Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “EPIDIDYMITIS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,405 records · Page 78Linked to original sources
PubMed1983

The relationship between motility and the FITC-BSA binding properties of mouse epididymal spermatozoa.

Mouse epididymal spermatozoa exposed to fluorescein isothiocyanate-conjugated bovine serum albumin (FITC-BSA) immediately following dilution or after a 2-hour incubation period under fertilization conditions, were assessed by fluorescence microscopy for albumin adsorption. Motile spermatozoa exhibited light fluorescence in the midpiece and tail but not in the head. In contrast the majority of nonmotile spermatozoa displayed a strong and characteristic fluorescence in the post acrosomal region of the sperm head as well as the midpiece. Spermatozoa immobilised by short-term heat stress exhibited fluorescence in the post acrosomal region and midpiece as before but also in the acrosomal cap. The equatorial region failed to fluoresce. The significance of these observations on the involvement of albumin in capacitation is discussed.

Acrosome↗
PubMed1991

Effect of photoperiod on the rate of 3H-thymidine incorporation of epididymal principal cells in adult Syrian hamsters.

Photoperiod-induced cycles of gonadal regression and recrudescence in the Syrian hamster were used to determine if epididymal growth in adults involves mitotic activity of principal cells. In Experiment 1, the following groups of adult hamsters were examined: induced recrudescing (5L:19D [5 hr light and 19 hr dark] for 13 wk followed by 14L:10D for at least 3 wk), spontaneous recrudescing (5L:19D for 25 wk), and active gonadal state (14:10D). In Experiment 2, adult hamsters were divided into the following groups: induced recrudescing, active, and regressed (5L:19D for 16 wk). Hamsters received subcutaneous injections of 0.5 microCi 3H-thymidine/g body weight three times/wk for 3 wk. The epididymis was fixed in a glutaraldehyde followed by osmium, embedded in Epon 812, and sectioned at 1 micron. Slides were dipped in Kodak NTB-3 emulsion, exposed for 2 or 3 months, developed, and evaluated for isotopic labeling of principal and basal cell nuclei by scoring 500 to 1,000 nuclei. In Experiment 1, the percentages of labeled principal cell nuclei for the induced recrudescing, spontaneous recrudescing, and active groups were 26 +/- 2%, 23 +/- 5%, and 9 +/- 1%, respectively. Considering the intermittent availability of 3H-thymidine during 21 days, this represents daily recruitment of 6.3%, 5.6%, and 2.2%, respectively. In Experiment 2, the percentages of labeled principal cell nuclei for induced recrudescing, active, and regressed groups were 12 +/- 4%, 3 +/- 1%, and 4 +/- 1%, respectively. There was no effect of photoperiod on labeling pattern of basal cells (1.5 +/- 0.6%, 1.2 +/- 0.1%, 0.4 +/- 0.1% for the three photoperiod groups, respectively).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1991

Zinc-protein from rat prostate fluid binds epididymal spermatozoa.

The detection and the isolation of a zinc-protein from the secretion of the rat dorsolateral prostate is described. The purification procedure, based on gel filtration and cationic exchange chromatography, allowed to separate a minor protein (Mr approximately 66,000) from free zinc ions and other secretory components. Two zinc ions were estimated to be associated with one molecule of isolated protein. The zinc-protein was labelled with 125I and then incubated at 37 degrees C with spermatozoa from rat epididymal cauda. Time-dependent in vitro binding of the radioactive protein to sperm cells was demonstrated. This binding was not affected by the presence of proteins from the seminal vesicle during the incubation, while it was blocked in the presence of an excess of unlabelled zinc-protein. After binding, the labelled spermatozoa were treated with a buffer containing 0.5% sodium deoxycholate and 40 mM EDTA; only very small amounts of label were removed from the cells, thus suggesting that the zinc-proteins were kept on the plasma membrane by interactions which do not involve merely hydrophobic bonds.

Animals↗
PubMed1991

Fertilizing capacity of epididymal and testicular spermatozoa microinjected under the zona pellucida of the mouse oocyte.

Mouse spermatozoa were obtained from the testis and caput, corpus, and cauda epididymis incubated for 2 h in capacitation medium and a single spermatozoon from the capacitated samples microinjected into the pervitelline space of mature mouse oocytes. Spermatozoa from the testis were unable to fertilize oocytes and few spermatozoa from the caput were capable of fertilization (0-7% depending on the method of preparation). Similar fertilization rates (30-45%) were obtained with spermatozoa with forward progressive motility from the proximal and distal corpus and the cauda epididymis, but those that were vibratory or with local circular motility had significantly reduced fertilizing capacity (6-10%). The capacity of spermatozoa from the different regions of the testis and epididymis to bind to zona-free oocytes followed the same pattern as fertilization rate after microinjection. There was a progressive increase in acrosome reactions after 2 h incubation in capacitation medium in samples obtained from the testis to the cauda epididymis. Maturation of the capacity to bind to the perivitelline membrane and to develop forward progressive motility, rather than the capacity to acrosome react, appears to govern the fertilization of oocytes in which the zona has been bypassed by microinjection. These characteristics are obtained in the proximal segment of the corpus. However, there was evidence that the embryo developmental capacity of oocytes fertilized by spermatozoa from the higher segments of the epididymis is reduced, particularly in oocytes fertilized by caput spermatozoa. These observations suggest that sperm microinjection may have only a limited benefit for improving fertilization rates for men with high epididymal obstructive azoospermia.

Acrosome↗
PubMed1992

Specific distribution of an epididymal 50 kDa protein revealed by an anti-Mos protein monoclonal antibody.

An anti-Mos protein monoclonal antibody, 4A6, was used to investigate the distribution of the antigen in the epididymis, in which the c-mos gene is reportedly expressed. The 4A6-reactive antigen was found on the basement membrane and luminal surface of the epithelial cells in the caput epididymis of BALB/c male mice as well as in the proximal corpus epididymis, the cauda epididymis, and the vas deferens. The 4A6 antigen was also found on the luminal surface of the epithelial cells in the epididymis of male germ cell-deficient C57BL/6J-Wv/Wv mice. This confirmed that the 4A6 antigen does not derive entirely from the testicular c-Mos protein but is synthesized in the epididymis. Western blot analysis revealed that the molecular weight of the epididymal 4A6 antigen was 50 kDa, which is unusually high for the c-Mos protein. With its specific distribution in the epididymis, the protein should play a specific role in functions of the epididymis.

Animals↗
PubMed1992

Cauda epididymal sperm interactions with seminal vesicle fluid.

The interaction of rat cauda epididymal sperm cAMP-dependent protein kinase (PKA) with seminal vesicle fluid (SVF) proteins was examined. Specific proteins in SVF act as substrates for the sperm cell PKA. The apparent molecular weights of these proteins are 45.0, 31.5, 17.2, 14.7, and 13.3 kDa. The phosphorylation of one low-molecular-weight cauda sperm protein is blocked in the presence of SVF. There is no PKA enzyme activity in SVF. The presence of phosphate transfer activity between the sperm cell enzyme and the SVF proteins is species dependent. For example, mouse and rat SVF proteins are efficient phosphate acceptors, but there is no phosphorylation activity when hamster SVF is used as the enzyme substrate. The sperm cell samples were also assessed for membrane integrity. Specifically, cauda sperm cells used in these assays were judged to be intact when examined microscopically using the fluorescent vital dye carboxyfluorodiacetate. Although there was enzyme activity in the supernatants of the rat sperm cell samples, in the protein kinase assay it required three times as much supernatant volume (compared with intact cell sample volume) to measure the activity. Supernatant enzyme activity did not increase with washing, indicating that the cells were not damaged by this procedure. The enzyme itself does not adhere to the sperm cells, so the PKA enzyme activity is most likely oriented on the external surface of the sperm cell.

Animals↗
PubMed1992

Human sperm proteins from testicular and epididymal origin that participate in fertilization: modulation of sperm binding to zona-free hamster oocytes, using monoclonal antibodies.

In order to identify human sperm surface proteins involved in the gamete recognition process, mouse monoclonal antibodies were directed against human spermatozoa and screened with live spermatozoa by enzyme-linked immunosorbent assay (ELISA). Immunoperoxidase staining of human testis showed the early presence of four corresponding proteins on germinal cells, while six were detected primarily in testis fluid. The presence of 17 proteins was evidenced in the epididymis. Eight were detected with a decreasing gradient from the beginning to the end of the organ, including vasa efferentia for three of them. The other nine were observed in only one defined segment, usually the caput epididymis, which was found to be the most active region. Comparison of spermatozoa patterns from testis, vasa efferentia, and the three regions of epididymis pointed out a progressive coating. By contrast, three antibodies displayed a migration of spermatozoa surface domains in the course of epididymal transit. Six antibodies were found to inhibit human spermatozoa adherence to zona-free hamster oocytes, while nine promoted it. Molecular weights of antigens corresponding to nine of the antibodies ranged from 11 to 215 kDa. No correlation could be established with previously described human proteins. These observations emphasize the role of epididymis in human sperm maturation.

Animals↗
PubMed1993

Improved preservation of rat epididymal sperm for high-resolution low-voltage scanning electron microscopy (HR-LVSEM).

Various fixation protocols were used in an attempt to improve preservation of rat epididymal sperm for high-resolution low-voltage scanning electron microscopy (HR-LVSEM). Wash solutions and fixatives of different composition and osmolarity were tested. Paraformaldehyde and glutaraldehyde concentrations were varied between 0.5% and 3%. Ruthenium red was tested as an additive in both primary fixation and postfixation, or in postfixation alone. HR-LVSEM revealed various degrees of ruffing, folding, blebbing, and peeling off of the plasma membrane, as well as holes of different sizes. The plasma membrane overlying the acrosome and the connecting piece proved to be particularly sensitive to varying fixation conditions. Consistent topographical differences were revealed among the different domains over the sperm head. Most of the differences were considered to be artifacts. Their consistency, however, suggests that structural and biochemical differences exist either within the membrane or in the structures subjacent to the membrane. Primary fixation turned out to be less critical than postfixation. Preservation of a smooth plasma membrane without holes could only be achieved when primary fixation in low aldehyde concentrations, with or without ruthenium red, was followed by postfixation with OSO4 and 1,000 ppm ruthenium red. Examination of thin sections of the same material confirmed that even a considerable number of small holes are difficult to detect in transmission electron microscopy. These results show that with the recent increase in resolution of LVSEM there is need for further effort to improve sample processing.

Animals↗
PubMed1993

Biochemical characterization and epididymal localization of the maturation-dependent ram sperm surface antigen ESA152.

We examine here the biochemical properties and epididymal localization of a maturation dependent ram sperm surface antigen. A monoclonal antibody, ESA152, identifies an antigen that is present on the surface of ejaculated sperm, but is absent from testicular sperm. Crosslinking of the ESA152 antigen with bivalent antibodies induces the acrosome reaction, redistributing the antigen into the anterior region of the sperm head where it associates with the fusion product of the plasma membrane and the outer acrosomal membrane. The ESA152 antigen appears as a polypeptide of 18 kDa on immunoblots of SDS-polyacrylamide gels. The ESA152 epitope includes the sialic acid termini of N-linked oligosaccharides, as shown by its sensitivity to neuraminidase and endoglycosidase F. The ESA152 antigen is a highly hydrophobic integral membrane protein that resists aqueous extraction, partitions into the detergent phase of Triton-X-114, and solubilizes in chloroform-methanol mixtures. The anchoring of ESA152 is unaffected by phosphtidylinositol specific phospholipase C. The antigen is absent from extracts of caput and corpus epididymidis but appears abruptly in the first segment of the cauda. Immunofluorescence reveals that the ESA152 epitope first appears in clusters of cells in the luminal epithelium of the proximal cauda, prior to or concurrent with its appearance on sperm.

Animals↗
PubMed1994

Maturation of hamster epididymal sperm motility and influence of the thiol status of hamster and rat spermatozoa on their motility patterns.

A method for objective quantification of hamster sperm movement parameters as an indicator of maturation along the epididymis was established using a computerised system. Analysis of spermatozoa released into medium from five epididymal regions showed that the most drastic increases in percentage motility and curvilinear velocity (VCL) occurred from the distal corpus to the beginning of the proximal cauda and in straight-line velocity (VSL) from the beginning to a more distal site within the proximal cauda region. Both high osmolarity (400 mOsm/kg) and the thiol-oxidising agent diamide (10 microM) increased flagellar straightness of distal corpus spermatozoa, but VSL was increased only with the latter. The thiol-reducing agent dithiothreitol (DTT, 1mM) stimulated and maintained percentage motility and velocities of spermatozoa from the caput, stimulated only percentage motility of distal corpus sperm, but decreased velocities of those from the proximal cauda in prolonged incubation. In rats, diamide increased path straightness but not velocities of caput spermatozoa and yet caused immotility within 15 min, whereas DTT prolonged the maintenance of in vitro motility. The slight increases in kinematic parameters in the presence of DTT were enhanced by a 2-min preincubation with diamide. The finding that the effects of DTT and diamide were not compensatory suggests that the influence of the SH/S-S status on sperm movement is multifaceted, with decreasing sensitivity to stimulation upon sperm maturation.

Animals↗
PubMed1987

Cytochemical analysis of the anionic sites on the membrane of the stallion spermatozoa during the epididymal transit.

The structure, relative density, and distribution of anionic sites on the surface of epididymal and ejaculated spermatozoa were studied using polycationic ferritin (CF), colloidal iron hydroxide (CIH), various enzymatic treatments, methylation, and de-acetylation. Macro-molecules containing sugar residues, probably sialic acid, are part of the sperm membrane and show a characteristic distribution and density that is dependent of the sperm region and of its origin. Unlike the spermatozoa of other eutheria examined, the exposure of the stallion spermatozoa to neuraminidase treatment did not produce significant changes in the density of the negative charge of the sperm surface. The ability of purified neuraminidase to act only after saponification suggests that sialic acid may be present in the acetylated form. When CIH was used it is seen that the density of the negative charge is rather uniform within a particular segment of the spermatozoa and abruptly changes at the junction of morphologically distinct segments (Between the acrosomal and post acrosomal region of the sperm head and between the post acrosomal region and middle piece of the flagellum). The acrosome presented more negative groups dissociated at pH 1.8 than the postacrosomal region. A greater concentration of anionic sites over the flagellum was also observed when CIH and CF were used. This asymmetry probably represents different domains that may be related to specific functions. The cytochemical observations and the cellular electrophoretic mobility measurements did not show striking differences on the negative charge of sperm obtained from different regions of epididymis and ejaculates in contrast to previous results in other species. The spermatozoa collected from caput epididymidis bind CIH but not all population present equal response. In corpus and cauda region of epididymis the population displaying the capacity to bind CIH or CF significantly over the head and tail surface was the majority. This study corroborates that the distribution and density of terminal oligosaccharide residues on the sperm plasma membrane has species specific characteristics. The surface charge of the spermatozoa obtained either during the breeding or nonbreeding season, determined by measurements of cellular electrophoretic mobility and by the binding pattern of CIH and CF, does not show significant differences.

Animals↗
PubMed1988

Hamster sperm motility transformation during development of hyperactivation in vitro and epididymal maturation.

The transformation of hamster sperm motility during capacitation in vitro and during maturation in the caudal epididymis was analyzed and compared using videomicrography. Sperm recovered from the distal portion of the caudal epididymis, as well as ejaculated sperm recovered from the uterus exhibited low amplitude, planar flagellar beating. By 3 hr of incubation under capacitating conditions, the caudal epididymal sperm were swimming in helical patterns apparently produced by significantly increased acuteness of flagellar bending and by torsion seen as abrupt, periodic turning of the head. By 4 hr, most sperm were hyperactivated, swimming in circles resulting from asymmetrical, planar flagellar bending that was significantly more acute than the preceding patterns. When motility parameters of fresh sperm were compared with those of sperm swimming in the transitional helical pattern and with hyperactivated sperm, transitional sperm had significantly higher net and average path velocities than the others, indicating that they covered space at the greatest rate. This suggests that the transitional phase plays an important role in sperm transport. Sperm recovered from the proximal region of the caudal epididymis, near the corpus, swam in either the helical or hyperactivated patterns, or a mixture of the two. The means of their flagellar curvature ratios and linear indices were intermediate between helical and hyperactivated mean values. Thus, sperm undergoing final maturation in the caudal epididymis reverse the pattern of development of hyperactivation. Also, the development of hyperactivated motility must therefore entail induction of a preexisting potential for flagellar movement, rather than a maturational process.

Acrosome↗
PubMed2006

Epididymal cystadenomas and epithelial tumourlets: effects of VHL deficiency on the human epididymis.

Although epididymal cystadenomas (ECAs) are among the most frequent VHL disease-associated tumours, fundamental questions about their pathogenesis have remained unanswered. Classification of ECAs is controversial, and the cell of origin is unknown. It is also unknown whether ECAs-like other VHL disease-associated tumours-arise as a result of VHL gene inactivation, and whether ECAs exhibit subsequent activation of hypoxia-inducible factor HIF. Moreover, the morphological spectrum of earliest ECA formation is unknown. In a detailed molecular pathological analysis of a series of epididymides collected from VHL patients at autopsy, we found that ECAs are true neoplasms that arise secondary to inactivation of the wild-type copy of the VHL gene, followed by early and simultaneous activation of HIF1 and HIF2 associated with up-regulation of downstream targets, including CAIX and GLUT-1. The observations also indicate that ECA formation evolves from a variety of microscopic epithelial tumourlets, and that these tumourlets are confined to the efferent ductular system. Although genetic and immunohistochemical analysis of precursor structures consistently revealed VHL gene inactivation and activation of HIF in the precursor lesions, only a small subset appears to progress into frank cystadenoma. Thus, ECA tumorigenesis in VHL disease shares fundamental principles with tumorigenesis in other affected organ systems.

Basic Helix-Loop-Helix Proteins↗
PubMed1993

Purification and characterization of a 38-kDa protein, sp38, with zona pellucida-binding property from porcine epididymal sperm.

A 38-kDa protein, sp38, was purified from the detergent extract of porcine epididymal sperm. Sp38 showed zona pellucida-binding properties similar to those of proacrosin. These two proteins specifically bound to the 90-kDa glycoprotein form of the zona pellucida components in a calcium-dependent manner. The binding of sp38 to the zona pellucida glycoprotein was inhibited by proacrosin. These findings suggest that the two proteins competitively interact with the zona pellucida during the early stage of fertilization.

Acrosin↗
PubMed1997

Distribution of 105-kDa sperm unique antigen on goat epididymal mature spermatozoa.

The sperm surface antigens are organized into topographic domains, specifically formed into the membrane during the sperm maturation in the epididymis. The present study was directed to determine the distribution of 105 KD sperm membrane antigen (SMA2) into the cell by affinity purified antibody, generated by 105 KD sperm antigen. The cytoimmunofluorescence study of the integrated sperm cell reveal that the antigen is localized in the anterior head overlying the acrosome. On immunoblotting of isolated head and flagellum polypeptides it has been demonstrated that this antigen is selectively present in the head membrane and absent in the flagellum. Because of its selective presence in the anterior head membrane overlying the region of acrosome on mature spermatozoa, the 105 KD sperm unique glyco-antigen may have a role in events leading to sperm-egg recognition. It is a first report of a high molecular mass membrane antigen being localized in the anterior head membrane of goat mature epididymal spermatozoa.

Animals↗
PubMed1998

Identification of phosphoproteins coupled to initiation of motility in live epididymal mouse sperm.

A method for collecting live immotile cauda epididymal mouse sperm that initiate motility by dilution into an activation buffer is described. Sperm in collection buffer showed low percent motility (MOT) and population progression (PRG) that increased 10-fold and 9-fold, respectively, during the first 2 min after dilution into activation buffer. Western phosphoserine (pS), phosphothreonine (pT), and phosphotyrosine (pY) analysis revealed a 120 kDa protein that markedly increased in pT content during initiation of motility and may be related to FP130, the motility-coupled axonemal protein of sea urchin sperm. A prominent 82 kDa protein that was pS and pT-phosphorylated in immotile and motile sperm is likely the fibrous sheath component AKAP82 that is phosphorylated during spermatogenesis. Analysis of live human sperm also identified a prominent 120 kDa pT protein. Thus it appears that phosphorylation of FP130 and related 120 kDa proteins in mouse, and perhaps human sperm, represent common targets during motility initiation in sperm.

Animals↗
PubMed2000

Development of a simple sperm cryopreservation model using a chemically defined medium and goat cauda epididymal spermatozoa.

This investigation was carried out to develop a simple sperm cryopreservation model using a chemically defined synthetic medium (modified Ringer's solution) and mature goat cauda epididymal sperm as the model system. Rates of cooling, freezing, and maximum freezing temperature were manipulated with the help of a computer-controlled programmable biofreezer. Highly motile goat cauda sperm dispersed in a modified Ringer's solution was subjected to the freezing protocol: cooling 0.25 degrees C min(-1) to 5 degrees C, 5 degrees C min (-1) to -20 degrees C, 20 degrees C min(-1) to -100 degrees C, prior to plunging into liquid nitrogen. In the absence of any cryoprotective agent, all of the spermatozoa lost their motility. Addition of glycerol (0.22 to 0.87 M) caused a dose-dependent increase of sperm motility recovery. The highest recovery of forward and total motility was (32 and 35%, respectively) at 0.87 M. Further increase of the glycerol concentration caused a marked decrease in motility. Changes in the cooling rate particularly before and during freezing had a notable effect on the sperm motility recovery. There was no or low recovery (0-18%) of sperm motility when the cells were transferred directly to liquid nitrogen from the initial two cooling stages. The data demonstrate the importance of all of the cooling stages in the cryopreservation of the cells. Like glycerol, dimethyl sulfoxide (Me(2)SO) and ethylene glycol also showed a dose-dependent increase in motility recovery as well as a biphasic curve of cryoprotection. At optimal concentrations, dimethyl sulfoxide (1.00 M) and ethylene glycol (1.29 M) were effective in recovering sperm motility to the extent of 20 and 13%, respectively. Thus these reagents have markedly lower cryoprotection potential than glycerol.

Animals↗
PubMed2001

Effect of amino acids on goat cauda epididymal sperm cryopreservation using a chemically defined model system.

Studies were carried out to analyze the cryoprotecting efficacy of several amino acids by use of a chemically defined synthetic medium (modified Ringer's solution) and goat cauda epididymal sperm as the model system. Motile goat cauda sperm dispersed in the synthetic medium were subjected to a freezing protocol in a computer-controlled bio-freezer, cooling 0.25 degrees C x min(-1) to 5 degrees C, 5 degrees C x min(-1) to -20 degrees C, and 20 degrees C x min(-1) to -100 degrees C, prior to being plunged into liquid nitrogen. In the absence of amino acids, sperm cells completely lost their flagellar motility. Of all the amino acids tested, l-alanine showed maximal cryoprotection potential. l-Alanine at 135 mM offered optimum cryoprotection potential: recovery of sperm forward motility and total motility were 14 +/- 2% and 19 +/- 2%, respectively. l-Glutamine, l-proline, and glycine at optimum concentration (100-150 mM) cryopreserved approx. 11-17% total motility of the sperm cells, whereas amino acids such as l-arginine, l-lysine, and l-histidine offered little cryoprotection (0-5%) to the cells. Increasing the amino acid concentration beyond the optimum level sharply decreased the recovery of the sperm motility, which therefore showed a biphasic cryoprotection profile. Addition of amino acids enhanced (approx. 7-10%) the cryoprotection efficacy of the well-known cryoprotectants glycerol and a combination of glycerol and dimethyl sulfoxide. The presence of glycerol caused a marked reduction (from 100-150 mM to 20-70 mM levels) in the optimal cryoprotective concentration of the amino acids. The combined cryoprotecting action of glycerol, dimethyl sulfoxide, and amino acids provided motility recovery as high as 52%. The observation that amino acids and dimethyl sulfoxide had an additive effect in augmenting the cryoprotecting potential of glycerol suggests that the mechanism of their action is different from that of glycerol. This cocktail of cryoprotectants may be useful for cryopreservation of semen of various species.

Amino Acids↗