Effect of Seminal Phospholipid-Binding Proteins and Follicular Fluid on Bovine Sperm Capacitation1

Thérien, Isabelle; Bousquet, D.; Manjunath, Puttaswamy

doi:10.1095/biolreprod65.1.41

Cited by 57 publications

(50 citation statements)

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“…On the basis of these results, we suggest referring to these 2 proteins as RSVP14 and RSVP20, respectively, according to their origin and molecular weight. Because of the high homology found between RSVP14 and bovine PDC 109 (both containing the FN2 domain) and the obtained evidence that P14 is partially released from the sperm membrane during capacitation and is redistributed over the sperm surface (Barrios et al, 2005), as reported for BSP proteins (Thérien et al, 2001), we have recently suggested that RSVP14 may take part in the protein structure surrounding the spermatozoa in a similar way as fibronectin, stabilizing membrane phospholipids and cytoskeleton (Barrios et al, 2005). We have found out by partition in a 2-phase system with Triton X-114 (Sigma) that these proteins are highly hydrophobic (data not shown), and it was confirmed by the obtained results of partial amino acid sequencing, especially P20 (Barrios et al, 2005).…”

Section: Discussionmentioning

confidence: 63%

“…The homology was found from amino acid 19-34 (CVFPFTYYDDRHFDCT) with 49-64 of PDC-109 (CVFPFVYRNRKHFDCT), which is the FN2 domain (Greube et al, 2001). PDC-109 has been reported to stabilize the sperm membrane in a first step (Greube et al, 2001) and subsequently to participate in the female tract in capacitation by releasing cholesterol and binding high-density lipoprotein and heparin (Thérien et al, 1998(Thérien et al, , 2001Gwathmey et al, 2003). However, the P20 fragment was not homologous with any reported protein (Barrios et al, 2005).…”

Section: Discussionmentioning

confidence: 97%

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Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

Fernández‐Juan

Gallego

Barrios

et al. 2006

Journal of Andrology

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Previously, we reported that the addition of seminal plasma proteins before cold-shock treatment prevents sperm membrane injury, and that 2 proteins of approximately 14 (P14) and 20 (P20) kDa, the main components of fraction 6 isolated by exclusion chromatography, are responsible for this protective effect. The objective of the present study was to localize P14 and P20 in tissues of the ram reproductive tract to determine their origin. Antiserum generated against purified P14 and P20 reacted with proteins in seminal vesicles and vas deferens by Western blot analyses of protein tissue extracts. However, these antisera failed to detect P14 and P20 in testis, prostate, efferent ductules, bulbourethral glands, and epididymis (caput, corpus, and cauda). Immunohistochemical analyses by both indirect immunofluorescence and the avidin-biotin complex technique confirmed that only seminal vesicles showed reactivity, restricted to the secretory cells, with both antibodies. Obtained results indicate that P14 and P20 are secreted specifically in the seminal vesicles. To further confirm that P14 and P20 are specifically expressed in seminal vesicles, we used Northern blot analyses to investigate the expression of both proteins in seminal vesicles and vas deferens. These assays corroborated again that P14 and P20 were specifically expressed in seminal vesicles. Consequently, we suggest referring to these 2 proteins as RSVP14 and RSVP20, respectively, according to their origin and molecular weight.

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Section: Discussionmentioning

confidence: 63%

Section: Discussionmentioning

confidence: 97%

Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

Fernández‐Juan

Gallego

Barrios

et al. 2006

Journal of Andrology

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“…Anteriormente, se ha podido reconocer para otras especies que el fluido folicular favorece ciertas funciones asociadas con la capacidad fecundante como la movilidad y la reacción acrosomal (Yanagimachi, 1969;Tesarík, 1985;Suarez et al, 1986;Morales et al, 1989;Ravnik et al, 1990;Hansen et al, 1991;McNutt y Killian, 1991;Ravnik et al, 1992;McNutt et al, 1994;Cheng et al, 1998;Jeon et al, 2001;Thérien et al, 2001;Briton-Jones et al, 2001;Schuffner et al, 2002;Getpook y Wirotkarun, 2007;Esmaeilpour et al, 2014;Leemans et al, 2015). Estudios previos en nuestro laboratorio determinaron que el fluido folicular favorece la movilidad espermática en alpaca (Bravo y Valdivia, 2017).…”

Section: Discussionunclassified

“…Se ha podido observar que el fluido folicular puede estimular las funciones espermáticas relacionadas con la capacidad fecundante en varias especies. Por ejemplo, se ha reconocido que el fluido folicular tiene un efecto favorable en la movilidad espermática (Yanagimachi, 1969;Tesarík, 1985;McNutt et al, 1994;Jeon et al, 2001;Briton-Jones et al, 2001;Getpook y Wirotkarun, 2007;Esmaeilpour et al, 2014;Leemans et al, 2015) y la reacción acrosomal (Yanagimachi, 1969;Thérien et al, 2001;Thérien et al, 2005). En el caso de la alpaca, Bravo & Valdivia (2017) pudieron observar que el fluido folicular estimulaba la movilidad espermática.…”

Section: Introductcionunclassified

EFECTO DEL FLUIDO FOLICULAR SOBRE LA CAPACIDAD DE UNIÓN A ZONA PELÚCIDA DE ESPERMATOZOIDES EPIDIDIMARIOS DE ALPACA (Vicugna pacos)

Bravo¹,

Rubén²,

Valdivia³

2017

SPERMOVA

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Follicular fluid is the liquid fraction that surrounds the oocyte during its growth and maturation in the ovary. The components of the follicular fluid can favor the functionality of the sperm. In the present research, the binding to the zona pellucida of epididymal spermatozoa of alpaca incubated with follicular fluid was studied. In the experiment a control group and a treatment group were used. The sperm from the control group and the treatment were incubated with zona pellucidae. The incubation of the treatment group was performed in the presence of follicular fluid at a concentration of 30%; while the incubation of the control group occurred in the absence of follicular fluid. It was observed that a greater number of spermatozoa joined the zona pellucida in the group incubated in the presence of follicular fluid. It was found that there were statistical differences between treatment and control. It is concluded that alpaca follicular fluid enhances the in vitro binding of spermatozoa to the zona pellucida of this species.Keywords: Alpaca, follicular fluid, zona pellucida, epididymal sperm, gametic interaction. RESUMENEl fluido folicular es la fracción líquida que rodea al ovocito durante su crecimiento y maduración en el ovario. Los componentes del fluido folicular pueden favorecer la funcionalidad de los espermatozoides. En el presente trabajo se ha estudiado la unión a zona pelúcida de espermatozoides epididimarios de alpaca incubados con fluido folicular de esta especie. En el experimento se utilizó un grupo control y un grupo tratamiento. Los espermatozoides del grupo control y el tratamiento fueron incubados con zonas pelúcidas. La incubación del grupo tratamiento se realizó en presencia de fluido folicular a una concentración de 30%; mientras que la incubación del grupo control se dio en ausencia de fluido folicular. Se observó que un mayor número de espermatozoides se unían a la zona pelúcida en el grupo incubado en presencia de fluido folicular. Se encontró que había diferencias estadísticas entre el tratamiento y el control. Se concluye que el fluido folicular de alpaca favorece la unión in vitro de espermatozoides a la zona pelúcida de esta especie.Palabras clave: Alpaca, fluido folicular, zona pelúcida, espermatozoides epididimarios, interacción gamética.

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“…HDL also contains choline phospholipids, which could also be responsible for the BSP binding. Through this interaction, bovine BSP proteins can increase the stimulation of capacitation caused by HDLs (Thérien et al 2001). To determine whether murine BSPH1 could be implicated in a similar mechanism, the effect of anti-BSPH1 on the HDLinduced capacitation in murine sperm was tested.…”

Section: Hdl-induced Capacitationmentioning

confidence: 99%

Murine binder of sperm protein homolog 1: a new player in HDL-induced capacitation

Plante

Manjunath

2015

Reproduction

Self Cite

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Binder of sperm (BSP) proteins are ubiquitous among mammals and are exclusively expressed in male genital tract. The main function associated with BSP proteins is their ability to promote sperm capacitation. In mice, two proteins (BSP protein homolog 1 (BSPH1) and BSPH2) have been studied. Using recombinant strategies, BSPH1 was found to bind to epididymal sperm membranes and promote sperm capacitation in vitro. The goal of this study was to evaluate the role of native murine BSPH1 protein in sperm capacitation induced by BSA and HDLs. The effect of antibodies, antigen-binding fragments (Fabs), and F(ab 0 ) 2 specific for murine BSPH1 on BSA-and HDL-induced capacitation was tested. Results indicate that BSPH1 has no direct role in BSA-induced capacitation. However, antibodies, Fabs, and F(ab 0 ) 2 could block capacitation induced by HDLs and could inhibit the HDL-induced increase in tyrosine phosphorylation, suggesting a specific interaction between HDLs and BSPH1. Results indicate that murine BSPH1 proteins in mice could be a new important piece of the puzzle in sperm capacitation induced by HDLs. As murine BSPH1 is orthologous to human BSPH1, this study could also lead to new insights into the functions and the importance of the human protein in male fertility. Free French abstract: A French translation of this abstract is freely available at

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Effect of Seminal Phospholipid-Binding Proteins and Follicular Fluid on Bovine Sperm Capacitation1

Cited by 57 publications

References 58 publications

Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

Immunohistochemical Localization of Sperm‐Preserving Proteins in the Ram Reproductive Tract

EFECTO DEL FLUIDO FOLICULAR SOBRE LA CAPACIDAD DE UNIÓN A ZONA PELÚCIDA DE ESPERMATOZOIDES EPIDIDIMARIOS DE ALPACA (Vicugna pacos)

Murine binder of sperm protein homolog 1: a new player in HDL-induced capacitation

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