scholarly journals Specific Seminal Plasma Fractions Are Responsible for the Modulation of Sperm–PMN Binding in the Donkey

Animals ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 1388
Author(s):  
Jordi Miró ◽  
Jaime Catalán ◽  
Henar Marín ◽  
Iván Yánez-Ortiz ◽  
Marc Yeste
Keyword(s):  
Molecular Weight ◽  
Sperm Motility ◽  
Seminal Plasma ◽  
Potential Effect ◽  
Polymorphonuclear Neutrophils ◽  
Low Fertility ◽  
Plasma Fractions ◽  
Complex Fluid ◽  
First Time

While artificial insemination (AI) with frozen-thawed sperm results in low fertility rates in donkeys, the addition of seminal plasma, removed during cryopreservation, partially counteracts that reduction. Related to this, an apparent inflammatory reaction in jennies is induced following AI with frozen-thawed sperm, as a high amount of polymorphonuclear neutrophils (PMN) are observed within the donkey uterus six hours after AI. While PMN appear to select the sperm that ultimately reach the oviduct, two mechanisms, phagocytosis and NETosis, have been purported to be involved in that clearance. Remarkably, sperm interacts with PMN, but the presence of seminal plasma reduces that binding. As seminal plasma is a complex fluid made up of different molecules, including proteins, this study aimed to evaluate how different seminal plasma fractions, separated by molecular weight (<3, 3–10, 10–30, 30–50, 50–100, and >100 kDa), affect sperm–PMN binding. Sperm motility, viability, and sperm–PMN binding were evaluated after 0 h, 1 h, 2 h, 3 h, and 4 h of co-incubation at 38 °C. Two seminal plasma fractions, including 30–50 kDa or 50–100 kDa proteins, showed the highest sperm motility and viability. As viability of sperm not bound to PMN after 3 h of incubation was the highest in the presence of 30–50 and 50–100 kDa proteins, we suggest that both fractions are involved in the control of the jenny’s post-breeding inflammatory response. In conclusion, this study has shown for the first time that specific fractions rather than the entire seminal plasma modulate sperm–PMN binding within the donkey uterus. As several proteins suggested to be involved in the control of post-AI endometritis have a molecular weight between 30 and 100 kDa, further studies aimed at determining the identity of these molecules and evaluating their potential effect in vivo are much warranted.

scholarly journals Gelatinases in Boar Seminal Plasma and Their Relation to Semen Indicators

2010 ◽  
Vol 79 (3) ◽  
pp. 491-496 ◽  
Author(s):  
Maja Zakošek Pipan ◽  
Marjan Kosec ◽  
Janko Mrkun ◽  
Petra Zrimšek
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Seminal Plasma ◽  
Animal Species ◽  
Sperm Concentration ◽  
Gelatin Zymography ◽  
Motile Sperm ◽  
Molecular Weights ◽  
Simultaneous Identification ◽  
First Time

Matrix metalloproteinases were detected in reproductive tissues and seminal plasma of various animal species. The aim of this study was to determine for the first time the presence of gelatinases and metalloproteases in boar seminal plasma and to correlate the results with semen indicators. Gelatin zymography was used for simultaneous identification and measurement of gelatinase enzyme activity associated with their molecular weights. Several gelatinase forms were identified in seminal plasma of boars. Those that were stimulated by CaCl2 and inhibited by EDTA and phenanthroline were considered as metalloproteases. Negative correlation between semen indicators (sperm index, sperm concentration and concentration of progressive motile sperm) and the concentrations of metalloprotease at 78 kDa and 66 kDa means that higher values of semen indicators correlate with lower concentrations of these metaloproteases in seminal plasma. Gelatinases with molecular weight of 225, 78 and 66 kDa correlated with higher levels of acrosome damage. Samples with sperm index above 110 M/ml contained gelatinases of significantly lower band intensities at 78 and 66 kDa compared to samples with SI less than 110 M/ml. Bands with 225, 78 and 66 kDa are suggested to belong to a dimer of MMP-9, proMMP-2 and mature MMP-2.

scholarly journals Studies on Liquefaction Time and Proteins Involved in the Improvement of Seminal Characteristics in Dromedary Camels (Camelus dromedarius)

Scientifica ◽  
2016 ◽  
Vol 2016 ◽  
pp. 1-6 ◽  
Author(s):  
Gorakh Mal ◽  
Sumant Vyas ◽  
Alagiri Srinivasan ◽  
Nitin Vasant Rao Patil ◽  
Krishan Murari Lal Pathak
Keyword(s):  
Growth Factors ◽  
Sperm Motility ◽  
Seminal Plasma ◽  
Dromedary Camel ◽  
Rheological Characteristics ◽  
Dromedary Camels ◽  
Nerve Growth Factors ◽  
Molecular Masses ◽  
First Time ◽  
Artificial Vagina

Semen was collected from six dromedary camels using artificial vagina during rutting season. Liquefaction of the viscous semen occurred in23.89±1.49 h. During liquefaction, proteins with molecular masses of 24.55 kDa and 22.07 kDa appeared in conjunction with the disappearance of intact 26.00 kDa protein after 18–24 h. These proteins were identified asβ-nerve growth factors (β-NGFs) in liquefied camel semen. Guanidine-HCL improves the rheological characteristics of dromedary camel semen along with significant (P<0.01) increase in sperm motility. No significant differences were found in viability of spermatozoa indicating no visible detrimental effects on spermatozoa. The cause of semen viscosity, as well as proteins that are present in liquefied dromedary camel seminal plasma, is described for the first time.

scholarly journals Measurement of Oxidative Stress Index in Seminal Plasma Can Predict In Vivo Fertility of Liquid-Stored Porcine Artificial Insemination Semen Doses

Antioxidants ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1203
Author(s):  
Isabel Barranco ◽  
Camila P. Rubio ◽  
Asta Tvarijonaviciute ◽  
Heriberto Rodriguez-Martinez ◽  
Jordi Roca
Keyword(s):  
Oxidative Stress ◽  
Litter Size ◽  
Sperm Motility ◽  
Seminal Plasma ◽  
Artificial Insemination ◽  
Stress Index ◽  
Trolox Equivalent Antioxidant Capacity ◽  
Oxidative Stress Index ◽  
Farrowing Rate

The study evaluated the relation between the oxidative stress index (OSI) in porcine seminal plasma (n = 76) with sperm resilience and in vivo fertility (farrowing rate and litter size of 3137 inseminated sows) of liquid-stored artificial insemination (AI) semen doses. The OSI was assessed as the ratio of advanced oxidation protein products to Trolox-equivalent antioxidant capacity, both measured using an automated analyzer. Sperm motility (computer-assisted sperm analyzer) and viability (flow cytometry) were evaluated in semen AI-doses at 0 and 72 h of storage at 17 °C. Sperm resilience was defined as the difference between storage intervals. Semen AI-doses were hierarchically clustered as having high, medium and low seminal OSI (p < 0.001) with those of low displaying higher resilience (p < 0.01). Boars were hierarchically clustered into two groups (p < 0.001) as having either positive or negative farrowing rate and litter size deviation; the negative one showing higher seminal OSI (p < 0.05). In sum, seminal OSI was negatively related to sperm motility and the in vivo fertility of liquid-stored boar semen AI-doses, with the receiver operating characteristic curve presenting seminal OSI as a good predictive biomarker of in vivo fertility of AI-boars (area under the curve: 0.815, p < 0.05).

scholarly journals Decreased Sperm Motility is Associated with Increased Seminal Plasma IGF-I, IGF-II, IGFBP-2 and PSA Levels in Male Infertility

2021 ◽  
Author(s):  
Li Fu ◽  
Kevin Yuen ◽  
Aye Nyein Tint ◽  
Andrew R. Hoffman ◽  
Ariff T. Bongso ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Seminal Plasma ◽  
Sperm Count ◽  
Infertile Men ◽  
Igf Receptors ◽  
Sperm Counts ◽  
Aging Men ◽  
Igf I ◽  
Igfbp 3

Abstract PurposePrevious studies have suggested the involvement of serum IGFs and IGFBPs in the regulation of the female reproductive system. Little is known of these peptides in the seminal plasma (SP) of men and their potential effects on fertility. We assessed SP levels of these peptides in infertile men with low sperm motility (asthenozoospermic; AZ) and low sperm counts (oligozoospermic; OZ), its effects on in vivo sperm motility, and whether aging affects these peptides.MethodsTwenty eight infertile men (AZ; n = 18 and OZ; n = 10) and 20 fertile normozoospermic (NZ) men were studied. Seminal plasma IGF-I, IGF-II, IGFBP-2, IGFBP-3 and PSA levels were measured, and spermatozoa mRNA transcript patterns were examined.ResultsAsthenozoospermic men had higher SP IGF-I, IGF-II, IGFBP-2 and PSA levels than NZ and OZ men (all P < 0.05), whereas SP IGFBP-3 levels were no different between the three groups. Sperm count positively correlated with SP IGF-I, IGF-II and IGFBP-2; sperm motility negatively correlated with SP IGF-II and IGFBP-2; and age correlated positively with SP IGF-II (all P < 0.04). The expression of IGF-I and IGF-II mRNA and mRNA receptors was detectable, but no variations in transcript levels were noted. ConclusionDecreased sperm motility, but not sperm count, in infertile AZ men is associated with increased SP IGF-I, IGF-II, IGFBP-2 and PSA levels. Changes in SP IGFs and their interactions with IGFBPs and IGF receptors, and PSA levels suggest a role of these SP peptides in modulating sperm motility and possibly prostate disease development in aging men.

Low molecular weight components in bovine semen diffusate and their effects on motility of bull sperm

1994 ◽  
Vol 6 (2) ◽  
pp. 165 ◽  
Author(s):  
N al-Somai ◽  
R Vishwanath ◽  
P Shannon ◽  
PC Molan
Keyword(s):  
Molecular Weight ◽  
Sperm Motility ◽  
Seminal Plasma ◽  
Detrimental Effect ◽  
Gel Permeation Chromatography ◽  
Low Molecular Weight ◽  
Small Molecular Weight ◽  
Bovine Semen ◽  
Molecular Weights ◽  
Sperm Survival

Dialysis of diluted semen before cryopreservation is beneficial to sperm survival. This is due to removal of low molecular weight components from seminal plasma that are damaging to sperm. The apparent molecular weights (M(r)) of these components range between 1000 and 12,000 as estimated by gel permeation chromatography and electrophoresis. The detrimental effect on sperm motility is greatest with the components of M(r) between 5000 and 12,000 and with those of M(r) < 1500. Their effect on sperm motility was dependent on concentration. The small molecular weight components were derived from the high molecular weight components of seminal plasma through disaggregation under prescribed conditions.

scholarly journals Seminal Plasma, Sperm Concentration, and Sperm-PMN Interaction in the Donkey: An In Vitro Model to Study Endometrial Inflammation at Post-Insemination

2020 ◽  
Vol 21 (10) ◽  
pp. 3478 ◽  
Author(s):  
Jordi Miró ◽  
Henar Marín ◽  
Jaime Catalán ◽  
Marion Papas ◽  
Sabrina Gacem ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Artificial Insemination ◽  
In Vitro Model ◽  
Sperm Concentration ◽  
Polymorphonuclear Neutrophils ◽  
Low Fertility ◽  
Fertility Rates ◽  
Vitro Model ◽  
Instrumental Role

In the donkey, artificial insemination (AI) with frozen-thawed semen is associated with low fertility rates, which could be partially augmented through adding seminal plasma (SP) and increasing sperm concentration. On the other hand, post-AI endometrial inflammation in the jenny is significantly higher than in the mare. While previous studies analyzed this response through recovering Polymorphonuclear Neutrophils (PMN) from uterine washings, successive lavages can detrimentally impact the endometrium, leading to fertility issues. For this reason, the first set of experiments in this work intended to set an in vitro model through harvesting PMN from the peripheral blood of jennies. Thereafter, how PMN, which require a triggering agent like formyl-methionyl-leucyl-phenylalanine (FMLP) to be activated, are affected by donkey semen was interrogated. Finally, we tested how four concentrations of spermatozoa (100 × 106, 200 × 106, 500 × 106 and 1000 × 106 spermatozoa/mL) affected their interaction with PMN. We observed that semen, which consists of sperm and SP, is able to activate PMN. Whereas there was a reduced percentage of spermatozoa phagocytosed by PMN, most remained attached on the PMN surface or into a surrounding halo. Spermatozoa not attached to PMN were viable, and most of those bound to PMN were also viable and showed high tail beating. Finally, only sperm concentrations higher than 500 × 106 spermatozoa/mL showed free sperm cells after 3 h of incubation, and percentages of spermatozoa not attached to PMN were higher at 3 h than at 1 h, exhibiting high motility. We can thus conclude that semen activates PMN in the donkey, and that the percentage of spermatozoa phagocytosed by PMN is low. Furthermore, because percentages of spermatozoa not attached to PMN were higher after 3 h than after 1 h of incubation, we suggest that PMN-sperm interaction plays an instrumental role in the reproductive strategy of the donkey.

scholarly journals Oxidation of polymines by diamine oxidase from human seminal plasma

1975 ◽  
Vol 145 (2) ◽  
pp. 373-378 ◽  
Author(s):  
E Hölttä ◽  
P Pulkkinen ◽  
K Elfving ◽  
J Jänne
Keyword(s):  
Molecular Weight ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Diamine Oxidase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Human Semen ◽  
Human Seminal Plasma ◽  
Ph Values

1. Diamine oxidase [amine-oxygen oxidoreductase (deaminating)(pyridoxal-containing), EC 1.4.3.6] was purified from human seminal plasma more than 1,700-fold. The enzyme appeared to be homogeneous on polyacrylamide-gel electrophoresis at two different pH values. 2. The general properties of the enzyme were comparable with those described for other diamine oxidases from different mammalian sources. The molecular weight of the enzyme was calculated to be about 182,000. 3. The enzyme had highest affinity for diamines, but polyamines spermidine and spermine were also degraded at concentrations that can be considered physiological in human semen. 3. The possible degradation of spermine by diamine oxidase in human semen in vivo may give rise to the formation of cytotoxic aldehydes that conceivably can influence the motility and survival of the spermatozoa.

Effects of Unfractionated and Low Molecular Weight Heparins on Platelet Thromboxane Biosynthesis “In Vivo”

1994 ◽  
Vol 72 (06) ◽  
pp. 942-946 ◽  
Author(s):  
Raffaele Landolfi ◽  
Erica De Candia ◽  
Bianca Rocca ◽  
Giovanni Ciabattoni ◽  
Armando Antinori ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Unfractionated Heparin ◽  
Low Molecular Weight Heparin ◽  
Primary Source ◽  
In Vivo Studies ◽  
Low Molecular Weight ◽  
Heparin Administration ◽  
To Receive

SummarySeveral “in vitro” and “in vivo” studies indicate that heparin administration may affect platelet function. In this study we investigated the effects of prophylactic heparin on thromboxane (Tx)A2 biosynthesis “in vivo”, as assessed by the urinary excretion of major enzymatic metabolites 11-dehydro-TxB2 and 2,3-dinor-TxB2. Twenty-four patients who were candidates for cholecystectomy because of uncomplicated lithiasis were randomly assigned to receive placebo, unfractionated heparin, low molecular weight heparin or unfractionaed heparin plus 100 mg aspirin. Measurements of daily excretion of Tx metabolites were performed before and during the treatment. In the groups assigned to placebo and to low molecular weight heparin there was no statistically significant modification of Tx metabolite excretion while patients receiving unfractionated heparin had a significant increase of both metabolites (11-dehydro-TxB2: 3844 ± 1388 vs 2092 ±777, p <0.05; 2,3-dinor-TxB2: 2737 ± 808 vs 1535 ± 771 pg/mg creatinine, p <0.05). In patients randomized to receive low-dose aspirin plus unfractionated heparin the excretion of the two metabolites was largely suppressed thus suggesting that platelets are the primary source of enhanced thromboxane biosynthesis associated with heparin administration. These data indicate that unfractionated heparin causes platelet activation “in vivo” and suggest that the use of low molecular weight heparin may avoid this complication.

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