The activity of N-acetyl-β-hexosaminidase in boar seminal plasma is linked with semen quality and its suitability for cryopreservation

Wysocki, Paweł; Orzołek, Aleksandra; Strzeżek, J.; Koziorowska-Gilun, Magdalena; Zasiadczyk, Łukasz; Kordan, Władysław

doi:10.1016/j.theriogenology.2014.12.025

Cited by 26 publications

(20 citation statements)

References 36 publications

(42 reference statements)

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“…According to the above, there are reports of proteins related to acrosome integrity as the N-acetyl-β-hexosaminidase [4] and proteins of sperm surface, called Aspartic acid-Glutamine-Histidine, DQH [40] with acrosome protective function. In addition, this finding may be related to the action of L-PGDS in the acrosome membrane.…”

Section: Resultsmentioning

confidence: 99%

“…Some studies have reported significant associations between several seminal proteins and freezability of boar semen, some located in the seminal plasma such as fibronectin type 1 [3] and β subunit of N-acetyl-β-hexosaminidase [4], and others in the sperm cell, such as the heat shock protein 90 alpha [5], the acrosin binding protein and the triosephosphate isomerase protein [6]. …”

Section: Introductionmentioning

confidence: 99%

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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%

Section: Introductionmentioning

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

show abstract

“…The absence of quantitative differences in SP-protein expression between P1 and P2 may be understandable, as P1 and P2 together comprise the first naturally occurring ejaculate fraction (SRF), whose SP has a common origin, albeit having amount differences [5]. to some specific sperm functionalities, as membrane stability and permeability (GLB1L3, [46]; ARSA, [47]), capacitation (HEXB, [48]), acrosome reaction (GP2, [49]), fertilizing ability (LCN-5, [50]) or sperm-zone pellucid binding (ARSA, [51]). …”

Section: Discussionmentioning

confidence: 99%

“…Nucleobinding-1 belongs to a family of proteins with calcium and DNA binding properties [56], but its reproductive function is still unknown. In addition, some of the above related proteins, as HEXB [48], FN1 [57] or AP [58], have been linked to the ability of sperm to overcome cryopreservation.…”

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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“…In addition, the activity of Nacetyl-β-hexosaminidase in fresh seminal plasma has been found to be negatively correlated with sperm motility, survival and lipid peroxidation, which indicates that high levels of β-HEX activity are linked to low resilience to withstand freeze-thawing procedures (Wysocki et al, 2015).…”

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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The activity of N-acetyl-β-hexosaminidase in boar seminal plasma is linked with semen quality and its suitability for cryopreservation

Cited by 26 publications

References 36 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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