylated charge analogues stimulated inhibin B production when compared to inhibin A at all doses studied; in contrast, less acidic/sialylated charge analogues stimulated inhibin A production and elicited no effect on inhibin B. Glycoforms bearing complex oligosaccharides showed a potent stimulatory effect on inhibin B when compared to inhibin A production (i.e. dose 1ng/mL: 4.9±0.5vs0.9±0.1 fold stimulation, P<0.001). Glycoforms bearing hybrid type oligosaccharides favoured inhibin A production (i.e. dose 4ng/mL 2.9±0.1vs1.6±0.1 fold stimulation, P<0.05). These results show that the sialylation degree as well as the complexity of oligosaccharides present in the rhFSH molecule may be considered additional factors that differentially regulate dimeric inhibin production by rat granulosa cells.Fil: Loreti, Rosana Nazareth. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina. 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: Ambao, Veronica Ana. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; ArgentinaFil: Andreone, Luz. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; ArgentinaFil: Trigo, Romina. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; ArgentinaFil: Bussmann, Ursula Agnes. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Campo, Stella Maris. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; ArgentinaBioScientifica2013-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/1403Loreti, Rosana Nazareth; Ambao, Veronica Ana; Andreone, Luz; Trigo, Romina; Bussmann, Ursula Agnes; et al.; Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells; BioScientifica; Reproduction; 145; 2; 1-2013; 127-1351470-1626enginfo:eu-repo/semantics/reference/url/info:eu-repo/semantics/reference es info:eu-repo/semantics/reference/pmid/PMID: 23166369 [PubMed - indexed for MEDLINE] Free full textinfo:eu-repo/semantics/altIdentifier/doi/10.1530/REP-12-0228info:eu-repo/semantics/altIdentifier/url/https://rep.bioscientifica.com/view/journals/rep/145/2/127.xmlinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:23:25Zoai:ri.conicet.gov.ar:11336/1403instacron: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:34982025-09-29 10:23:25.909CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
title Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
spellingShingle Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
Loreti, Rosana Nazareth
Fsh
Sialylation
Inhibin
title_short Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
title_full Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
title_fullStr Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
title_full_unstemmed Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
title_sort Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells
dc.creator.none.fl_str_mv Loreti, Rosana Nazareth
Ambao, Veronica Ana
Andreone, Luz
Trigo, Romina
Bussmann, Ursula Agnes
Campo, Stella Maris
author Loreti, Rosana Nazareth
author_facet Loreti, Rosana Nazareth
Ambao, Veronica Ana
Andreone, Luz
Trigo, Romina
Bussmann, Ursula Agnes
Campo, Stella Maris
author_role author
author2 Ambao, Veronica Ana
Andreone, Luz
Trigo, Romina
Bussmann, Ursula Agnes
Campo, Stella Maris
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Fsh
Sialylation
Inhibin
topic Fsh
Sialylation
Inhibin
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Granulosa cell inhibin A and B production is regulated by FSH and gonadal factors. This gonadotrophin is released as a mixture of glycoforms, which induce different biological responses in vivo and in vitro. Our aim was to determine the effect of recombinant human FSH glycosylation variants on inhibin A and B production by rat granulosa cells. Preparative isoelectrofocusing was used to isolate more acidic/sialylated (pH<4.00) and less acidic/sialylated (pH>5.00) rhFSH charge analogues. Concanavalin-A was used to isolate unbound and firmly bound rhFSH glycoforms on the basis of their oligosaccharide complexity. Granulosa cells, obtained from oestrogen-primed immature rats, were cultured with either native rhFSH or its glycosylation variants. Inhibin A and B were determined using specific ELISAs. Results were expressed as mean±SEM. Under basal conditions inhibin A was the predominant dimer produced (inhibin A: 673±55; inhibin B: 80±4 pg/mL). More acidic/sialylated charge analogues stimulated inhibin B production when compared to inhibin A at all doses studied; in contrast, less acidic/sialylated charge analogues stimulated inhibin A production and elicited no effect on inhibin B. Glycoforms bearing complex oligosaccharides showed a potent stimulatory effect on inhibin B when compared to inhibin A production (i.e. dose 1ng/mL: 4.9±0.5vs0.9±0.1 fold stimulation, P<0.001). Glycoforms bearing hybrid type oligosaccharides favoured inhibin A production (i.e. dose 4ng/mL 2.9±0.1vs1.6±0.1 fold stimulation, P<0.05). These results show that the sialylation degree as well as the complexity of oligosaccharides present in the rhFSH molecule may be considered additional factors that differentially regulate dimeric inhibin production by rat granulosa cells.
Fil: Loreti, Rosana Nazareth. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina. 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: Ambao, Veronica Ana. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Andreone, Luz. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Trigo, Romina. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
Fil: Bussmann, Ursula Agnes. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Campo, Stella Maris. 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. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina
description Granulosa cell inhibin A and B production is regulated by FSH and gonadal factors. This gonadotrophin is released as a mixture of glycoforms, which induce different biological responses in vivo and in vitro. Our aim was to determine the effect of recombinant human FSH glycosylation variants on inhibin A and B production by rat granulosa cells. Preparative isoelectrofocusing was used to isolate more acidic/sialylated (pH<4.00) and less acidic/sialylated (pH>5.00) rhFSH charge analogues. Concanavalin-A was used to isolate unbound and firmly bound rhFSH glycoforms on the basis of their oligosaccharide complexity. Granulosa cells, obtained from oestrogen-primed immature rats, were cultured with either native rhFSH or its glycosylation variants. Inhibin A and B were determined using specific ELISAs. Results were expressed as mean±SEM. Under basal conditions inhibin A was the predominant dimer produced (inhibin A: 673±55; inhibin B: 80±4 pg/mL). More acidic/sialylated charge analogues stimulated inhibin B production when compared to inhibin A at all doses studied; in contrast, less acidic/sialylated charge analogues stimulated inhibin A production and elicited no effect on inhibin B. Glycoforms bearing complex oligosaccharides showed a potent stimulatory effect on inhibin B when compared to inhibin A production (i.e. dose 1ng/mL: 4.9±0.5vs0.9±0.1 fold stimulation, P<0.001). Glycoforms bearing hybrid type oligosaccharides favoured inhibin A production (i.e. dose 4ng/mL 2.9±0.1vs1.6±0.1 fold stimulation, P<0.05). These results show that the sialylation degree as well as the complexity of oligosaccharides present in the rhFSH molecule may be considered additional factors that differentially regulate dimeric inhibin production by rat granulosa cells.
publishDate 2013
dc.date.none.fl_str_mv 2013-01
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/11336/1403
Loreti, Rosana Nazareth; Ambao, Veronica Ana; Andreone, Luz; Trigo, Romina; Bussmann, Ursula Agnes; et al.; Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells; BioScientifica; Reproduction; 145; 2; 1-2013; 127-135
1470-1626
url http://hdl.handle.net/11336/1403
identifier_str_mv Loreti, Rosana Nazareth; Ambao, Veronica Ana; Andreone, Luz; Trigo, Romina; Bussmann, Ursula Agnes; et al.; Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells; BioScientifica; Reproduction; 145; 2; 1-2013; 127-135
1470-1626
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/doi/10.1530/REP-12-0228
info:eu-repo/semantics/altIdentifier/url/https://rep.bioscientifica.com/view/journals/rep/145/2/127.xml
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publisher.none.fl_str_mv BioScientifica
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