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8. Capacitation increases glucose consumption in murine sperm

Author

Hidalgo, David M., primary, Romarowski, Ana, additional, Gervasi, María G., additional, Navarrete, Felipe, additional, Balbach, Melanie, additional, Salicioni, Ana M., additional, Levin, Lonny R., additional, Buck, Jochen, additional, and Visconti, Pablo E., additional

Published
2020
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10. Transient Sperm Starvation Improves the Outcome of Assisted Reproductive Technologies

Author

Navarrete, Felipe A., primary, Aguila, Luis, additional, Martin-Hidalgo, David, additional, Tourzani, Darya A., additional, Luque, Guillermina M., additional, Ardestani, Goli, additional, Garcia-Vazquez, Francisco A., additional, Levin, Lonny R., additional, Buck, Jochen, additional, Darszon, Alberto, additional, Buffone, Mariano G., additional, Mager, Jesse, additional, Fissore, Rafael A., additional, Salicioni, Ana M., additional, Gervasi, María G., additional, and Visconti, Pablo E., additional

Published
2019
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11. Biphasic Role of Calcium in Mouse Sperm Capacitation Signaling Pathways

Author

Navarrete, Felipe A., García-Vázquez, Francisco A., Alvau, Antonio, Escoffier, Jessica, Krapf, Dario, Sánchez-Cárdenas, Claudia, Salicioni, Ana M., Darszon, Alberto, and Visconti, Pablo E.

Subjects
Male, Mice, Knockout, Blotting, Western, Sperm capacitation, Article, purl.org/becyt/ford/1 [https], Ciencias Biológicas, Mice, Cyclic AMP, Sperm Motility, Animals, Tyrosine, Calcium, PKA, Calcium Channels, Phosphorylation, purl.org/becyt/ford/1.6 [https], Biología Reproductiva, Sperm Capacitation, CIENCIAS NATURALES Y EXACTAS, Signal Transduction
Abstract

Mammalian sperm acquire fertilizing ability in the female tract in a process known as capacitation. At the molecular level, capacitation is associated with up-regulation of a cAMP-dependent pathway, changes in intracellular pH, intracellular Ca2+, and an increase in tyrosine phosphorylation. How these signaling systems interact during capacitation is not well understood. Results presented in this study indicate that Ca2+ ions have a biphasic role in the regulation of cAMP-dependent signaling. Media without added Ca2+ salts (nominal zero Ca2+) still contain micromolar concentrations of this ion. Sperm incubated in this medium did not undergo PKA activation or the increase in tyrosine phosphorylation suggesting that these phosphorylation pathways require Ca2+. However, chelation of the extracellular Ca2+ traces by EGTA induced both cAMP-dependent phosphorylation and the increase in tyrosine phosphorylation. The EGTA effect in nominal zero Ca2+ media was mimicked by two calmodulin antagonists, W7 and calmidazolium, and by the calcineurin inhibitor cyclosporine A. These results suggest that Ca2+ ions regulate sperm cAMP and tyrosine phosphorylation pathways in a biphasic manner and that some of its effects are mediated by calmodulin. Interestingly, contrary to wild-type mouse sperm, sperm from CatSper1 KO mice underwent PKA activation and an increase in tyrosine phosphorylation upon incubation in nominal zero Ca2+ media. Therefore, sperm lacking Catsper Ca2+ channels behave as wild-type sperm incubated in the presence of EGTA. This latter result suggests that Catsper transports the Ca2+ involved in the regulation of cAMP-dependent and tyrosine phosphorylation pathways required for sperm capacitation. Fil: Navarrete, Felipe A.. University of Massachusetts; Estados Unidos Fil: García Vázquez, Francisco A.. University of Massachusetts; Estados Unidos. Universidad de Murcia; España Fil: Alvau, Antonio. University of Massachusetts; Estados Unidos Fil: Escoffier, Jessica. University of Massachusetts; Estados Unidos Fil: Krapf, Dario. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina Fil: Sánchez Cárdenas, Claudia. Universidad Nacional Autónoma de México; México Fil: Salicioni, Ana M.. University of Massachusetts; Estados Unidos Fil: Darszon, Alberto. Universidad Nacional Autónoma de México; México Fil: Visconti, Pablo E.. University of Massachusetts; Estados Unidos

Published
2015

12. Transient exposure to calcium ionophore enables in vitro fertilization in sterile mouse models

Author

Navarrete, Felipe A., primary, Alvau, Antonio, additional, Lee, Hoi Chang, additional, Levin, Lonny R., additional, Buck, Jochen, additional, Leon, Patricia Martin-De, additional, Santi, Celia M., additional, Krapf, Dario, additional, Mager, Jesse, additional, Fissore, Rafael A., additional, Salicioni, Ana M., additional, Darszon, Alberto, additional, and Visconti, Pablo E., additional

Published
2016
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15. Compartmentalization of Distinct cAMP Signaling Pathways in Mammalian Sperm

Author

Wertheimer, Eva, primary, Krapf, Dario, additional, de la Vega-Beltran, José L., additional, Sánchez-Cárdenas, Claudia, additional, Navarrete, Felipe, additional, Haddad, Douglas, additional, Escoffier, Jessica, additional, Salicioni, Ana M., additional, Levin, Lonny R., additional, Buck, Jochen, additional, Mager, Jesse, additional, Darszon, Alberto, additional, and Visconti, Pablo E., additional

Published
2013
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17. Tamoxifen down-regulates CD36 messenger RNA levels in normal and neoplastic human breast tissues

Author

Silva, Ismael Dale Cotrim Guerreiro da [UNIFESP], Salicioni, Ana M., Russo, I. H., Higgy, N. A., Gebrim, Luiz H [UNIFESP], Russo, J., FOX CHASE CANC CTR, and Universidade Federal de São Paulo (UNIFESP)

Abstract

Tamoxifen (TAM) exerts a long-term suppressive effect on human breast cancer cell proliferation on. To determine whether the effects of TAM are mediated by specific gene activation or repression, normal and tumoral human breast tissues obtained before and during TAM treatment were analysed by differential display technique, Total RNA for differential display analysis was obtained from breast tissues from two women with the diagnosis of estrogen receptor-positive stage II (T(2)N(1)M(0)) infiltrating ductal carcinoma, made by incisional biopsy, followed by modified radical mastectomy performed after a 30-day treatment with TAM (20 mg/day), One 202-bp cDNA band, AP5-1, was present in normal and tumoral biopsy samples, but was absent in breast tissue obtained during TAM treatment, and was confirmed by Northern hybridization, which showed a 2.7-kb band in both patients, The differentially expressed cDNA fragment showed 99% homology to Homo sapiens CD36 gene, a glycoprotein that acts as a receptor for the extracellular matrix proteins thrombospondin-1, collagen types I and IV, and oxidized low-density lipoprotein, These results indicate that the down-regulation of CD36 induced by TAM might represent alternative or additional mechanisms of action of this drug affecting the functions of thrombospondin-1, which is involved in hematogenous tumor spread, invasion and angiogenesis, and oxidized low-density lipoprotein, playing a role in inhibition of arteriosclerosis. The multiple functions affected by the down-regulation of CD36 by TAM warrant the need for additional studies. FOX CHASE CANC CTR,BREAST CANC RES LAB,PHILADELPHIA,PA 19111 UNIV FED SAO PAULO,ESCOLA PAULISTA MED,DEPT GYNECOL,MASTROL GRP,SAO PAULO,BRAZIL UNIV FED SAO PAULO,ESCOLA PAULISTA MED,DEPT GYNECOL,MASTROL GRP,SAO PAULO,BRAZIL Web of Science

Published
1997

28. Impaired Sperm Maturation in Rnase9Knockout Mice1

Author

Westmuckett, Andrew D., Nguyen, Edward B., Herlea-Pana, Oana M., Alvau, Antonio, Salicioni, Ana M., and Moore, Kevin L.

Abstract

Ribonuclease, RNase A family, 9 (RNASE9) is a ribonuclease A superfamily member that is expressed only in the epididymis. It is a small, secreted polypeptide, it lacks ribonuclease activity, and its function(s) is unknown. However, epididymis-specific expression suggests a role in sperm maturation. We generated Rnase9−/−mice to study RNASE9 function in vivo. We confirm that RNASE9 expression is restricted to the epididymis. Within the epididymis, RNASE9 is first detected in midcaput, persists through the distal caput and corpus, and wanes in the cauda. Rnase9−/−mice are born at the expected Mendelian ratio, have normal postnatal growth and development, and have no outwardly apparent phenotype. Spermatogenesis is normal, and Rnase9-null sperm are morphologically normal. Rnase9−/−males have normal fertility in unrestricted mating trials, and fertilization rates in in vitro fertilization assays are indistinguishable from wild-type mice. Visual observations coupled with analyses of sperm velocities shortly after swim out from the corpus shows that motility of Rnase9-null sperm is significantly impaired. However, no differences between wild-type and Rnase9-null sperm are detected by computer-assisted sperm analysis 10–90 min after sperm isolation from the corpus or cauda. Assessment of capacitation-dependent signaling pathways in Rnase9-null sperm showed that, while levels of tyrosine phosphorylation of sperm proteins were normal, there was decreased phosphorylation of protein kinase A substrates upon capacitation compared to wild-type mice. In conclusion, RNASE9 is dispensable for fertility, but the absence of RNASE9 during epididymal transit results in impaired sperm maturation.

Published
2014
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29. Differential role of bovine serum albumin and HCO3- in the regulation of GSK3 alpha during mouse sperm capacitation.

Author

Mohanty G, Sanchez-Cardenas C, Paudel B, Tourzani DA, Salicioni AM, Santi CM, Gervasi MG, Pilsner JR, Darszon A, and Visconti PE

Subjects
Animals, Female, Male, Mice, Calcium metabolism, Cyclic AMP metabolism, Glycogen Synthase Kinase 3 beta metabolism, Mammals, Phosphorylation, Semen metabolism, Sperm Motility, Spermatozoa metabolism, Glycogen Synthase Kinase 3 genetics, Glycogen Synthase Kinase 3 metabolism, Serum Albumin, Bovine pharmacology, Serum Albumin, Bovine metabolism, Sperm Capacitation
Abstract

To become fertile, mammalian sperm are required to undergo capacitation in the female tract or in vitro in defined media containing ions (e.g. HCO3 -, Ca2+, Na+, and Cl-), energy sources (e.g. glucose, pyruvate) and serum albumin (e.g. bovine serum albumin (BSA)). These different molecules initiate sequential and concomitant signaling pathways, leading to capacitation. Physiologically, capacitation induces changes in the sperm motility pattern (e.g. hyperactivation) and prepares sperm for the acrosomal reaction (AR), two events required for fertilization. Molecularly, HCO3 - activates the atypical adenylyl cyclase Adcy10 (aka sAC), increasing cAMP and downstream cAMP-dependent pathways. BSA, on the other hand, induces sperm cholesterol release as well as other signaling pathways. How these signaling events, occurring in different sperm compartments and with different kinetics, coordinate among themselves is not well established. Regarding the AR, recent work has proposed a role for glycogen synthase kinases (GSK3α and GSK3β). GSK3α and GSK3β are inactivated by phosphorylation of residues Ser21 and Ser9, respectively, in their N-terminal domain. Here, we present evidence that GSK3α (but not GSK3β) is present in the anterior head and that it is regulated during capacitation. Interestingly, BSA and HCO3 - regulate GSK3α in opposite directions. While BSA induces a fast GSK3α Ser21 phosphorylation, HCO3 - and cAMP-dependent pathways dephosphorylate this residue. We also show that the HCO3--induced Ser21 dephosphorylation is mediated by hyperpolarization of the sperm plasma membrane potential (Em) and by intracellular pH alkalinization. Previous reports indicate that GSK3 kinases mediate the progesterone-induced AR. Here, we show that GSK3 inhibition also blocks the Ca2+ ionophore ionomycin-induced AR, suggesting a role for GSK3 kinases downstream of the increase in intracellular Ca2+ needed for this exocytotic event. Altogether, our data indicate a temporal and biphasic GSK3α regulation with opposite actions of BSA and HCO3 -. Our results also suggest that this regulation is needed to orchestrate the AR during sperm capacitation., (© The Author(s) 2024. Published by Oxford University Press on behalf of European Society of Human Reproduction and Embryology. All rights reserved. For permissions, please email: journals.permissions@oup.com.)

Published
2024
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30. Signalling pathways involved in sperm capacitation.

Author

Salicioni AM, Platt MD, Wertheimer EV, Arcelay E, Allaire A, Sosnik J, and Visconti PE

Subjects
Acrosome Reaction physiology, Animals, Cell Membrane metabolism, Female, Male, Phosphorylation, Seminal Plasma Proteins metabolism, Mammals metabolism, Signal Transduction physiology, Sperm Capacitation physiology, Spermatozoa metabolism
Abstract

After ejaculation, mammalian sperm have not yet acquired full fertilising capacity. They will require a finite period of residence in the female reproductive tract before they become fertilisation competent. The molecular, biochemical, and physiological changes that occur to sperm while in the female tract are collectively referred to as capacitation. During capacitation, changes in membrane properties, enzyme activities, and motility render spermatozoa responsive to stimuli that induce the acrosome reaction and prepare spermatozoa for penetration of the egg investments prior to fertilisation. These changes are facilitated by the activation of cell signalling cascades in the female reproductive tract in vivo or in defined media in vitro. The purposes of this review are to consider some recent contributions towards our understanding of capacitation, to summarise open questions in this field, and to discuss future avenues of research.

Published
2007

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