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Seminal Plasma (seminal + plasma)
Kinds of Seminal Plasma Terms modified by Seminal Plasma Selected AbstractsAutologous Whole Ram Seminal Plasma and its Vesicle-free Fraction Improve Motility Characteristics and Membrane Status but not In Vivo Fertility of Frozen,Thawed Ram SpermatozoaREPRODUCTION IN DOMESTIC ANIMALS, Issue 5 2007R El-Hajj Ghaoui Contents Motility characteristics (assessed subjectively and with computer-assisted semen analysis) and membrane status (after staining with chlortetracycline) of washed and non-washed frozen,thawed ram spermatozoa were evaluated after incubation in buffer and buffer containing autologous whole seminal plasma or one of its two fractions: the pellet of membrane vesicles obtained by ultracentrifugation (and used at three times normal protein concentration) or the vesicle-free supernatant fraction. Whole seminal plasma and supernatant, but not membrane vesicles, improved the motility characteristics of spermatozoa after 3 and 6 h of post-thaw incubation compared with the control buffer. Resuspension and incubation with whole seminal plasma, supernatant or membrane vesicles lowered the proportion of acrosome-reacted frozen,thawed spermatozoa compared with the control buffer. Unwashed frozen,thawed semen from three rams, incubated with autologous whole seminal plasma or its fractions and inseminated using cervical or intrauterine artificial insemination, had no effect on pregnancy rates of ewes in synchronized oestrus. However, fertility was higher after laparoscopic than cervical insemination (44.9 vs 12.3%, p < 0.001). In conclusion, resuspension and incubation of frozen,thawed ram spermatozoa in autologous whole seminal plasma or its vesicle-free supernatant fraction improved their motility characteristics and, with membrane vesicles, membrane status, but these benefits were not reflected in improved fertility after cervical or intrauterine insemination. [source] Effect of Insemination,Ovulation Interval and Addition of Seminal Plasma on Sow Fertility to Insemination of Cryopreserved SpermREPRODUCTION IN DOMESTIC ANIMALS, Issue 4 2007M Abad Contents In swine, the use of frozen-thawed (FT) sperm for artificial insemination (AI) is limited because of poor sow fertility, possibly associated with a post-thaw capacitation-like status resulting in fewer fully viable sperm. Sow fertility to AI with FT sperm may improve with deeper deposition of sperm within the female tract, insemination very close to ovulation, or reversal of cryocapacitation by seminal plasma (SP). We performed two experiments to examine these suggestions. In experiment 1, 122 multiparous Yorkshire sows received 600 IU equine chorionic gonadotrophin at weaning and 5 mg pLH 80 h later to control time of ovulation. The predicted time of ovulation (PTO) was 38 h after pLH injection. Thereafter, sows were assigned on the basis of parity to a single AI of FT sperm at 2 h before PTO, or at 12 h before PTO, or FT sperm supplemented with 10% SP at 12 h before PTO. Control sows received fresh semen at 12 h before PTO. All semen doses were adjusted to 3 × 109 live cells and deposited into the cervix. Experiment 2 employed 99 multiparous crossbred sows and repeated the treatments of experiment 1 except that all FT inseminations were intrauterine. In both experiments, farrowing rates were lower (p < 0.01) following FT inseminations with no effect of time of insemination or of supplemental SP. In experiment 1, litter size was smaller following FT insemination (p < 0.05), but no effect on litter size was evident in experiment 2. Supplemental SP had no effect on litter size in either experiment. The lack of effect of either SP or timing of FT insemination on sow fertility suggests that the non-lethal sperm cryoinjury affecting fertility involves more than just cryocapacitation. [source] The Origin of Membrane Vesicles in Ram Seminal PlasmaREPRODUCTION IN DOMESTIC ANIMALS, Issue 2 2006R El-Hajj Ghaoui Contents The hypothesis tested in this study was that the membrane vesicles present in ram seminal plasma are of testicular origin, rather than being secreted by the accessory sex glands as has been previously reported for a number of species. Membrane vesicles were present in cellular extracts from reproductive organs and accessory sex glands of six rams, and in the seminal plasma of a further eight rams. When four of the latter rams were subjected to vasectomy, to isolate ejaculate contents to only the secretions of the accessory sex glands, the vesicles were largely eliminated from their ejaculates, while vesicles were still present in the ejaculates of the four control rams. The constituents of the cytoplasmic droplets and membrane vesicles derived from the seminal plasma were compared by transmission electron microscopy (TEM). Vesicles present in the cytoplasmic droplets were similar in morphology but smaller on average than those in the seminal plasma. It was concluded that the membrane vesicles in ram seminal plasma originate from either the cytoplasmic droplets, or a combination of vesicles from the droplets and the epididymis. [source] Increased IL-18 Levels in Seminal Plasma of Infertile Men with Genital Tract InfectionsAMERICAN JOURNAL OF REPRODUCTIVE IMMUNOLOGY, Issue 6 2006Ioannis M. Matalliotakis Problem Interleukin (IL)-18 is a novel cytokine, previously known as interferon (IFN)- , inducing factor. We evaluated the levels of IL-18 and IFN- , in seminal plasma (SP) of fertile and infertile men. Method of study Semen samples were obtained by masturbation from 80 men, and were examined for the levels of IL-18 and IFN- , by enzyme-linked immunosorbent assay. Seven groups were included: (i) fertile men (n = 18), (i) infertile men with genital tract infections (n = 17), (iii) with varicocele (n = 15), (iv) with Klinefelter syndrome (n = 6), (v) with cryptorchidism (n = 7), (vi) with mumps orchitis (n = 7), and (vii) with idiopathic testicular lesions (n = 10). Results Mean levels of IL-18 were higher in SP from infertile men with genital tract infections compared with SP from other groups except Klinefelter syndrome (P < 0.05). However, no significant differences could be detected for IFN- ,. A significant positive correlations was found between IL-18 and IFN- , in total patient population (P < 0.001). Moreover, a negative correlation was observed between IL-18 and sperm concentrations, and motility (P < 0.01 and <0.03, respectively). Furthermore, there was a positive and statistically significant association between IL-18 and IFN- , levels in SP of infertile men with genital tract infections (P < 0.0001). However, there was no relationship between IL-18 and IFN- ,, and semen parameters in the same group. Conclusion SP IL-18 levels were increased in men with urogenital infections. Thus, the elevated expression of IL-18 in SP may be used as a diagnostic marker in the male genital tract infections. [source] ,1 -antitrypsin prevents polymorphonuclear leucocyte-elastase effects on spermatozoa qualityINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 1 2010J. Leßig Summary Elevated levels of polymorphonuclear leucocyte (PMN)-derived elastase, which is suggested as marker for inflammations in the male genital tract, correlate well with spermatozoa deterioration. PMN elastase caused a time- and concentration-dependent (up to a elastase concentration of 0.5 ,g/mL) externalization of phosphatidylserine and intercalation of propidium iodide on human spermatozoa. There are apparently a limited number of target sites for elastase on spermatozoa surface, because the further enhancement of elastase amount did not fasten alterations in spermatozoa parameters. Analysis of flow cytometry data revealed that most spermatozoa were in a necrotic state after an exposure with elastase for 22 h. Some apoptotic cells were only detected at shorter incubation periods. Seminal plasma prevented in a concentration-dependent manner the PMN elastase-mediated loss of vitality of spermatozoa. We detected by blotting techniques large amounts of ,1 -antitrypsin in seminal plasma. This antiproteinase is known to inactivate elastase at inflammatory sites. Increasing concentrations of ,1 -antitrypsin prevented gradually spermatozoa deterioration induced by elastase. Thus, ,1 -antitrypsin contributes to an efficient protease/antiproteinase balance in seminal plasma. A disturbed balance will promote the development of chronic inflammations which can also be the reason for male infertility problems. [source] Heme oxygenase enzyme activity in seminal plasma of oligoasthenoteratozoospermic males with varicoceleANDROLOGIA, Issue 4 2010M. T. Abdel Aziz Summary This work aimed to assess seminal plasma heme oxygenase (HO) enzyme activity in oligoasthenoteratozoospermia (OAT) males with varicocele. Ninety-three men were divided according to their sperm count and clinical examination into: healthy fertile controls (n = 34), OAT without varicocele (n = 37) and OAT associated with varicocele (n = 22). They were subjected to semen analysis and estimation of seminal plasma HO enzyme activity in the form of bilirubin concentration. Seminal plasma HO enzyme activity decreased significantly in OAT cases compared with controls. Seminal plasma HO in OAT cases associated with varicocele decreased significantly compared with OAT cases without varicocele and healthy controls (mean ± SD; 109.2 ± 29.5, 283.6 ± 88.4, 669.5 ± 236.1 nMol bilirubin/mg ptn/min, P < 0.001). There was positive correlation between seminal plasma HO enzyme activity and sperm concentration, per cent of motile spermatozoa, number of motile spermatozoas ml,1 and significant negative correlation with sperm abnormal forms per cent. It is concluded that varicocele has a negative impact on seminal HO enzyme activity. Therefore, improved seminal picture after correcting varicocele repair might be related, in part, to improved HO action(s). [source] Acrosome reaction in Chlamydia-positive and negative patientsANDROLOGIA, Issue 5 2003A. Jungwirth Summary. Chlamydia trachomatis infections might have a detrimental effect on various sperm functions. Data concerning the effect of C. trachomatis on the capacitation activity of sperms are lacking. The study was undertaken to evaluate whether chlamydial infection influences acromsome reaction (AR). Three groups of men were investigated for ARs - Chlamydia negative (n = 46) and positive (n = 30) patients, and healthy men (n = 53) undergoing vasectomy. The fluorescence technique for the evaluation of AR was applied. The normal range for the induction of AR was assumed ,AR > 12.5% for this technique. Seminal plasma was examined for IgA antibodies against C. trachomatis. There was a significant difference in AR between healthy volunteers, Chlamydia-negative and Chlamydia- positive patients. ,ARs were 15.8 ± 1.6% in healthy volunteers versus 12.15 ± 2.4% in Chlamydia- negative and 9.08 ± 1.8% in Chlamydia- positive patients, respectively (P <0.05). Significant elevated titres of C. trachomatis- specific IgA in seminal plasma showed a negative correlation with the AR of spermatozoa. AR seems to be a valuable marker, especially in couples with idiopathic infertility. [source] Effect of norethisterone and its A-ring reduced metabolites on the acrosome reaction in porcine spermatozoaANDROLOGIA, Issue 5 2002G. Martinez Summary. The synthetic progestin, norethisterone (NET), has been reported as a contragestational postcoital agent in humans, rodents and rabbits. The effect and molecular mechanisms of NET and its A-ring reduced metabolites, 5,-NET and 3,5,-NET, on the acrosome reaction (AR) are unknown. The aim of this study was to assess the effect of these compounds on an in vitro progesterone-induced AR in porcine spermatozoa. The spermatozoa were obtained from semen ejaculated by proven fertile adult pigs. Seminal plasma removed and incubated under capacitating conditions was performed in TALP-Hepes medium for 4 h. Progesterone (P4) and three different progestins: norethisterone (NET), 5,-norethisterone (5,-NET) and 3,5,-NET were then added at equimolar doses, and the spermatozoa were incubated for 15 min. Double-staining with PSA-FITC and Hoechst-33258 assessed the AR and sperm viability. Both P4 and NET induced the AR, while 5,-NET not only did not induce this process, but was able to block the effect of P4 on the spermatozoa. 3,5,-NET was not able to inhibit P4 action. These results suggest that NET and its A-ring reduced metabolites act in different ways on the progesterone-induced AR in porcine spermatozoa. [source] Leptin exists in tubuli seminiferi and in seminal plasmaANDROLOGIA, Issue 4 2002H.-J. Glander Summary. Leptin is a 167-amino acid protein that stimulates gonadotrophin-releasing hormone secretion and exerts indirect effects on the gonads via neuropeptide Y, NPY. Recent research has suggested that leptin may also have an effect on testosterone secretion. To investigate the role of leptin in reproduction, leptin in testicular tissue and seminal plasma was examined in relation to leptin in serum, semen sample qualities and vasectomy. Seminal plasma and serum of 64 infertility patients, and 15 individuals after vasectomy, were assayed for leptin using a competitive ,in house' radioimmunoassay. The concentration of leptin in seminal plasma was significantly lower in the ,normal' semen sample group than in the ,pathological' group (Mean ± SEM; 1.45 ± 0.18 vs. 3.19 ± 0.57 ng ml,1; P <,0.05), and showed a significantly negative correlation with percentage of motile spermatozoa (r=,0.46; P=0.0005) and with the velocity straight line, VSL, (r=,0.30; P= 0.029). In contrast, leptin concentration in serum did not show any relationship with the spermiogram parameters. In testicular tissue, leptin was preferentially found within the tubuli seminiferi using anti-leptin polyclonal antibody, Ob A-20 Sc 842. The amount of leptin per ejaculate did not significantly change after vasectomy, and was not correlated to fructose, zinc or neutral alpha glucosidase in seminal plasma (P > 0.05). These results suggest that the amount of leptin in the genital tract, including the tubuli seminiferi, may influence the mechanisms involved in the motility development of spermatozoa. [source] ,-Microseminoprotein-related molecules may participate in formation of the mesoderm in the chick embryoDEVELOPMENT GROWTH & DIFFERENTIATION, Issue 4 2003Aditi Karandikar It has previously been shown that human ,-microseminoprotein enhances development of mesodermal structures in the chick embryo. The present study was carried out to elucidate the mechanism of action of human ,-microseminoprotein in the chick embryo. ,-Microseminoprotein brought about significant modulation of expression of Brachyury in gastrulating embryos. In approximately 50% of the treated embryos, Brachyury expression was enhanced around the Hensen's node. These cells not only expressed higher levels of Brachyury, but also appeared to switch off Brachyury expression prematurely, postinvagination. The spatial modulation of Brachyury is not clearly reflected in the northern blots, indicating that ,-microseminoprotein treatment results in redistribution of available transcripts or that the upregulation is compensated for by early switching off of Brachyury postinvagination. Because higher levels of Brachyury during gastrulation are believed to result in early exit of cells from the primitive streak, ,-microseminoprotein treatment appeared to have stimulated morphogenetic movements by upregulating Brachyury around the Hensen's node. This deduction was confirmed by scanning electron microscopic analysis that showed that altered morphogenetic movements accompany modulation of Brachyury. The specific responses elicited by ,-microseminoprotein indicate presence of a structurally related molecule in the chick. By western blotting, similar molecules were indeed detected in the chicken seminal plasma and in chick embryos. These data strongly suggest that ,-microseminoprotein-related molecule(s) participates in mesoderm formation in the chick embryo. [source] Mass spectrometry study of ecto-5,-nucleotidase from bull seminal plasmaFEBS JOURNAL, Issue 16 2000Carlo Fini The structure of ecto-5,-nucleotidase from bull seminal plasma, containing a glycosyl-phosphatidylinositol anchor, was studied using mass spectrometry. MALDI-MS analysis of intact protein indicated a mass of 65 568.2 Da for the monomeric form, and it also showed a heterogeneous population of glycoforms with the glycosidic moiety accounting for ,,6000 Da. MALDI-MS analysis showed that Asn53, Asn311, Asn333 and Asn403 were four sites of N -glycosylation. GC-MS analysis provided information on the glycosidic structures linked to the four asparagines. Asn53, Asn311 and Asn333 were linked to high-mannose saccharide chains, whereas the glycan chains linked to Asn403 contained a heterogeneous mixture of oligosaccharides, the high-mannose type structure being the most abundant and hybrid or complex type glycans being minor components. By combining enzymatic and/or chemical hydrolysis with GC-MS analysis, detailed characterization of the glycosyl-phpsphatidylinositol anchor was obtained. MALDI spectral analysis indicated that the glycosyl-phosphatidylinositol core contained EtN(P)Man3GlcNH2 -myo-inositol(P)-glycerol, principally modified by stearoyl and palmitoyl residues or by stearoyl and myristoyl residues to a minor extent. Moreover, 1-palmitoylglycerol and 1-stearoylglycerol outweighed 2-palmitoylglycerol and 2-stearoylglycerol. The combination of chemical and enzymatic digestions of the protein with the mass spectral analysis yielded a complete pattern of S,S bridges. The protein does not contain free thiols and its eight cysteines are linked by intramolecular disulfide bonds, the pairs being: Cys51,Cys57, Cys353,Cys358, Cys365,Cys387 and Cys476,Cys479. This work resolves details of the structure of ecto-5,-nucleotidase, with particular regard to the localization and composition of the glycidic moiety, number and localization of the disulfide bridges and characterization of the glycosyl-phosphatidylinositol anchor. [source] Amplification and overexpression of prosaposin in prostate cancerGENES, CHROMOSOMES AND CANCER, Issue 4 2005Shahriar Koochekpour We identified prosaposin (PSAP) as a secreted protein expressed in androgen-independent (AI) prostate cancer cells by cloning/sequencing, after probing a PC-3 cDNA library expressed in the ,TriplEx phagemid expression vector with a polyclonal rabbit antibody generated against pooled human seminal plasma. PSAP is a neurotrophic molecule; its deficiency or inactivation has proved to be lethal in man and mice, and in mice, it leads to abnormal development and atrophy of the prostate gland, despite normal testosterone levels. We used Southern hybridization, quantitative real-time polymerase chain reaction, and/or single nucleotide polymorphism (SNP) array analysis, and we now report the genomic amplification of PSAP in the metastatic AI prostate cancer cell lines, PC-3, DU-145, MDA-PCa 2b, M-12, and NCI-H660. In addition, by using SNP arrays and a set of 25 punch biopsy samples of human prostate cancer xenografts (LAPC3, LuCaP 23.1, 35, 49, 58, 73, 77, 81, 86.2, 92.1, 93, 96, 105, and 115), lymph nodes, and visceral-organ metastases, we detected amplification of the PSAP locus (10q22.1) in LuCaP 58 and 96 xenografts and two lymph node metastases. In addition, AI metastatic prostate cancer cell lines C4-2B and IA8-ARCaP over-expressed PSAP mRNA without evidence of genomic amplification. Taken together with prior data that demonstrated the growth-, migration-, and invasion-promoting activities, the activation of multiple signal transduction pathways, and the antiapoptotic effect of PSAP (or one of its active domains, saposin C) in prostate cancer cells, our current observation of PSAP amplification or overexpression in prostate cancer suggests, for the first time, a role for this molecule in the process of carcinogenesis or cancer progression in the prostate. © 2005 Wiley-Liss, Inc. [source] ,1 -antitrypsin prevents polymorphonuclear leucocyte-elastase effects on spermatozoa qualityINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 1 2010J. Leßig Summary Elevated levels of polymorphonuclear leucocyte (PMN)-derived elastase, which is suggested as marker for inflammations in the male genital tract, correlate well with spermatozoa deterioration. PMN elastase caused a time- and concentration-dependent (up to a elastase concentration of 0.5 ,g/mL) externalization of phosphatidylserine and intercalation of propidium iodide on human spermatozoa. There are apparently a limited number of target sites for elastase on spermatozoa surface, because the further enhancement of elastase amount did not fasten alterations in spermatozoa parameters. Analysis of flow cytometry data revealed that most spermatozoa were in a necrotic state after an exposure with elastase for 22 h. Some apoptotic cells were only detected at shorter incubation periods. Seminal plasma prevented in a concentration-dependent manner the PMN elastase-mediated loss of vitality of spermatozoa. We detected by blotting techniques large amounts of ,1 -antitrypsin in seminal plasma. This antiproteinase is known to inactivate elastase at inflammatory sites. Increasing concentrations of ,1 -antitrypsin prevented gradually spermatozoa deterioration induced by elastase. Thus, ,1 -antitrypsin contributes to an efficient protease/antiproteinase balance in seminal plasma. A disturbed balance will promote the development of chronic inflammations which can also be the reason for male infertility problems. [source] Effect of leptin on motility, capacitation and acrosome reaction of human spermatozoaINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 6 2009H. W. R. Li Summary Leptin is a polypeptide hormone with important roles in reproduction. It has been detected in human seminal plasma as well as on human ejaculated spermatozoa. This study aimed at studying the possible role of leptin in regulating human sperm functions. Immunofluorescent staining was used to study the expression of leptin and its receptor. The correlation between the concentration of leptin and soluble leptin receptor (ObRs) in seminal plasma as measured by enzyme-linked immunosorbant assay and sperm motility parameters measured by computer-assisted sperm analyais (CASA) was determined. The effects of recombinant leptin on human sperm motility, capacitation and acrosome reaction as measured by chlortetracycline staing were also studied. Leptin immunoreactivity was demonstrated at the equatorial and neck regions of human spermatozoa, whereas that of ObRs was shown up on the tail. After Percoll separation, spermatozoa with high density had more intense leptin immunoreactivity compared with those with low density. No significant correlation was found between seminal plasma concentration of leptin/ObRs and sperm motility parameters. After incubation with recombinant human leptin for either 3 h or overnight, there was no change in all the CASA motility parameters determined and percentages of capacitated and acrosome-reacted spermatozoa. We concluded that leptin does not have a significant effect on motility and capacitation/acrosome reaction in human ejaculated mature spermatozoa. Its role in male reproduction is yet to be determined. [source] Leptin and varicocele-related spermatogenesis dysfunction: animal experiment and clinical studyINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 5 2009Bin Chen Summary The objective of this study was to explore the relationships between varicocele-related spermatogenesis dysfunction and the expression of leptin and leptin receptors. In rats with experimental varicocele, the function of spermatogenesis, the expression of leptin and leptin receptors in testes were analysed; and in patients with varicocele-related male infertility, serum and seminal plasma levels of leptin, gonadal hormones and semen parameters were evaluated. In the testes of rats, leptin was expressed in seminiferous tubules and intersitium, leptin receptor was predominantly expressed in interstitium. The expression of leptin and its receptor in the testis of rats was not related to the weight of rat, but was inversely related to the weight of testis (r = ,0.408, p = 0.009 and r = ,0.433, p = 0.005, respectively), the Johnsen scores (r = ,0.916, p = 0.000 and r = ,0.863, p = 0.000, respectively), the seminiferous tubules diameter (r = ,0.853, p = 0.000 and r = ,0.870, p = 0.000, respectively) and the thickness of seminiferous epithelium (r = ,0.929, p = 0.000 and r = ,0.948, p = 0.000, respectively). In varicocele patients (N = 40), the sperm concentration and motility were significantly lower (p = 0.000) than those in the control group (N = 25), and the leptin level in seminal plasma was significantly higher (p = 0.000) than that in the control group. The leptin in serum and seminal plasma was positively related (r = 0.223, p = 0.002). The seminal plasma leptin level was inversely related to sperm concentration (r = ,0.632, p = 0.000) and motility (r = ,0.635, p = 0.000). There was no significant relation between serum leptin and seminal parameters and between leptin and gonadal hormone values. The dysfunction of spermatogenesis in varicocele-related infertile male is associated with increase in leptin and leptin receptors. Leptin may have local effects on the function of testis and spermatogenesis. [source] Advanced glycation end products accumulate in the reproductive tract of men with diabetesINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 4 2009C. Mallidis Summary Light microscopic studies comparing sperm parameters show little association between diabetes and male fertility. However, with the introduction of new analytical techniques, evidence is now emerging of previously undetectable effects of diabetes on sperm function. Specifically, a recent study has found a significantly higher sperm nuclear DNA fragmentation in diabetic men. As advanced glycation end products (AGEs) are important instigators of oxidative stress and cell dysfunction in numerous diabetic complications, we hypothesized that these compounds could also be present in the male reproductive tract. The presence and localization of the most prominent AGE, carboxymethyl-lysine (CML), in the human testis, epididymis and sperm was determined by immunohistochemistry. Parallel ELISA and Western blot analyses were performed to ascertain the amount of CML in seminal plasma and sperm from 13 diabetic and nine non-diabetic subjects. CML immunoreactivity was found throughout the seminiferous epithelium, the nuclei of spermatogonia and spermatocytes, in the basal and principle cells cytoplasm and nuclei of the caput epididymis and on most sperm tails, mid pieces and all cytoplasmic droplets. The acrosomal cap, especially the equatorial band, was prominently stained in diabetic samples only. The amount of CML was significantly higher (p = 0.004) in sperm from non-diabetic men. Considering the known detrimental actions of AGEs in other organs, the presence, location and quantity of CML, particularly the increased expression found in diabetic men, suggest that these compounds may play a hitherto unrecognized role in male infertility. [source] Flow cytometric technique for determination of prostasomal quantity, size and expression of CD10, CD13, CD26 and CD59 in human seminal plasmaINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 2 2006LENA CARLSSON Summary Prostasomes are prostate-derived organelles in seminal plasma exhibiting pluripotent properties to facilitate the fertilization process. Seminal prostasome concentration, size distribution and expression of the prostasomal surface antigens CD10, CD13, CD26 and CD59 were examined by flow cytometry. The study group consisted of 79 men with involuntary infertility. Very strong correlations existed between the prostasome expressions of the different CD markers. Significant correlations between prostasome concentration and CD molecules were weak or lacking. Further, no or weak relationships were observed between the prostasomal CD markers and sperm morphology, seminal fructose, neutral , -glucosidase activity, zinc and tumour necrosis factor , concentrations. Flow cytometry is a practical way to study prostasomes in seminal fluid without prior separation. This is a new technique for evaluation of the role of prostasomes and their functions in male reproductive physiology. [source] Leptin and leptin receptor in human seminal plasma and in human spermatozoaINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 6 2003T. Jope Summary Leptin, a 167 amino acid peptide, is known to influence the gonads via direct and indirect effects. Recent studies provide contradictory proposition about the peripheral impact of leptin in the male gonads. Thus, we examined leptin and its receptors in human seminal plasma and in human ejaculated spermatozoa by Western blot technique and fluorescence microscopy. In seminal plasma we found a free leptin band (16 kDa) by an anti-leptin polyclonal antibody. Incubation of seminal plasma with recombinant leptin caused a statistically significant increase in the amount of free leptin (p < 0.01) and supports this finding. Furthermore, a soluble leptin receptor (145 kDa) was found in human seminal plasma in the same specimen. We also detected a 145-kDa leptin receptor isoform in ejaculated spermatozoa as a possible target of leptin action in the male genital tract, which was localized at the tail of spermatozoa by immunofluorescence microscopy only. This receptor was significantly associated with the intactness of sperm plasma membranes. Spermatozoa with deteriorated membranes contained 49.2 ± 6.9% leptin receptor signal intensity compared with spermatozoa having intact membranes (p < 0.01). This finding is difficult to interpret and may be caused by a leakage of OB-R due to loss of membrane integrity. In conclusion, these data provide further hints for a peripheral role of leptin in the male genital tract, possibly, by an interaction between leptin and spermatozoa via sperm leptin receptors. [source] Tachykinins and their possible modulatory role on testicular function: a reviewINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 4 2003Luciano Debeljuk Summary Tachykinins are vasoactive and smooth muscle-contracting peptides with widespread localizations. Tachykinins have been localized in the nerve fibres that supply the testes, in the Leydig cells of different animal species, and also in Sertoli cells of the Siberian hamster testes. The presence of substance P (SP) has also been demonstrated in ejaculated human spermatozoa and in the seminal plasma. Tachykinins have been shown to inhibit the release of testosterone by testicular fragments or by isolated Leydig cells in vitro. Acting on Sertoli cells, tachykinins have been shown to stimulate the release of lactate and transferrin by these cells in vitro, and also to stimulate aromatase activity. Leydig and Sertoli cells express the Preprotachykinin A gene, and this fact strongly suggests that tachykinins can be synthesized in the testes. These findings suggest that tachykinins may have a physiological function in the testes as modulators of the functions of the different cell types contained in these organs. [source] Penile vibratory stimulation and electroejaculation in the treatment of ejaculatory dysfunction,INTERNATIONAL JOURNAL OF ANDROLOGY, Issue 6 2002JENS SØNKSEN Summary The purpose of this review is to present the current understanding of penile vibratory stimulation (PVS) and electroejaculation (EEJ) procedures and its clinical use in men with ejaculatory dysfunction. Unfortunately, the record of treating such individuals has been quite poor, but within recent years development and refinement of PVS and EEJ in men with spinal cord injury (SCI) has significantly enhanced the prospects for treatment of ejaculatory dysfunction. The majority of spinal cord injured men are not able to produce antegrade ejaculation by masturbation or sexual stimulation. However, approximately 80% of all spinal cord injured men with an intact ejaculatory reflex arc (above T10) can obtain antegrade ejaculation with PVS. Electroejaculation may be successful in obtaining ejaculate from men with all types of SCI, including men who do not have major components of the ejaculatory reflex arc. Because vibratory stimulation is very simple in use, non-invasive, it does not require anaesthesia and is preferred by the patients when compared with EEJ, PVS is recommended to be the first choice of treatment in spinal cord injured men. Furthermore, EEJ has been successfully used to induce ejaculation in men with multiple sclerosis and diabetic neuropathy. Any other conditions which affect the ejaculatory mechanism of the central and/or peripheral nervous system including surgical nerve injury may be treated successfully with EEJ. Finally, for sperm retrieval and sperm cryopreservation before intensive anticancer therapy in pubertal boys, PVS and EEJ have been successfully performed in patients who failed to obtain ejaculation by masturbation. Nearly all data concerning semen characteristics in men with ejaculatory dysfuntion originate from spinal cord injured men. Semen analyses demonstrate low sperm motility rates in the majority of spinal cord injured men. The data give evidence of a decline in spermatogenesis and motility of ejaculated spermatozoa shortly after (few weeks) an acute SCI. Furthermore, it is suggested that some factors in the seminal plasma and/or disordered storage of spermatozoa in the seminal vesicles are mainly responsible for the impaired semen profiles in men with chronic SCI. Home insemination with semen obtained by penile vibratory and introduced intravaginally in order to achieve successful pregnancies may be an option for some spinal cord injured men and their partners. The majority of men will further enhance their fertility potential when using either penile vibratory or EEJ combined with assisted reproduction techniques such as intrauterine insemination or in-vitro fertilization with or without intracytoplasmic sperm injection. [source] Varicocelectomy reduces reactive oxygen species levels and increases antioxidant activity of seminal plasma from infertile men with varicoceleINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 5 2001T. Mostafa Several theories have been advanced to explain the mechanisms by which varicocele impairs male fertility. These theories include scrotal hyperthermia, retrograde flow of adrenal or renal metabolites, Leydig cell dysfunction and hypoxia. Varicocele is reported to be associated with elevated reactive oxygen species (ROS) production in spermatozoa and diminished seminal plasma antioxidant activity. The aim of this study was to investigate whether surgical correction of varicocele might reduce ROS or increase the antioxidant capacity of seminal plasma from infertile patients with varicocele. The study group consisted of 68 infertile males, selected from patients scheduled for varicocelectomy at Cairo University Hospital during the year 1999. Seminal plasma levels of two ROS [malondialdehyde (MDA), hydrogen peroxide (H2O2)] and one ROS radical [nitric oxide (NO)] were estimated as well as six antioxidants [superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), vitamin C (Vit C), vitamin E (Vit E), albumin) on the day prior to varicocelectomy. For comparison, the same parameters were measured again 3 and 6 months post-operatively. A statistically significant reduction in the 3 month post-operative levels of MDA, H2O2 and NO was observed when compared with the pre-operative values. A further significant reduction took place during the following 3 months. Four of the six antioxidants tested (SOD, CAT, GPx, and Vit C) showed a significant increase in seminal levels when comparing 3-month post-operative with pre-operative values. A further significant increase of the four antioxidant levels took place during the following 3 months. No significant change in the level of seminal plasma albumen took place during the first 3 months after varicocelectomy, however, a significant increase was noted during the next 3 months. In contrast to other antioxidants, seminal plasma levels of Vit E showed a significant decrease when comparing 3-month post-operative with pre-operative values. A further significant decrease took place during the following 3 months. It is concluded that varicocelectomy reduces ROS levels and increases antioxidant activity of seminal plasma from infertile men with varicocele. [source] Evidence for the presence of 5,-deiodinase in mammalian seminal plasma and for the increase in enzyme activity in the prepubertal testisINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 4 2000Brzezi, lebodzi Thyroid hormones are critical for structural and functional development of the testis and Sertoli cells are considered true target cells for triiodothyronine (T3). However, the role of thyroid hormones in the adult testis seems to be minimal and the mechanism by which they affect testicular function is not known. Due to the existing blood,testis barrier the concentration of thyroid hormones in seminal plasma is kept lower than in blood plasma. We have found that T3 may reach the testis not only from the circulation but also from local enzymic conversion of thyroxine to T3. The presence of the enzymic activity responsible for thyroxine 5,deiodination and for generating T3 locally was also found in boar's seminal plasma. The seminal plasma 5,-deiodinase (5,-D) appeared to be predominantly the propylthiouracil (PTU)-insensitive type II isoenzyme found, so far, in tissues where it plays a role in paracrine signalling. It contains selenocysteine in its molecule (inhibition by aurothioglucose), and has an apparent Km for reverse-T3 as substrate of 0.36 n M and a Vmax 23.8 fmol I,/mg protein/min. Because the seminal plasma 5,-D is partially, but uncompetitively, inhibited by PTU, the presence in seminal plasma of two 5,-D isoenzymes (type I and II) cannot be excluded. The 5,-D activity in testes increased significantly between week 3 and 4, and this increase was concomitant with increase in testicular size. The relationship between testicular weight gain and age showed a similar characteristic change and corresponded to the change in 5,-D activity. Unlike in rodents, the testis of the prepubertal pig has thyroid hormone receptors in Sertoli cells, and suggests that in growing piglets, testicular 5,-D is a key factor regulating local supply of biologically active T3, and is an essential factor in testicular paracrine function. The present results are the first demonstration and characterization of the 5,-deiodinase in seminal plasma. [source] Ultrastructural localization of glycodelin oligosaccharides Le-x and Le-y in human seminal vesicles by immunogold stainingJOURNAL OF ANATOMY, Issue 3 2007M. Piludu Abstract Histo-blood group antigens Le-x and Le-y are oligosaccharidic terminals that characterize many glycoproteins in the human tissues. In seminal plasma, they are expressed as part of the so-called glycodelin S, which is suggested to regulate sperm capacitation/decapacitation. It has recently been demonstrated that the core protein of glycodelin S is secreted by seminal vesicles. Here we show that epithelial cells of human seminal vesicles also release the Le-x and Le-y antigens. The presence of these substances in secretory material was revealed by means of an immunogold staining method in normal surgical samples. The results suggest that glycodelin S is secreted by seminal vesicles in its finished glycosylated form. Moreover, antigen reactivity was also revealed associated with plasma membranes. [source] Protein profile study in European eel (Anguilla anguilla) seminal plasma and its correlation with sperm qualityJOURNAL OF APPLIED ICHTHYOLOGY, Issue 5 2010D. S. Peñaranda Summary Along with sperm quality parameters, the protein profile of European eel seminal plasma was analyzed during induced spermiation (n = 56 samples). Motility, Percentage of live cells, spermatozoa head morphometry and concentration showed low values during the initial weeks of spermiation and maintained high levels throughout the rest of the experiment. The protein profile gradient by SDS-PAGE (4,15%) registered four important electrophoretic bands around 80, 40, 26 and 12 KDa. Three of them showed significant differences in concentration during treatment (80, 40 and 12 KDa), and all of them showed the highest value on the 8th week. Both 80 and 12 KDa bands increased until the 8th week, followed by a progressive decline. One possible explanation for these profiles is that, in the first weeks of treatment, proteins originated from blood plasma are accumulated in the seminal plasma, and from the 8th week some of these proteins are incorporated into the spermatic membranes. The 40 KDa protein band also increased during the first 8 weeks, but maintained high concentrations in the seminal plasma for the rest of the experiment. One result confirms the theory that the presence of proteins in the seminal plasma having a molecular weight lower than 50 KDa increased spermatozoa motility, since the 40 KDa band displayed significantly higher values coinciding with the high percentages of spermatozoa motility. Seminal plasma proteins seem to have an important role in spermatogenesis and spermatozoa movement, but further studies are necessary to discover the identity of these proteins and their precise functions. [source] Physico-biochemical parameters and protein profiles of sperm from beluga Huso husoJOURNAL OF APPLIED ICHTHYOLOGY, Issue 5 2010P. Li Summary Basic physico-biochemical parameters and protein profiles of sperm from beluga (Huso huso), have been evaluated. The results show a stable spermatozoan velocity (ranging from 136.23 ± 5.63 to 105.78 ± 5.27 ,ms,1) and motility during 2 min post activation, as well as a long duration of the overall spermatozoa motility period (up to 5 min). Mean values were determined for seminal plasma protein concentration (0.29 ± 0.16 mg ml,1), spermatozoa concentration (0.28 ± 0.27 × 109 spz ml,1), seminal plasma osmolality (51.33 ± 4.91 mOsmol kg,1), the pH (8.49 ± 0.01) and Na+ (18.97 ± 3.65 mm), K+ (2.83 ± 1.36 mm), Ca2+ (0.19 ± 0.06 mm), Mg2+ (0.49 ± 0.23 mm) and Cl, (6.33 ± 0.58 mm) concentrations. Moreover, in seminal plasma, five protein bands with molecular weights (MW) of 71, 49, 46, 34, 29 kDa were identified. In spermatozoa, about 100 spots with molecular weights varying from 26.5 to 107 kDa and iso-electric points ranging from 5 to 9.5 were found. The observed physiological and biochemical properties, together with protein patterns, should be considered for the development of methods for controlled reproduction and sperm cryopreservation for the highly endangered beluga sturgeon. [source] Prostaglandins in rainbow trout (Oncorhynchus mykiss Walbaum, 1792) sperm biology , searching for answersJOURNAL OF APPLIED ICHTHYOLOGY, Issue 4 2008R. K. Kowalski Summary The purpose of this study was to determine the concentrations of prostaglandins E2 and F2, (PGE2 and PGF2,) in the blood, testis and seminal plasma of mature male rainbow trout and in the ovarian fluid to assess the effects of these prostaglandins on sperm motility parameters when present in activation media. Also prolonged incubation with prostaglandins on sperm motility and calcium influx were studied. The profile of PGE2 and PGF2, differed in concentration between blood, testicular supernatant and seminal plasma. PGE2 was predominant in the blood sample (0.29 ng ml,1) and testicular supernatant (3.1 ng ml,1) whereas their level in seminal plasma was lower than PGF2, (0.23 ng ml,1). The concentrations of PGF2, in blood, testis and seminal plasma were 0.04, 0.99, 1.3 ng ml,1, respectively. In the ovarian fluid the concentrations of both prostaglandins were higher than in the male reproductive tract. Adding both prostaglandins to activation buffer (at concentrations 15 and 70 ng ml,1) had no effect on any CASA parameters. Calcium influx related to rainbow trout sperm incubations with PGE2, and PGF2, was not detected. After 24 h incubation of sperm in artificial seminal plasma solution without and with prostaglandins all sperm samples increased their motility potential and intracellular calcium concentration. Therefore, this effect was not related to the presence of prostaglandins. In summary PGE2, and PGF2, were present in the rainbow trout male reproductive tract, and their profile varies from that of blood, testis and seminal plasma. The specific role of both prostaglandins in salmonid sperm biology remains unclear. [source] Respiration of steelhead trout sperm: sensitivity to pH and carbon dioxideJOURNAL OF FISH BIOLOGY, Issue 1 2003R. L. Ingermann Steelhead trout Oncorhynchus mykiss sperm held in seminal plasma or sperm-immobilizing buffer (pH 8·6) at 10° C consumed O2 at the rate of c. 2 nmol O2 min,1 10,9 sperm; the rate of O2 consumption was not different in sperm held for 4 or 24 h. Decreasing the extracellular pH from 8·5 to 7·5 either by diluting semen with buffer titrated with HCl or by increasing the partial pressure of CO2 in the incubation atmosphere resulted in c. a 40% decrease in the rate of sperm respiration. The data did not, however, support the hypothesis that the precipitous reduction in the capacity for sperm motility that occurs as external pH is reduced is a result of a decrease in cellular metabolism. The rate of O2 consumption of freshly collected semen from different males was not correlated to cellular ATP content or to the proportion of sperm that were motile upon activation; the initial ATP content and sperm motility were positively correlated. The rate of O2 consumption was not significantly increased following sperm activation or by the addition of an uncoupler of oxidative phosphorylation, carbonyl cyanide p -trifluoromethoxyphenylhydrazone, suggesting that these sperm have little, if any, capacity for increased oxidative metabolism. [source] Multicenter quality control of the detection of HIV-1 genome in semen before medically assisted procreationJOURNAL OF MEDICAL VIROLOGY, Issue 7 2006Christophe Pasquier Abstract Couples in whom the man is HIV-1-positive may use medically assisted procreation in order to conceive a child without contaminating the female partner. But, before medically assisted procreation, the semen has to be processed to exclude HIV and tested for HIV nucleic acid before and after processing. The performance was evaluated of the technical protocols used to detect and quantify HIV-1 in 11 centers providing medically assisted procreation for couples with HIV-1 infected men by testing panels of seminal plasma and cells containing HIV-1 RNA and/or DNA. The performance of these tests varied due to the different assays used. False positive results were obtained in 14,19% of cases. The sensitivity for RNA detection in seminal plasma was 500,1,000 RNA copies/ml, over 500 RNA copies/106 cells in semen cells, and for DNA detection in semen cells 50,500 DNA copies/106 cells. The use of silica-based extraction seemed to increase the assay performance, whereas the use of internal controls to detect PCR inhibitor did not. This first quality control highlights the need for technical improvements of the assays to detect and quantify HIV in semen fractions and for regular evaluation of their performance. J. Med. Virol. 78:877,882, 2006. © 2006 Wiley-Liss, Inc. [source] Modified expression of cytoplasmic isocitrate dehydrogenase electrophoretic isoforms in seminal plasma of men with sertoli-cell-only syndrome and seminomaMOLECULAR CARCINOGENESIS, Issue 6 2008Mireille Starita-Geribaldi Abstract Two isoforms of human cytoplasmic isocitrate dehydrogenase (IDPc) of close molecular weights and different isoelectric points were identified in human seminal plasma (SP) by two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry (MS). These two isoforms were detected in the normospermic men SP and their expressions were markedly altered in patients with testicular seminoma, the most frequent testicular germ cell cancer (TGCC): increase of the more acidic spot and decrease of the more basic one. Since oligospermia has been considered as a high risk pathological condition for developing a testicular cancer, the two IDPc isoforms were analyzed in SP of a group of secretory azoospermic patients. In this group the two spots displayed similar variations of expression to those observed in testicular seminoma. These results propose IDPc as a promising SP biomarker of testicular seminoma. Whether IDPc alteration in secretory azoospermia is predictive of testicular seminoma remains to be elucidated. © 2007 Wiley-Liss, Inc. [source] Heparin-binding proteins of human seminal plasma: purification and characterizationMOLECULAR REPRODUCTION & DEVELOPMENT, Issue 12 2008Vijay Kumar Abstract Human seminal plasma (HuSP) contains several proteins that bind heparin and related glycosaminoglycans. Heparin binding proteins (HBPs) from seminal plasma have been shown to participate in modulation of capacitation or acrosome reaction and thus have been correlated with fertility in some species. However, these have not been studied in detail in human. The objective of this study was to purify major HBPs from HuSP in order to characterize these proteins. HBPs were isolated by affinity,chromatography on Heparin,Sepharose column, purified by reverse-phase high-performance liquid chromatography (RP-HPLC) and Size-exclusion chromatography and checked for purity on sodium-dodecyl PAGE (SDS,PAGE). Identification of HBPs was done by matrix-assisted laser desorption-ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS). Here we report the purification and identification of seven HBPs in seminal fluid. The major HBPs are lactoferrin and its fragments, semenogelin I fragments, semenogelin II, prostate specific antigen, homolog of bovine seminal plasma-proteins (BSP), zinc finger protein (Znf 169) and fibronectin fragments. In this study we are reporting for the first time the purification and identification of BSP-homolog and Znf 169 from HuSP and classified them as HBPs. Here we report the purification of seven clinically important proteins from human seminal fluid through heparin affinity chromatography and RP-HPLC, in limited steps with higher yield. Mol. Reprod. Dev. 75: 1767,1774, 2008. © 2008 Wiley-Liss, Inc. [source] | |||||||||||||||||||||||||||||||