Relationship of sperm small heat-shock protein 10 and voltage-dependent anion channel 2 with semen freezability in boars

Vilagran, Ingrid; Yeste, Marc; Sancho, S.; Casas, Isabel; Álamo, Maria Montserrat Rivera del; Bonet, Sergi

doi:10.1016/j.theriogenology.2014.04.023

Cited by 53 publications

(42 citation statements)

References 49 publications

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“…There exist reports that associate high intracellular levels of HSP90a with motility [5, 23], and in the present study the SPZ of MLF combinations showed higher amount of this protein in the seminal plasma after 3 h incubation, possibly due to leakage from inside the cell. Other sperm proteins recently associated with freezability and motility are voltage-dependent anion channel 2 which regulate the permeability of the membrane [41], the acrosin binding protein and the triosephosphate isomerase protein connected to the capacitation process [6]. …”

Section: Resultsmentioning

confidence: 99%

Relationship between HSP90a, NPC2 and L-PGDS proteins to boar semen freezability

Valencia

Gómez

López

et al. 2017

J Animal Sci Biotechnol

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BackgroundThe purpose of this study was to determine the association of three proteins involved in sperm function on the freezability of porcine semen: the heat shock protein 90 alpha (HSP90a), the Niemann-Pick disease type C2 protein (NPC2), and lipocalin-type prostaglandin D synthase (L-PGDS).Six adult boars (each boar was ejaculated three times, 18 in total) were classified by freezability based on the percentage of functionally competent sperm. The male semen with highest freezability (MHF) and the male semen with lowest freezability (MLF) were centrifuged immediately after collection to separate seminal plasma and spermatozoa to make four possible combinations of these two components and to incubate them for 3 h, adjusting the temperature to 17 °C, to freeze them afterwards. The quantification of proteins was performed in two stages: at zero and at 3 h after incubation of the four combinations.ResultsThe spermatozoa × incubation time (IT) interaction only had effect (P < 0.01) on HSP90a levels; this protein increased in seminal plasma, after 3 h of incubation, in larger quantity (P < 0.05) in combinations with MLF spermatozoa. In relation with the NPC2 protein, two isoforms of 16 and 19 kDa were identified. The 19 kDa isoform was affected (P < 0.01) only by the seminal plasma × IT interaction, with superior values (P < 0.01) both at zero and three hours of incubation, in the combinations with MHF seminal plasma; and 16 kDa isoform was affected (P < 0.01) only by the IT with reduction after 3 h of incubation. The levels of L-PGDS was affected (P < 0.01) only by the spermatozoa × IT interaction, which reduced (P < 0.01) in combinations with MLF spermatozoa after 3 h of incubation.ConclusionsIt is possible to consider that the three proteins evaluated were associated with freezability of boar semen due, especially, to the fact that mixtures with MLF spermatozoa showed greater increase levels of the HSP90a protein and reduction of L-PGDS in plasma. In addition, the seminal plasma of MHF had higher concentration of the NPC2 of 19 kDa protein, which was reduced by incubating with MHF spermatozoa.

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Section: Resultsmentioning

confidence: 99%

Relationship between HSP90a, NPC2 and L-PGDS proteins to boar semen freezability

Valencia

Gómez

López

et al. 2017

J Animal Sci Biotechnol

View full text Add to dashboard Cite

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“…Other five of these 18 SP-proteins (EGF-like repeat and discoidin I-like domain-containing protein 3, Putative phospholipase B-like 2 isoform 1, Prominin-2, Ezrin and Syntaxinbinding protein 2) have been related with sperm capacitation [63][64][65][66][67]. Heat shock cognate 71 kDa is a protein related to environmental or physiological stresses [68] synthesized by sperm cells [69] that has been recently related to boar sperm cryotolerance [70]. Finally, Ectonucleotide pyrophosphatase/phosphodiesterase family member is an ATPhydrolyzing enzyme described in epididymis suggesting that this protein could be involved in the modulation of the epididymal environment [71].…”

Section: Discussionmentioning

confidence: 99%

Characterization of the porcine seminal plasma proteome comparing ejaculate portions

Pérez-Patiño

Barranco

Parrilla

et al. 2016

Journal of Proteomics

102

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Full identification of SP-proteins remains challenging, particularly in some livestock species such as porcine. This experimental study aims to provide an extensive proteomic analysis of boar SP and to generate a public accessible database of boar SP-proteome. A SP-pool from 33 entire ejaculates from 11 boars (3 ejaculates per boar) was analyzed to characterize the boar SP-proteome. Moreover, 20 ejaculates collected in fractions (P1: first 10 mL of sperm rich ejaculate fraction (SRF), P2: rest of SRF and P3: post-SRF) from 5 boars (4 ejaculates per boar) were analyzed to evaluate differentially expressed SP-proteins among portions. SP-samples were subjected to a combination of SEC, 1-D SDS PAGE and NanoLC-ESI-MS/MS followed by functional bioinformatics analysis.The identified proteins were quantified from normalized LFQ intensity data. A total of 33,557 spectra corresponding to 8,189 peptides and 536 SP-proteins were identified with ≥ 95% Confidence (Unused Score > 1.3) and a false discovery rate (FDR) ≤ 1%. Of the 536 SP-proteins, 409 were identified in Sus Scrofa taxonomy and 374 of them were Biological Significance: This proteomic study provides the major characterization of the boar SP-proteome with more than 250 proteins first reported. The boar SP-proteome is described so that a spectral library can be built for relative 'label free' protein quantitation with SWATH approach. This proteomic profiling allows the creation of a publicly accessible database of the boar SP-proteome, as a first step for further understanding the role of SP-proteins in reproductive outcomes as well as for identification of biomarkers for sperm quality and fertility.

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“…Thus far, the following sperm freezability markers have been identified: heat shock protein 90 (HSP90AA1), acrosin binding protein (ACRBP), triosephosphate isomerase (TPI) and voltage-dependent anion channel 2 (VDAC2; Casas et al, 2010a;Vilagran et al, 2013Vilagran et al, , 2014. Acrosin activity in fresh sperm is also related to ejaculate freezability, the ejaculates presenting higher cryotolerance being those with higher acrosin activity (Estrada et al, 2015;Pinart et al, 2015b).…”

Section: Ejaculate Resilience To Withstand Cryopreservationmentioning

confidence: 99%

State-of-the-art of boar sperm preservation in liquid and frozen state

Yeste

2017

Anim Reprod

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Pig breeding is mainly conducted through Artificial Insemination (AI) in Western and developing countries. Apart from requiring specific catheters and trained staff, preserving boar semen in proper conditions is needed to ensure high reproductive performances. Although, at present, boar sperm may be preserved in liquid (15-17ºC) or frozen states, more than 95% of AIs are conducted using liquid semen. The present work reviews the state-the-art of these two preservation technologies. Thus, the composition and types of extenders for liquid-stored semen are discussed, together with the specific requirements for boar sperm, which are stored at 15-17ºC. Commercial extenders for liquid semen are compared and the effects of storage on sperm quality are also summarised. In the second part of the manuscript, the main features of boar sperm cryopreservation are described and reference to cryodamage is also made. These cryoinjuries mainly affect sperm motility, membrane permeability and chromatin integrity. Furthermore, the individual variability in the sperm resilience to withstand cryopreservation procedures is reviewed and a brief summary about freezability markers is also included. Final sections briefly discuss the improvement of freezing extenders with additives, such as seminal plasma and antioxidants, and highlight the relevance of using a proper AI technique to avoid dramatic drops in reproductive performance.

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Relationship of sperm small heat-shock protein 10 and voltage-dependent anion channel 2 with semen freezability in boars

Cited by 53 publications

References 49 publications

Relationship between HSP90a, NPC2 and L-PGDS proteins to boar semen freezability

Relationship between HSP90a, NPC2 and L-PGDS proteins to boar semen freezability

Characterization of the porcine seminal plasma proteome comparing ejaculate portions

State-of-the-art of boar sperm preservation in liquid and frozen state

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