Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10662/21227
Títulos: Identification and function of exchange proteins activated directly by cyclic AMP (Epac) in mammalian spermatozoa
Autores/as: Miró Morán, Álvaro
Jaridn Polo, Isaac
Ortega Ferrusola, Cristina
Salido Ruiz, G. M.
Peña Vega, Fernando Juan
Tapia García, José Antonio
Aparicio Donoso, Inés María
Palabras clave: EPAC;Spermatozoas;Mammalian;Espermatozoides;Mamíferos;Intracellular signaling;Espermatozoide;Señalización intracelular
Fecha de publicación: 2012
Editor/a: Public Library of Science
Universidade Federal do Rio de Janeiro
Resumen: The role of cAMP in spermatic functions was classically thought to be mediated exclusively through the activation of Protein Kinase A (PKA). However, it has recently been shown that cAMP also exerts its effects through a PKA-independent pathway activating a family of proteins known as Epac proteins. Therefore, many of the spermatic functions thought to be regulated by cAMP through the activation of PKA are again under study. We aimed to identify and to investigate the role of Epac proteins in spermatozoa using a specific permeable analog (8-Br-2′-O-Me-cAMP). Also, we aimed to study its relationship with E-cadherin, an adhesion protein involved in fertility. Our results demonstrate the presence and sub-cellular distribution of Epac 1 and Epac 2 in mammalian spermatozoa. Capacitation and the acrosome reaction induced a change in the localization of Epac proteins in sperm. Moreover, incubation with 8-Br-2′-O-Me-cAMP prompted an increase in Rap1 activation, in the scrambling of plasma membrane phospholipids (necessary for the capacitation process), the acrosome reaction, motility, and calcium mobilization, when spermatozoa were incubated in acrosome reaction conditions. Finally, the activation of Epac proteins induced a change in the distribution of E-cadherin. Therefore, the increase in the acrosome reaction, together with the increase in calcium (which is known to be essential for fertilization) and the Epac nteraction with E-cadherin, might indicate that Epac proteins have an important role in gamete recognition and fertilization.
URI: http://hdl.handle.net/10662/21227
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0037713
Colección:CTS002 - Artículos
DFSIO - Artículos

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