Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm

This study evaluated the effect of recombinant heat shock protein HSPA1A on bovine sperm subjected to cooling (for 96 hours at 5 °C) and freezing process. An initial experiment determined the optimal concentration of HSPA1A (0, 15, 30, and 45 µg/mL) supplemented into the OPTIXcell extender, using 18 ejaculates (from 2 bulls) refrigerated for 96 hours. Subsequently, the effect of supplementing 45 µg/mL of HSPA1A (optimal concentration) into the OPTIXcell extender was evaluated, using 6 ejaculates subjected to freezing via static liquid nitrogen vapor. The results indicated that all concentrations of HSPA1A produced higher values for kinematic variables, viability, and acrosomal integrity compared to the control during 96 hours of refrigeration (p < 0.05). Additionally, 45 µg/mL HSPA1A showed a higher beat cross frequency (BCF) than the other HSPA1A concentrations (p < 0.05). After thawing, the motilities, BCF, and cryoresistance indices for motility, viability, and acrosomal integrity were higher in samples frozen with HSPA1A compared to the control (p < 0.05). In conclusion, the recombinant HSPA1A protein improved the motility, viability, and acrosomal integrity of refrigerated and cryopreserved bull sperm.

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Main Authors: Sancho, José L., Carrión, Edison P., Largo, Estefany M., Pando, Heydi I., Duma, Mauricio, Vallecillo, Antonio J., Galarza, Diego A.
Format: Digital revista
Language:spa
Published: Asociacion Latinoamericana de Produccion Animal 2024
Online Access:https://ojs.alpa.uy/index.php/ojs_files/article/view/3338
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country Uruguay
countrycode UY
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databasecode rev-alpa
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region America del Sur
libraryname Biblioteca ALPA
language spa
format Digital
author Sancho, José L.
Carrión, Edison P.
Largo, Estefany M.
Pando, Heydi I.
Duma, Mauricio
Vallecillo, Antonio J.
Galarza, Diego A.
spellingShingle Sancho, José L.
Carrión, Edison P.
Largo, Estefany M.
Pando, Heydi I.
Duma, Mauricio
Vallecillo, Antonio J.
Galarza, Diego A.
Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm
author_facet Sancho, José L.
Carrión, Edison P.
Largo, Estefany M.
Pando, Heydi I.
Duma, Mauricio
Vallecillo, Antonio J.
Galarza, Diego A.
author_sort Sancho, José L.
title Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm
title_short Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm
title_full Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm
title_fullStr Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm
title_full_unstemmed Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm
title_sort recombinant heat shock protein hspa1a increases cryoresistance of bull sperm
description This study evaluated the effect of recombinant heat shock protein HSPA1A on bovine sperm subjected to cooling (for 96 hours at 5 °C) and freezing process. An initial experiment determined the optimal concentration of HSPA1A (0, 15, 30, and 45 µg/mL) supplemented into the OPTIXcell extender, using 18 ejaculates (from 2 bulls) refrigerated for 96 hours. Subsequently, the effect of supplementing 45 µg/mL of HSPA1A (optimal concentration) into the OPTIXcell extender was evaluated, using 6 ejaculates subjected to freezing via static liquid nitrogen vapor. The results indicated that all concentrations of HSPA1A produced higher values for kinematic variables, viability, and acrosomal integrity compared to the control during 96 hours of refrigeration (p < 0.05). Additionally, 45 µg/mL HSPA1A showed a higher beat cross frequency (BCF) than the other HSPA1A concentrations (p < 0.05). After thawing, the motilities, BCF, and cryoresistance indices for motility, viability, and acrosomal integrity were higher in samples frozen with HSPA1A compared to the control (p < 0.05). In conclusion, the recombinant HSPA1A protein improved the motility, viability, and acrosomal integrity of refrigerated and cryopreserved bull sperm.
publisher Asociacion Latinoamericana de Produccion Animal
publishDate 2024
url https://ojs.alpa.uy/index.php/ojs_files/article/view/3338
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spelling oai:ojs.ojs.alpa.uy:article-33382024-11-22T22:12:32Z Recombinant heat shock protein HSPA1A increases cryoresistance of bull sperm La proteína recombinante de choque térmico HSPA1A incrementa la crioresistencia de espermatozoides de toro A proteína de choque térmico recombinante HSPA1A aumenta a criorresistência do esperma de touro Sancho, José L. Carrión, Edison P. Largo, Estefany M. Pando, Heydi I. Duma, Mauricio Vallecillo, Antonio J. Galarza, Diego A. HSPA1A sperm cryoresistance bovines HSPA1A crioresistencia espermática bovinos HSPA1A criorresistência espermática bovinos This study evaluated the effect of recombinant heat shock protein HSPA1A on bovine sperm subjected to cooling (for 96 hours at 5 °C) and freezing process. An initial experiment determined the optimal concentration of HSPA1A (0, 15, 30, and 45 µg/mL) supplemented into the OPTIXcell extender, using 18 ejaculates (from 2 bulls) refrigerated for 96 hours. Subsequently, the effect of supplementing 45 µg/mL of HSPA1A (optimal concentration) into the OPTIXcell extender was evaluated, using 6 ejaculates subjected to freezing via static liquid nitrogen vapor. The results indicated that all concentrations of HSPA1A produced higher values for kinematic variables, viability, and acrosomal integrity compared to the control during 96 hours of refrigeration (p < 0.05). Additionally, 45 µg/mL HSPA1A showed a higher beat cross frequency (BCF) than the other HSPA1A concentrations (p < 0.05). After thawing, the motilities, BCF, and cryoresistance indices for motility, viability, and acrosomal integrity were higher in samples frozen with HSPA1A compared to the control (p < 0.05). In conclusion, the recombinant HSPA1A protein improved the motility, viability, and acrosomal integrity of refrigerated and cryopreserved bull sperm. Esta investigación evaluó el efecto de la proteína recombinante de choque térmico HSPA1A en espermatozoides bovinos sometidos a refrigeración durante 96 horas (5 °C), y congelación. Un experimento inicial determinó la concentración óptima de HSPA1A (0, 15, 30, y 45 µg/mL) suplementado al diluyente OPTIXcell, utilizando 18 eyaculados (de 2 toros) refrigerados durante 96 horas. Posteriormente, se evaluó el efecto de la suplementación de 45 µg/mL de HSPA1A (como concentración óptima) al diluyente OPTIXcell, utilizando 6 eyaculados sometidos a congelación mediante vapores de nitrógeno líquido estático. Los resultados indicaron que todas las concentraciones de HSPA1A produjeron mayores valores de las variables cinemáticas, de viabilidad y de integridad acrosomal que su control, durante 96 horas de refrigeración (p < 0,05). Además, con 45 µg/mL HSPA1A mostraron un valor más alto de frecuencia de batida de flagelo (BCF) que las otras concentraciones de HSPA1A (p < 0,05). Tras la descongelación, las motilidades, la BCF y los índices de crioresistencia de motilidad, viabilidad e integridad acrosomal fueron mayores en muestras congeladas con la proteína HSPA1A comparadas con el control (p < 0,05). En conclusión, la proteína recombinante HSPA1A mejoró la motilidad, viabilidad e integridad acrosomal de espermatozoides de toro refrigerados y congelados. Esta pesquisa avaliou o efeito da proteína de choque térmico recombinante HSPA1A em espermatozóides bovinos submetidos à refrigeração por 96 horas (5 °C) e ao congelamento. Um experimento inicial determinou a concentração ideal de HSPA1A (0, 15, 30 e 45 µg/mL) suplementado com diluente OPTIXcell, utilizando 18 ejaculados (de 2 touros) refrigerados por 96 horas. Posteriormente, avaliou-se o efeito da suplementação de 45 µg/mL de HSPA1A (como concentração ideal) ao diluente OPTIXcell, utilizando 6 ejaculados submetidos ao congelamento com vapores de nitrogênio líquido estático. Os resultados indicaram que todas as concentrações de HSPA1A produziram valores superiores das variáveis ​​cinemáticas, viabilidade e integridade acrossomal do que seu controle, durante 96 horas de refrigeração (p < 0,05). Além disso, com 45 µg/mL de HSPA1A apresentaram um valor de frequência de batimento do flagelo (BCF) mais elevado do que as outras concentrações de HSPA1A (p < 0,05). Após o descongelamento, as motilidades, BCF e índices de criorresistência de motilidade, viabilidade e integridade acrossomal foram maiores nas amostras congeladas com proteína HSPA1A em comparação ao controle (p < 0,05). Em conclusão, a proteína recombinante HSPA1A melhorou a motilidade, viabilidade e integridade acrossomal de espermatozóides bovinos refrigerados e congelados. Asociacion Latinoamericana de Produccion Animal 2024-10-13 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Text Texto Articulo cientifico original Texto application/pdf https://ojs.alpa.uy/index.php/ojs_files/article/view/3338 10.53588/alpa.320512 Archivos Latinoamericanos de Producción Animal; Vol. 32 Núm. Supl 1 (2024): V Congreso Internacional de Producción Animal Especializada en Bovinos ; 121-126 Archivos Latinoamericanos de Producción Animal; Vol. 32 No. Supl 1 (2024): 5th International Congress on Animal Production Specialized in Bovines; 121-126 Archivos Latinoamericanos de Producción Animal; v. 32 n. Supl 1 (2024): V Congresso Internacional de Produção Animal Especializado em Bovinos; 121-126 2075-8359 1022-1301 spa https://ojs.alpa.uy/index.php/ojs_files/article/view/3338/1999 Copyright (c) 2024 José L. Sancho, Edison P. Carrión, Estefany M. Largo, Heydi I. Pando, Mauricio Duma, Antonio J. Vallecillo, Diego A. Galarza https://creativecommons.org/licenses/by-nc-sa/4.0