Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation
- Autores
- Battistone, Maria Agustina; Alvau, A.; Salicioni, A. M.; Visconti, P. E.; Da Ros, Vanina Gabriela; Cuasnicu, Patricia Sara
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Sperm capacitation involves an increase in intracellular Ca(2+) concentration as well as in protein kinase A (PKA)-dependent protein tyrosine (Tyr) phosphorylation. Interestingly, in humans, a decrease in extracellular Ca(2+) concentration ([Ca(2+)]e) during capacitation induces an increase in Tyr phosphorylation indicating the complexity of Ca(2+) signaling during this process. In view of this, in the present study we further investigated the Ca(2+)-mediated signaling pathways implicated in Tyr phosphorylation during human sperm capacitation. Results revealed that sperm incubation in a medium without added Ca(2+) (e Ca(2+)) increased Tyr phosphorylation but did not modify PKA-mediated phosphorylation. Moreover, inhibition of either PKA or Src family kinase signaling cascades in e Ca(2+) down-regulated both PKA substrate and Tyr phosphorylations, indicating that the [Ca(2+)]e effects on Tyr phosphorylation depend on PKA targets. Inhibition of calmodulin or Ser/Thr protein phosphatase 2B also increased Tyr phosphorylation without affecting PKA-mediated phosphorylation, supporting the potential role of these Ca(2+) downstream effectors in the increase in Tyr phosphorylation observed in e Ca(2+). Experiments aimed to identify the kinase responsible for these observations revealed the presence of proline-rich tyrosine kinase 2 (PYK2), a focal adhesion kinase (FAK) family member, in human sperm, and the use of PF431396, an FAK inhibitor, supported the involvement of PYK2 in Tyr phosphorylation downstream of PKA activation. Results also showed that PYK2 was activated in e Ca(2+) as well as during capacitation and that PF431396 affected capacitated sperm motility, acrosome reaction and ability to penetrate both mouse cumulus matrix and zona-free hamster eggs. Together, our observations support PYK2 as an intermediary component of Ca(2+) signaling between PKA-mediated and Tyr phosphorylations that is required for achieving functional human sperm capacitation.
Fil: Battistone, Maria Agustina. 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: Alvau, A.. University of Massachussets; Estados Unidos
Fil: Salicioni, A. M.. University of Massachussets; Estados Unidos
Fil: Visconti, P. E.. University of Massachussets; Estados Unidos
Fil: Da Ros, Vanina Gabriela. 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: Cuasnicu, Patricia Sara. 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 - Materia
-
Calcium
Capacitation
Human
Sperm
Tyrosine Phosphorylation - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/22923
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Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitationBattistone, Maria AgustinaAlvau, A.Salicioni, A. M.Visconti, P. E.Da Ros, Vanina GabrielaCuasnicu, Patricia SaraCalciumCapacitationHumanSpermTyrosine Phosphorylationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Sperm capacitation involves an increase in intracellular Ca(2+) concentration as well as in protein kinase A (PKA)-dependent protein tyrosine (Tyr) phosphorylation. Interestingly, in humans, a decrease in extracellular Ca(2+) concentration ([Ca(2+)]e) during capacitation induces an increase in Tyr phosphorylation indicating the complexity of Ca(2+) signaling during this process. In view of this, in the present study we further investigated the Ca(2+)-mediated signaling pathways implicated in Tyr phosphorylation during human sperm capacitation. Results revealed that sperm incubation in a medium without added Ca(2+) (e Ca(2+)) increased Tyr phosphorylation but did not modify PKA-mediated phosphorylation. Moreover, inhibition of either PKA or Src family kinase signaling cascades in e Ca(2+) down-regulated both PKA substrate and Tyr phosphorylations, indicating that the [Ca(2+)]e effects on Tyr phosphorylation depend on PKA targets. Inhibition of calmodulin or Ser/Thr protein phosphatase 2B also increased Tyr phosphorylation without affecting PKA-mediated phosphorylation, supporting the potential role of these Ca(2+) downstream effectors in the increase in Tyr phosphorylation observed in e Ca(2+). Experiments aimed to identify the kinase responsible for these observations revealed the presence of proline-rich tyrosine kinase 2 (PYK2), a focal adhesion kinase (FAK) family member, in human sperm, and the use of PF431396, an FAK inhibitor, supported the involvement of PYK2 in Tyr phosphorylation downstream of PKA activation. Results also showed that PYK2 was activated in e Ca(2+) as well as during capacitation and that PF431396 affected capacitated sperm motility, acrosome reaction and ability to penetrate both mouse cumulus matrix and zona-free hamster eggs. Together, our observations support PYK2 as an intermediary component of Ca(2+) signaling between PKA-mediated and Tyr phosphorylations that is required for achieving functional human sperm capacitation.Fil: Battistone, Maria Agustina. 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: Alvau, A.. University of Massachussets; Estados UnidosFil: Salicioni, A. M.. University of Massachussets; Estados UnidosFil: Visconti, P. E.. University of Massachussets; Estados UnidosFil: Da Ros, Vanina Gabriela. 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: Cuasnicu, Patricia Sara. 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; ArgentinaOxford University Press2014-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/22923Battistone, Maria Agustina; Alvau, A.; Salicioni, A. M.; Visconti, P. E.; Da Ros, Vanina Gabriela; et al.; Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation; Oxford University Press; Molecular Human Reproduction; 20; 11; 1-9-2014; 1054-10661360-99471460-2407CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/molehr/article-lookup/doi/10.1093/molehr/gau073info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4209883/info:eu-repo/semantics/altIdentifier/doi/10.1093/molehr/gau073info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:02:07Zoai:ri.conicet.gov.ar:11336/22923instacron: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 10:02:07.894CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation |
title |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation |
spellingShingle |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation Battistone, Maria Agustina Calcium Capacitation Human Sperm Tyrosine Phosphorylation |
title_short |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation |
title_full |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation |
title_fullStr |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation |
title_full_unstemmed |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation |
title_sort |
Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation |
dc.creator.none.fl_str_mv |
Battistone, Maria Agustina Alvau, A. Salicioni, A. M. Visconti, P. E. Da Ros, Vanina Gabriela Cuasnicu, Patricia Sara |
author |
Battistone, Maria Agustina |
author_facet |
Battistone, Maria Agustina Alvau, A. Salicioni, A. M. Visconti, P. E. Da Ros, Vanina Gabriela Cuasnicu, Patricia Sara |
author_role |
author |
author2 |
Alvau, A. Salicioni, A. M. Visconti, P. E. Da Ros, Vanina Gabriela Cuasnicu, Patricia Sara |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Calcium Capacitation Human Sperm Tyrosine Phosphorylation |
topic |
Calcium Capacitation Human Sperm Tyrosine Phosphorylation |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Sperm capacitation involves an increase in intracellular Ca(2+) concentration as well as in protein kinase A (PKA)-dependent protein tyrosine (Tyr) phosphorylation. Interestingly, in humans, a decrease in extracellular Ca(2+) concentration ([Ca(2+)]e) during capacitation induces an increase in Tyr phosphorylation indicating the complexity of Ca(2+) signaling during this process. In view of this, in the present study we further investigated the Ca(2+)-mediated signaling pathways implicated in Tyr phosphorylation during human sperm capacitation. Results revealed that sperm incubation in a medium without added Ca(2+) (e Ca(2+)) increased Tyr phosphorylation but did not modify PKA-mediated phosphorylation. Moreover, inhibition of either PKA or Src family kinase signaling cascades in e Ca(2+) down-regulated both PKA substrate and Tyr phosphorylations, indicating that the [Ca(2+)]e effects on Tyr phosphorylation depend on PKA targets. Inhibition of calmodulin or Ser/Thr protein phosphatase 2B also increased Tyr phosphorylation without affecting PKA-mediated phosphorylation, supporting the potential role of these Ca(2+) downstream effectors in the increase in Tyr phosphorylation observed in e Ca(2+). Experiments aimed to identify the kinase responsible for these observations revealed the presence of proline-rich tyrosine kinase 2 (PYK2), a focal adhesion kinase (FAK) family member, in human sperm, and the use of PF431396, an FAK inhibitor, supported the involvement of PYK2 in Tyr phosphorylation downstream of PKA activation. Results also showed that PYK2 was activated in e Ca(2+) as well as during capacitation and that PF431396 affected capacitated sperm motility, acrosome reaction and ability to penetrate both mouse cumulus matrix and zona-free hamster eggs. Together, our observations support PYK2 as an intermediary component of Ca(2+) signaling between PKA-mediated and Tyr phosphorylations that is required for achieving functional human sperm capacitation. Fil: Battistone, Maria Agustina. 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: Alvau, A.. University of Massachussets; Estados Unidos Fil: Salicioni, A. M.. University of Massachussets; Estados Unidos Fil: Visconti, P. E.. University of Massachussets; Estados Unidos Fil: Da Ros, Vanina Gabriela. 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: Cuasnicu, Patricia Sara. 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 |
description |
Sperm capacitation involves an increase in intracellular Ca(2+) concentration as well as in protein kinase A (PKA)-dependent protein tyrosine (Tyr) phosphorylation. Interestingly, in humans, a decrease in extracellular Ca(2+) concentration ([Ca(2+)]e) during capacitation induces an increase in Tyr phosphorylation indicating the complexity of Ca(2+) signaling during this process. In view of this, in the present study we further investigated the Ca(2+)-mediated signaling pathways implicated in Tyr phosphorylation during human sperm capacitation. Results revealed that sperm incubation in a medium without added Ca(2+) (e Ca(2+)) increased Tyr phosphorylation but did not modify PKA-mediated phosphorylation. Moreover, inhibition of either PKA or Src family kinase signaling cascades in e Ca(2+) down-regulated both PKA substrate and Tyr phosphorylations, indicating that the [Ca(2+)]e effects on Tyr phosphorylation depend on PKA targets. Inhibition of calmodulin or Ser/Thr protein phosphatase 2B also increased Tyr phosphorylation without affecting PKA-mediated phosphorylation, supporting the potential role of these Ca(2+) downstream effectors in the increase in Tyr phosphorylation observed in e Ca(2+). Experiments aimed to identify the kinase responsible for these observations revealed the presence of proline-rich tyrosine kinase 2 (PYK2), a focal adhesion kinase (FAK) family member, in human sperm, and the use of PF431396, an FAK inhibitor, supported the involvement of PYK2 in Tyr phosphorylation downstream of PKA activation. Results also showed that PYK2 was activated in e Ca(2+) as well as during capacitation and that PF431396 affected capacitated sperm motility, acrosome reaction and ability to penetrate both mouse cumulus matrix and zona-free hamster eggs. Together, our observations support PYK2 as an intermediary component of Ca(2+) signaling between PKA-mediated and Tyr phosphorylations that is required for achieving functional human sperm capacitation. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-09-01 |
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/11336/22923 Battistone, Maria Agustina; Alvau, A.; Salicioni, A. M.; Visconti, P. E.; Da Ros, Vanina Gabriela; et al.; Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation; Oxford University Press; Molecular Human Reproduction; 20; 11; 1-9-2014; 1054-1066 1360-9947 1460-2407 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/22923 |
identifier_str_mv |
Battistone, Maria Agustina; Alvau, A.; Salicioni, A. M.; Visconti, P. E.; Da Ros, Vanina Gabriela; et al.; Evidence for the involvement of Proline-rich Tyrosine Kinase 2 (PYK2) in tyrosine phosphorylation downstream of PKA activation during human sperm capacitation; Oxford University Press; Molecular Human Reproduction; 20; 11; 1-9-2014; 1054-1066 1360-9947 1460-2407 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/molehr/article-lookup/doi/10.1093/molehr/gau073 info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4209883/ info:eu-repo/semantics/altIdentifier/doi/10.1093/molehr/gau073 |
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 application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Oxford University Press |
publisher.none.fl_str_mv |
Oxford University Press |
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 |
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1842269738772725760 |
score |
13.13397 |