Seminal hyperviscosity is not associated with semenogelin degradation or sperm deoxyribonucleic acid damage: a prospective study of infertile couples

Esfandiari, Navid; Lamirande, Eve de; Gukturk, Asli; Gabriel, Maria C. San; Nazemian, Zohreh; Burjaq, Hasan; Casper, Robert F.; Zini, Armand

doi:10.1016/j.fertnstert.2014.02.045

Cited by 3 publications

(3 citation statements)

References 28 publications

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“…SEMG 1 has been found in complex with both the glycosylphosphatidylinositol (GPI)-anchored and soluble CD52, and it has been hypothesized that GPI-anchored CD52 serves as a dock for SEMG1 in anchoring the sperm cells to form clots 65 , later degraded by PSA to enable sperm motility. Recent studies found a negative correlation between sperm motility and the proportion of SEMGs bound spermatozoa 66,67 . These findings suggest that unbound sperm may be a relevant parameter for in vivo fertilization 68 .…”

Section: Discussionmentioning

confidence: 98%

Surface protein profiling of prostate-derived extracellular vesicles by mass spectrometry and proximity assays

et al. 2022

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Extracellular vesicles (EVs) are mediators of intercellular communication and a promising class of biomarkers. Surface proteins of EVs play decisive roles in establishing a connection with recipient cells, and they are putative targets for diagnostic assays. Analysis of the surface proteins can thus both illuminate the biological functions of EVs and help identify potential biomarkers. We developed a strategy combining high-resolution mass spectrometry (HRMS) and proximity ligation assays (PLA) to first identify and then validate surface proteins discovered on EVs. We applied our workflow to investigate surface proteins of small EVs found in seminal fluid (SF-sEV). We identified 1,014 surface proteins and verified the presence of a subset of these on the surface of SF-sEVs. Our work demonstrates a general strategy for deep analysis of EVs’ surface proteins across patients and pathological conditions, proceeding from unbiased screening by HRMS to ultra-sensitive targeted analyses via PLA.

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Section: Discussionmentioning

confidence: 98%

Surface protein profiling of prostate-derived extracellular vesicles by mass spectrometry and proximity assays

et al. 2022

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“…Such a tendency was not observed in any of the other parameters, including the proportion of SEMG+. Although the precise molecular mechanism underlying the controlling fertilizing capacity of sperm in vivo have not been revealed, the role of SEMGs on sperm were well studied and proved to control motility and capacitation [ 8 , 16 – 18 ]. Moreover, according to our analysis in knockout mice, seminal vesicle secretion 2 (SVS2), an orthologue of SEMGs, is essential for in vivo fertilization [ 13 ].…”

Section: Discussionmentioning

confidence: 99%

“…During liquefaction, SEMGs are degraded into low molecular mass proteins by a prostate-specific antigen (PSA), and sperms start to move [ 7 ]. However, it was shown that seminal hyperviscosity had no relation to the degree of SEMG degradation [ 8 ], thereby indicating that SEMGs do not inhibit sperm motility through seminal viscosity. One of the fragments of the degraded SEMGs, a seminal plasma motility inhibitor (SPMI), inhibits the motility of both demembranated spermatozoa and intact spermatozoa.…”

Section: Introductionmentioning

confidence: 99%

Relationship between Semenogelins bound to human sperm and other semen parameters and pregnancy outcomes

Yamasaki

Yoshida

Yoshiike

et al. 2017

Basic Clin. Androl.

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BackgroundSemenogelins (SEMGs) are major components of human seminal vesicle secretions. Due to SEMG’s sperm-motility inhibitor, a significant negative correlation between sperm motility and the proportion of SEMG-bound spermatozoa (SEMG+) was found in asthenozoospermic patients. SEMGs also show intrinsic inhibitory capability for sperm capacitation; however, studies on actual clinical specimens have not been conducted.MethodsTo reveal the relationship between SEMGs and the fertilizing capacity of sperm from male infertile patients who are not restricted to asthenozoospermia, we measured the proportion of SEMG+ in the spermatozoa of 142 male infertile patients. The pregnancy outcomes in partners of these patients were retrospectively analyzed using questionnaires.ResultsAmong examined semen parameters, only the total SEMG-unbound sperm count showed a tendency to be different between the spontaneous pregnancy or intra-uterine-insemination-pregnancy groups and in-vitro-fertilization- or intracytoplasmic-sperm-injection-pregnancy groups. It was elevated in the former group, which includes patients who used in vivo fertilization.ConclusionsThe total SEMG-unbound sperm count would be a relevant parameter for in vivo fertilization. This result suggests that SEMGs inhibit ectopic capacitation before sperm reach the fertilization site and that the number of total SEMG-unbound sperm is a parameter directly linked to the possibility of in vivo fertilization.Electronic supplementary materialThe online version of this article (doi:10.1186/s12610-017-0059-6) contains supplementary material, which is available to authorized users.

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Treatment of semen samples with α‐chymotrypsin alters the expression pattern of sperm functional proteins—a pilot study

et al. 2018

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Semen hyperviscosity delays the liquefaction of semen sample and is subjected to limited proteolysis by addition of α-chymotrypsin to reduce the viscosity. α-Chymotrypsin is a proteolytic enzyme involved in degradation of the proteins and polypeptides. Even though α-chymotrypsin improves the handling of hyperviscous samples, its effect on the sperm proteins is not clear. This study was aimed to evaluate the alteration in the expression of sperm functional proteins in samples treated with α-chymotrypsin. Among all the proteins examined in both donor and patient samples, HSPA2 (70 KDa), BAG6 (150 KDa), HIST1H2BA (14 KDa), SPA17 (17 KDa formed after cleavage of C-terminal calmodulin-binding domain), and OXPHOS complexes were undetectable in α-chymotrypsin-treated samples, while the expression of the native SPA17 (20 KDa) was significantly decreased in the α-chymotrypsin-treated samples in comparison with controls. The use of α-chymotrypsin for liquefaction of hyperviscous samples degrades functional proteins of spermatozoa. Intracellular proteins, such as OXPHOS complexes and HIST1H2BA, and sperm surface proteins (HSPA2, BAG6, and SPA17) were degraded in all treated samples. Whether treatment of samples with α-chymotrypsin affects the global proteomic outcome is unclear. More in-depth calibration studies are required to determine the appropriate concentration of α-chymotrypsin for processing hyperviscous semen samples without compromising its protein expression and function. Similarly, the effects of altered protein function on assisted reproductive techniques (ART), such as intrauterine insemination (IUI) and in vitro fertilization (IVF) outcome, are not known and require further research.

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Seminal hyperviscosity is not associated with semenogelin degradation or sperm deoxyribonucleic acid damage: a prospective study of infertile couples

Cited by 3 publications

References 28 publications

Surface protein profiling of prostate-derived extracellular vesicles by mass spectrometry and proximity assays

Surface protein profiling of prostate-derived extracellular vesicles by mass spectrometry and proximity assays

Relationship between Semenogelins bound to human sperm and other semen parameters and pregnancy outcomes

Treatment of semen samples with α‐chymotrypsin alters the expression pattern of sperm functional proteins—a pilot study

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