Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
Caltrin is a small and basic protein of the seminal vesicle secretion that inhibits sperm calcium uptake. The influence of rat caltrin on sperm physiological processes related to fertilizing competence was studied by examining its effect on 1) spontaneous acrosomal exocytosis, 2) protein tyrosine ph...
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2008
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063363_v79_n3_p493_Dematteis http://hdl.handle.net/20.500.12110/paper_00063363_v79_n3_p493_Dematteis |
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paper:paper_00063363_v79_n3_p493_Dematteis2023-06-08T14:31:08Z Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation Cuasnicú, Patricia S. Acrosome reaction Calcium Male reproductive tract Seminal vesicles Sperm capacitation calcium ionophore caltrin hyaluronidase inhibitor protein unclassified drug acrosome animal cell article cell interaction controlled study enzyme inhibition enzyme release exocytosis female fertilization immunoelectron microscopy immunofluorescence male nonhuman oocyte priority journal protein localization protein phosphorylation rat sperm spermatozoon capacitation zona pellucida Rattus Caltrin is a small and basic protein of the seminal vesicle secretion that inhibits sperm calcium uptake. The influence of rat caltrin on sperm physiological processes related to fertilizing competence was studied by examining its effect on 1) spontaneous acrosomal exocytosis, 2) protein tyrosine phosphorylation, and 3) sperm-egg interaction. Results show that the presence of caltrin during in vitro capacitation both reduced the rate of spontaneous acrosomal exocytosis without altering the pattern of protein tyrosine phosphorylation, and enhanced the sperm ability to bind to the zona pellucida (ZP). The significantly higher proportion of sperm with intact acrosome observed in the presence of caltrin was accompanied by a strong inhibition in the acrosomal hyaluronidase release. Enhancement of sperm-ZP binding was evident by the increase in the percentage of eggs with bound spermatozoa as well as in the number of bound sperm per egg. Similar results were obtained when the assays were performed using spermatozoa preincubated with caltrin and then washed to remove the unbound protein, indicating that the sperm-bound caltrin was the one involved in both acrosomal exocytosis inhibition and sperm-ZP binding enhancement. Caltrin bound to the sperm head was partially released during the acrosomal exocytosis induced by Ca-ionophore A23187. Indirect immunofluorescence and immunoelectron microscopy studies revealed that caltrin molecules distributed on the dorsal sperm surface disappeared after ionophore exposure, whereas those on the ventral region remained in this localization after the treatment. The present data suggest that rat caltrin molecules bound to the sperm head during ejaculation prevent the occurrence of the spontaneous acrosomal exocytosis along the female reproductive tract. Consequently, more competent spermatozoa with intact and functional acrosome would be available in the oviduct to participate in fertilization. © 2008 by the Society for the Study of Reproduction, Inc. Fil:Cuasnicu, P.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063363_v79_n3_p493_Dematteis http://hdl.handle.net/20.500.12110/paper_00063363_v79_n3_p493_Dematteis |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Acrosome reaction Calcium Male reproductive tract Seminal vesicles Sperm capacitation calcium ionophore caltrin hyaluronidase inhibitor protein unclassified drug acrosome animal cell article cell interaction controlled study enzyme inhibition enzyme release exocytosis female fertilization immunoelectron microscopy immunofluorescence male nonhuman oocyte priority journal protein localization protein phosphorylation rat sperm spermatozoon capacitation zona pellucida Rattus |
| spellingShingle |
Acrosome reaction Calcium Male reproductive tract Seminal vesicles Sperm capacitation calcium ionophore caltrin hyaluronidase inhibitor protein unclassified drug acrosome animal cell article cell interaction controlled study enzyme inhibition enzyme release exocytosis female fertilization immunoelectron microscopy immunofluorescence male nonhuman oocyte priority journal protein localization protein phosphorylation rat sperm spermatozoon capacitation zona pellucida Rattus Cuasnicú, Patricia S. Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation |
| topic_facet |
Acrosome reaction Calcium Male reproductive tract Seminal vesicles Sperm capacitation calcium ionophore caltrin hyaluronidase inhibitor protein unclassified drug acrosome animal cell article cell interaction controlled study enzyme inhibition enzyme release exocytosis female fertilization immunoelectron microscopy immunofluorescence male nonhuman oocyte priority journal protein localization protein phosphorylation rat sperm spermatozoon capacitation zona pellucida Rattus |
| description |
Caltrin is a small and basic protein of the seminal vesicle secretion that inhibits sperm calcium uptake. The influence of rat caltrin on sperm physiological processes related to fertilizing competence was studied by examining its effect on 1) spontaneous acrosomal exocytosis, 2) protein tyrosine phosphorylation, and 3) sperm-egg interaction. Results show that the presence of caltrin during in vitro capacitation both reduced the rate of spontaneous acrosomal exocytosis without altering the pattern of protein tyrosine phosphorylation, and enhanced the sperm ability to bind to the zona pellucida (ZP). The significantly higher proportion of sperm with intact acrosome observed in the presence of caltrin was accompanied by a strong inhibition in the acrosomal hyaluronidase release. Enhancement of sperm-ZP binding was evident by the increase in the percentage of eggs with bound spermatozoa as well as in the number of bound sperm per egg. Similar results were obtained when the assays were performed using spermatozoa preincubated with caltrin and then washed to remove the unbound protein, indicating that the sperm-bound caltrin was the one involved in both acrosomal exocytosis inhibition and sperm-ZP binding enhancement. Caltrin bound to the sperm head was partially released during the acrosomal exocytosis induced by Ca-ionophore A23187. Indirect immunofluorescence and immunoelectron microscopy studies revealed that caltrin molecules distributed on the dorsal sperm surface disappeared after ionophore exposure, whereas those on the ventral region remained in this localization after the treatment. The present data suggest that rat caltrin molecules bound to the sperm head during ejaculation prevent the occurrence of the spontaneous acrosomal exocytosis along the female reproductive tract. Consequently, more competent spermatozoa with intact and functional acrosome would be available in the oviduct to participate in fertilization. © 2008 by the Society for the Study of Reproduction, Inc. |
| author |
Cuasnicú, Patricia S. |
| author_facet |
Cuasnicú, Patricia S. |
| author_sort |
Cuasnicú, Patricia S. |
| title |
Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation |
| title_short |
Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation |
| title_full |
Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation |
| title_fullStr |
Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation |
| title_full_unstemmed |
Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation |
| title_sort |
rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation |
| publishDate |
2008 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063363_v79_n3_p493_Dematteis http://hdl.handle.net/20.500.12110/paper_00063363_v79_n3_p493_Dematteis |
| work_keys_str_mv |
AT cuasnicupatricias ratcaltrinproteinmodulatestheacrosomalexocytosisduringspermcapacitation |
| _version_ |
1768544711918747648 |