Fator do plasma seminal associado à integridade de membrana de espermatozóides suínos pós-descongelamento

Bianchi, Ivan; Collares, Tiago; Campos, Vinícius Farias; Cavalcanti, Paulo Varoni; Kaefer, Cristian; Corrêa, Érico Kunde; Dellagostin, Odir A.; Lucia, Thomaz; Deschamps, João Carlos; Corrêa, M. N.

doi:10.1590/s0102-09352008000200017

Cited by 4 publications

(4 citation statements)

References 19 publications

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“…The good results for the seminal quality associated with the 25 kDa protein in terms of plasmatic membrane integrity can be explained by the finds reported by (Bianchi et al, 2008). In this case, the authors relayed that in situ database, a protein group was observed with a molecular weight of approximately 26 kDa called Sialoproteins that have the ability to inhibit the agglutination of heads from the spermatozoids.…”

Section: Discussionmentioning

confidence: 86%

“…This fact demonstrates that even though the spermatozoids had good motility, they were not ready to be functional, especially when considering the proteins 25 and 50 kDa, for which the cell feasibility was the lowest. According to (Bianchi et al, 2008), when considering in silico database, a protein group was found with a molecular weight of approximately 26 kDa called Sialoproteins that has the ability to inhibit the heads'agglutination of the spermatozoids. According to (Strzeżek et al, 2002), the deficiency of this group can compromise the potential spermatic fertilization.…”

Section: Discussionmentioning

confidence: 99%

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Protein profile as a quality indicator of cryopreserved semen from Tambaqui Colossoma macropomum (Cuvier, 1818)

Galo

Corcini

et al. 2020

Braz. J. Biol.

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The aim of this study was to evaluate the association between proteins in the seminal plasma of tambaqui Colossoma macropomum (Cuvier, 1818) with seminal quality indicators after thawing. The semen was cryopreserved with a dilution based on BTS with 8% DMSO. A 200 µL sample of semen from each animal was diluted in 800 µL BTS, centrifuged at 800 rpm, and the supernatant was cryopreserved to further analyze of the protein profile of seminal plasma through one-dimensional electrophoresis (SDS-PAGE). After 15 days of cryopreservation, a cryopreserved semen straw was thawed to analyze both qualitative and quantitative parameters. When considering all collections, the SDS-PAGE identified 15 protein bands in the seminal plasma of tambaqui. When the interaction (presence or absence) between proteins observed in the seminal plasma and the post thawed spermatic parameters was evaluated, we observed a great influence of the presence of proteins on spermatic quality. A greater (P<0.05) fertilization rate was observed with the presence of proteins 12, 34, 44, 85, and 90 kDa. Proteins in seminal plasma of tambaqui influenced the spermatic quality after thawing, and thus, they can be utilized as an indicator of sperm quality, especially the proteins with a molecular weight ≤ 50 kDa.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Protein profile as a quality indicator of cryopreserved semen from Tambaqui Colossoma macropomum (Cuvier, 1818)

Galo

Corcini

et al. 2020

Braz. J. Biol.

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“…Two spermadhesins presenting 26 kDa (pI 6.2) and 55 kDa (pI 4.5) were identified as potential markers for fertility in this species, as its presence is associated with high prolificity rates (Flowers & Turner, 2001). In addition, the 26 kDa protein was related to better sperm membrane integrity after freezingthawing processes (Bianchi et al 2008). The characterization of proteins present in the seminal plasma may provide essential information for identification of molecular determinants of fertility.…”

Section: Introductionmentioning

confidence: 99%

Protein profile of the seminal plasma of collared peccaries (Pecari tajacu Linnaeus, 1758)

Santos¹,

Sousa²,

Martins³

et al. 2014

Reproduction

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This study was conducted to characterize the major proteins of the peccary seminal plasma, based on the semen samples collected from nine adult and reproductively sound animals. Our approach included the use of two-dimensional electrophoresis followed by Coomassie blue staining and analysis of polypeptide maps with PDQuest Software (Bio-Rad). Proteins were identified by tandem mass spectrometry (LC-MS/MS). We detected 179 protein spots per gel and 98 spots were identified by mass spectrometry, corresponding to 23 different proteins. The combined intensity of those spots accounted for 56.2G6% of the intensities of all spots and 60.9% of the intensities of spots presented in every protein map. Protein spots identified as clusterin represented 19.7G8.3% of the integrated optical densities of all spots detected in the seminal plasma maps. There was a negative association (rZK0.87; P!0.05) between the intensity of a clusterin spot and the percentage of sperm with functional membrane. Spermadhesin porcine seminal plasma protein 1 and bodhesin 2 comprised 5.4G1.9 and 8.8G3.9% of the total intensity of all spots respectively. Many proteins appeared in a polymorphic pattern, such as clusterin (27 spots), epididymal secretory glutathione peroxidase (ten spots), inter-a-trypsin inhibitor (12 spots), and IgG-binding protein (ten spots), among others. In conclusion, we presently describe the major seminal plasma proteome of the peccary, which exhibits a distinct high expression of clusterin isoforms. Knowledge of wild species reproductive biology is crucial for an understanding of their survival strategies and adaptation in a changing environment.

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“…Proteins present in the seminal plasma are described as having an important role for the maintenance of sperm motility in bulls (BAAS et al, 1983;JOBIM et al, 2004;MOURA, 2005;MOURA et al, 2007), rams (GRAHAM, 1994;CARDOZO et al, 2006) and boars (STRZEZEK et al, 1992;KORDAN et al, 1998). Additionally, such proteins would be associated to increased spermatozoa resistance to cold shock, in boars (BERGER et al, 1985) and rams (BARRIOS et al, 2000) and thus could be considered as cryomarkers for the mentioned species (RONCOLETTA et al, 1999;JOBIM et al, 2004;BARRIER-BATTUT et al, 2005;MOURA, 2005;BIANCHI et al, 2008). In fish, the acquisition of sperm motility is associated to the presence of some glycoproteins in the seminal plasma, which act as sperm immobilizing factor, as described for the Nile tilapia (Oreochromis niloticus) (MOCHIDA et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

ASSOCIAÇÃO ENTRE A PRESENÇA DE UM FATOR DE 38 kDa NO PLASMA SEMINAL E A INIBIÇÃO DA MOTILIDADE ESPERMÁTICA NO JUNDIÁ Rhamdia quelen

et al. 2010

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Protein factors have been identified in the seminal plasma of fish and mammal species and, in some situations, associated to sperm quality indicators. However, for jundiá fish (Rhamdia quelen), such factors and those potential associations remain unknown. In the present study, we aimed to identify some protein factors present in the seminal plasma of jundiá fish and to evaluate their association to sperm motility. SDS-PAGE was used to identify 14 bands, with molecular weight ranging from 217.1 to 7.1 kDa.Sperm motility was evaluated for 21 males. Four protein bands (81.5; 60.4; 33.6; and 25.5 kDa) were present in all seminal plasma samples. One protein band with molecular weight of 38.3 kDa was associated to reduced sperm motility of jundiá (P<0.01), since it was detected in 91.4% of the samples having motility lower than 80%. These results suggest that this seminal protein band associated to lower sperm motility may be considered a potential biochemical marker for sperm quality.

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Fator do plasma seminal associado à integridade de membrana de espermatozóides suínos pós-descongelamento

Cited by 4 publications

References 19 publications

Protein profile as a quality indicator of cryopreserved semen from Tambaqui Colossoma macropomum (Cuvier, 1818)

Protein profile as a quality indicator of cryopreserved semen from Tambaqui Colossoma macropomum (Cuvier, 1818)

Protein profile of the seminal plasma of collared peccaries (Pecari tajacu Linnaeus, 1758)

ASSOCIAÇÃO ENTRE A PRESENÇA DE UM FATOR DE 38 kDa NO PLASMA SEMINAL E A INIBIÇÃO DA MOTILIDADE ESPERMÁTICA NO JUNDIÁ Rhamdia quelen

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