Proteases and Proteases Inhibitors of Semen - A Review

Gurupriya, Vijayasaraswathy S.

doi:10.14737/journal.aavs/2014/2.8.447.456

Cited by 7 publications

(5 citation statements)

References 84 publications

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“…Zahn et al [46] stated that the protein with a MW of about 53-55 kDa is proacrosin. Gurupriya et al [47] stated that proacrosin is found in the acrosome. When the sperm acrosome is damaged, or there is early capacitation at the time of freeze-thawing, it can stimulate the premature transformation of proacrosin into the enzymatic protein called acrosin.…”

Section: The Analysis Of Sperm Protein By Sds-pagementioning

confidence: 99%

Sperm protein markers for Holstein bull fertility at National Artificial Insemination Centers in Indonesia

et al. 2020

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Background and Aim: Holstein cows and heifers are widely bred in Indonesia by artificial insemination (AI) to increase population and milk production. Sperm fertility is modulated by genetic factors, but the analysis of sperm quality is still based on macro- and microscopic characteristics. This study aimed to analyze both sperm quality and proteins of Holstein bulls at different fertility levels. Materials and Methods: The frozen semen samples were collected from the Indonesia National AI Center. They were classified based on the reproductive efficiency data and were grouped into high fertile (HF) and low fertile (LF). Sperm qualities were evaluated by microscopic evaluation. The Holstein sperm proteins were extracted using phenylmethanesulfonyl fluoride as a protease inhibitor and the benzidine detergent extraction method. Discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was conducted to analyze the molecular weights (MWs) of the sperm proteins. The data obtained were analyzed by a t-test using the one-factor bull fertility level, and Spearman's correlation analysis was used to identify the correlation between the sperm microscopic evaluation parameters and protein bands. Results: The sperm motility post-freeze thawing was not significantly different between the HF and LF (p>0.05). The HF level had a higher percentage of viability, intact plasma membrane integrity, and intact acrosomes than the LF (p<0.05). Five protein bands were found in the SDS-PAGE of sperm proteins of Holstein bulls with different concentrations. Sperm proteins with MWs of 17.51 kDa, 14.87 kDa, 33.71 kDa, and 41.97 kDa were abundant in the Holstein bulls with an HF level, while 55 kDa proteins were abundant in the LF level of Holstein bulls. The sperm of Holstein bulls in the HF level contained proteins of about 33.71 kDa that were not detected in the LF. Conclusion: The sperm protein with a molecular weight of 33.71 kDa was predicted to be a specific protein biomarker that influences bull fertility. Sperm fertilization abilities were also determined by the sperm proteins, the morphology of sperm acrosomes, and the quality of plasma membranes. This method can be used to select bulls with high fertility to increase the population of Holstein bulls.

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Section: The Analysis Of Sperm Protein By Sds-pagementioning

confidence: 99%

Sperm protein markers for Holstein bull fertility at National Artificial Insemination Centers in Indonesia

et al. 2020

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“…Proteomics profiles reflect sperm functional traits (Intasqui et al, ) and highly differ between species. A significant number of seminal proteases and protease inhibitors are suspected to participate in the regulation of maturation/activation, release, and protection of sperm (Cesari, Monclus Mde, Tejon, Clementi, & Fornes, ; Gurupriya et al, ; Laflamme & Wolfner, ). In many species, acrosin is an essential trypsin‐like serine protease stored in the sperm acrosome as an inactive zymogen form, proacrosin, before its activation by limited proteolysis that releases the active acrosin at the time of fertilization (Bozzola et al, ; Slowinska, Olczak, Liszewska, Watorek, & Ciereszko, ).…”

Section: Introductionmentioning

confidence: 99%

The seminal acrosin‐inhibitor ClTI1/SPINK2 is a fertility‐associated marker in the chicken

Thélie

Réhault-Godbert

Poirier

et al. 2019

Molecular Reproduction Devel

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The seminal plasma is a very complex fluid, which surrounds sperm in semen. It contains numerous proteins including proteases and protease inhibitors that regulate proteolytic processes associated with protein activation and degradation. We previously identified a seminal protein, chicken liver trypsin inhibitor 1 (ClTI‐1) over expressed in semen of roosters with high fertility, suggesting a role in male fertility. In the present study, we showed that ClTI‐1 gene is actually SPINK2. Using normal healthy adult roosters, we showed that SPINK2 amount in seminal plasma was positively correlated with male fertility in chicken lines with highly contrasted genetic backgrounds (broiler and layer lines). Using affinity chromatography combined to mass spectrometry analysis and kinetic assays, we demonstrated for the first time that two chicken acrosin isoforms (acrosin and acrosin‐like proteins) are the physiological serine protease targets of SPINK2 inhibitor. SPINK2 transcript was overexpressed all along the male tract, and the protein was present in the lumen as expected for secreted proteins. Altogether, these data emphasize the role of seminal SPINK2 Kazal‐type inhibitor as an important actor of fertility in birds through its inhibitory action on acrosin isoforms proteins.

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“…Denaturation of proteins during cryopreservation results in the leakage of protease from the lysosomes found in the acrosome leading to loss of membrane integrity (32). During cryopreservation, some proteases and protease inhibitors are prematurely activated; thus, natural proteolysis regulation in cryopreserved semen is compromised (33). This may also be due to the heterogenicity of seminal plasma and sperm in the mammalian ejaculate (34) The protein changes in sperm may also be due to the difference in their responsiveness to seminal plasma (35).…”

Section: Discussionmentioning

confidence: 99%

The cryopreservation process induces alterations in proteins associated with bull sperm quality: The equilibration process could be a probable critical control point

et al. 2022

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The present study quantitatively characterized the proteomic changes in bull spermatozoa induced by the cryopreservation process. We performed high-throughput comparative global proteomic profiling of freshly ejaculated (before cryopreservation), equilibrated (refrigerated storage; during cryopreservation), and frozen (ultralow temperature; after cryopreservation) bull spermatozoa. Using the liquid chromatography–mass spectrometry (LC-MS/MS) technique, a total of 1,692, 1,415, and 1,286 proteins were identified in fresh, equilibrated, and cryopreserved spermatozoa, respectively. When the proteome of fresh spermatozoa was compared with equilibrated spermatozoa, we found that 166 proteins were differentially expressed. When equilibrated spermatozoa were compared with cryopreserved spermatozoa, we found that 147 proteins were differentially expressed between them. Similarly, we found that 156 proteins were differentially expressed between fresh and cryopreserved spermatozoa. Among these proteins, the abundance of 105 proteins was lowered during the equilibration process itself, while the abundance of 43 proteins was lowered during ultralow temperature preservation. Remarkably, the equilibration process lowered the abundance of sperm proteins involved in energy metabolism, structural integrity, and DNA repair and increased the abundance of proteins associated with proteolysis and protein degradation. The abundance of sperm proteins associated with metabolism, cGMP-PKG (cyclic guanosine 3′,5′-monophosphate-dependent protein kinase G) signaling, and regulation of the actin cytoskeleton was also altered during the equilibration process. Collectively, the present study showed that the equilibration step in the bull sperm cryopreservation process was the critical point for sperm proteome, during which a majority of proteomic alterations in sperm occurred. These findings are valuable for developing efficient protocols to minimize protein damage and to improve the quality and fertility of cryopreserved bull spermatozoa.

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Proteases and Proteases Inhibitors of Semen - A Review

Cited by 7 publications

References 84 publications

Sperm protein markers for Holstein bull fertility at National Artificial Insemination Centers in Indonesia

Sperm protein markers for Holstein bull fertility at National Artificial Insemination Centers in Indonesia

The seminal acrosin‐inhibitor ClTI1/SPINK2 is a fertility‐associated marker in the chicken

The cryopreservation process induces alterations in proteins associated with bull sperm quality: The equilibration process could be a probable critical control point

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