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At least 937 records · Page 52Linked to original sources
PubMed1978

Microscopic vasoepididymostomy: specific microanastomosis to the epididymal tubule.

A new microscopic technique for vasoepididymostomy is described. Conventional approaches to epididymal obstruction rely on the formation of a fistulous tract after the walls of the vas deferens are grossly sutured to the outer tunic of the epididymis; such methods have a low success rate. With a direct and accurate end-to-end anastomosis of the inner lumen of the vas deferens specifically to the epididymal tubule there is a greater likelihood of normal patency. Furthermore, such an anastomosis can be performed at the lowest possible level of the epididymis, allowing a greater opportunity for sperm maturation.

Epididymis↗
PubMed1995

[Clinical evaluation of a new polymerase chain reaction assay for detection of Chlamydia trachomatis in young patients with acute epididymitis].

Specimens from 15 young patients presenting with acute epididymitis were tested for the presence of Chlamydia trachomatis by an enzyme immunoassay (EIA), polymerase chain reaction (PCR), and for other bacteria by standard laboratory techniques. C. trachomatis urethral infection was detected in 3 patients by an EIA test of the urethral swabs (20%) and in 13 patients by the PCR (87%). This difference in detection rate was statistically significant (p < 0.005). Thirteen specimens were positive by the PCR, but only three of them were positive by the EIA method. These findings indicate that the PCR assay is a highly sensitive assay for the detection of C. trachomatis in male urine specimens and provides a noninvasive technique for routine screening of chlamydia infection in the patient with acute epididymitis.

Acute Disease↗
PubMedDate not supplied

[Acute experimental and clinical epididymitis].

In pathogenesis of acute epididymitis (AE) an important role belongs to retrograde infection of the epididymis. The infection with urethral or urinary flora occurs via reflux and adhesive mechanisms. Staging of the disease and differentiation of acute epididymitis with epididymo-orchitis are the essential aims in the diagnosis. For elderly patients with AE who comprise the majority of AE patients urgent epididymectomy is thought the best therapeutic approach.

Acute Disease↗
PubMed1998

[Acute epididymitis in a 3-month-old infant: an infrequent presentation].

The acute Epididymitis is a very uncommon disease in children under 3 years old. We present the clinic case in a suckling child of 3 months old with onset of an acute scrotum, being necessary the surgical exploration to define the exact diagnosis of acute Epididymitis. We make a revision on world medical references and found out a very low incidence in children under 1 year old (0.7-3%); so it is considered of interest to publish it with the double finality to be taken into account in the presence of an acute scrotum and to contribute with a new case of this unusual pathology in babies under 1 year old.

Acute Disease↗
PubMed1998

[Epididymitis in infants--a possibility].

Usually, acute scrotum in infants is due to torsion, but there are reasons to believe that primary inflammation occurs more often than supposed. Urethrovasal reflux is the primary mechanism, and it is often associated with urogenital anomalies among infants and dysfunctional voiding among young boys. Colour Doppler ultrasound, scintigraphy and surgical exploration are the tools for differentiating epididymitis from torsion. We present a six months' old child with epididymitis, who was investigated because of suspected torsion. The investigations showed bacteruria, but no anomalies.

Diagnosis, Differential↗
PubMed1997

Cumulus cell dispersal from murine oocytes by an epididymal guanidinobenzoatase.

Guanidinobenzoatase (GB), a serine proteinase with a molecular weight of 71,000, is found both free in the epididymal fluids of the mouse and bound to the sperm surface. Microgram quantities of the enzyme, purified from epididymal fluid, will completely disperse follicle cells from freshly ovulated oocytes after 15 min of incubation. Purified GB exhibits no hyaluronidase activity as determined by the acid albumin assay. The ability of GB to disperse follicle cells is blocked by a proteinase inhibitor endogenous to the male reproductive tract. The inhibitor has no effect on bovine testicular hyaluronidase. Although the function of GB has not been defined, the observations presented here indicate that it may play a role in cumulus matrix penetration during fertilization.

Animals↗
PubMed1997

Characterization of the guanidinobenzoatase in the epididymal fluids of the mouse.

Guanidinobenzoatase (GB), a proteolytic enzyme found in the epididymal fluids of mice, was purified to apparent homogeneity by molecular sieving and affinity chromatography. It has a molecular mass of 71 kDa and its enzymatic activity is heat labile and sensitive to EGTA. Its kinetic parameters (K(m) of 6.66 microM and a Vmax of 4.38 nmol/min/mg) were determined using 4-methylumbelliferyl-p-guanidinobenzoate (MUGB) as the substrate. GB activity is concentrated in the cauda epididymal region of the genital tract. Heat-solubilized whole zonae, biologically active ZP3, and several serine proteinase inhibitors, including a proteinase inhibitor endogenous to the male genital tract, effectively block the ability of GB to hydrolyze MUGB. Pretreating cumulus-free, zonae intact oocytes with purified GB reduces, in a concentration-dependent manner, the number of sperm able to bind to the zonae. The function of the soluble enzyme is not known. Its ability to bind both trypsin inhibitors and ZP3 suggests a possible role in gamete recognition.

Acrosome↗
PubMed1999

Biochemical maturation of Spam1 (PH-20) during epididymal transit of mouse sperm involves modifications of N-linked oligosaccharides.

Indirect immunofluorescence of mouse caput and caudal sperm shows distinctly different distributions of Spaml protein, which is associated with structural and functional differences of the molecule. Spam1 is uniformly distributed over the surface of the head of caput sperm while in caudal sperm, light and confocal microscopy demonstrate that it is localized to the anterior and posterior regions. The hyaluronidase activity of Spaml in acrosome-intact caput sperm was significantly lower (4.3-fold; P < 0.0001) than that of caudal sperm. The increase in enzymatic activity in caudal sperm is accompanied by a reduction in the molecular weight (MW): in extracts from caput sperm there was a major band at approximately 74 kDa and a minor band at approximately 67 kDa; while for the cauda there was a major band at approximately 67 kDa and minor bands at approximately 70 and -56 kDa. Additionally, the bands from caput sperm were 4.9 to 7.7-fold less intense than those from caudal sperm. This decreased affinity for the polyclonal anti-Spaml suggests the presence of different surface characteristics of the molecule from the two epididymal regions. Computer analysis of the protein structure from Spam1 cDNA sequence reveals four putative N-linked glycosylation sites, and enzymatic deglycosylation suggests that all sites are functional. After endoglycosidase activity of extracts from caput and caudal sperm, both show a major band with a MW of approximately 56 kDa, the size of the membrane-anchored polypeptide backbone. Based on the difference in size and intensity of the Spaml bands and hyaluronidase activities from caput and caudal sperm, the data suggest that the activation of Spaml during epididymal maturation is regulated by deglycosylation.

Acrosome↗
PubMed1999

Responses of monkey epididymal sperm of different maturational status to second messengers mediating protein tyrosine phosphorylation, acrosome reaction, and motility.

The maturation of various aspects of sperm function have been demonstrated in monkey and human epididymal sperm, including the ability to undergo the acrosome reaction. The present study aimed to investigate the maturational changes in non-human primate sperm in the signal transduction mechanisms leading to the acrosome reaction involving cyclic AMP, Ca(2+) influx, protein kinase C, and protein tyrosine phosphorylation. Sperm from the caput, corpus, and cauda epididymidis of cynomolgus monkeys were incubated in a complete medium for 2.5 hr, followed by 30 min stimulation with 1 mM dibutyryl cAMP and 1 mM caffeine, 50 microM 1, 2-dioctanoyl-sn-glycerol (DOG), and 50 microM Ca(2+)-ionophore A23187. Quantitative Western blotting revealed little difference in tyrosine phosphorylated proteins among the caput, corpus, and cauda sperm without stimulation. Incubation with cAMP increased the amount of tyrosine phosphorylated proteins up to 10-fold in the corpus and cauda sperm, but to a lower extent in the caput sperm. Ca(2+)-ionophore attenuated the cAMP stimulation but had no effect on its own. Such responses in tyrosine phosphorylated proteins were in great contrast to the responses in the acrosome reaction, where A23187 was the strongest stimulant, resulting in induction of the reaction in 50 +/- 5%, 11 +/- 5%, and 8 +/- 4% cauda, corpus and caput sperm, respectively (mean +/- sem, n = 6). DOG and cAMP in combination induced acrosome reactions in about 10% of viable cells in the cauda and corpus but not caput sperm. Caput sperm responded to cAMP with increases in percentage motility without forward progression whereas cauda sperm displayed marked kinematic changes expected of hyperactivation. Comparisons of responses suggest that the major tyrosine phosphorylated proteins detected are unlikely to be involved immediately in the precipitation of the acrosome reaction, but more related to flagellar motion. Development of signal transduction pathways is part of the epididymal maturational process.

Acrosome Reaction↗
PubMed1983

Response of epididymal duct to the temporary depletion of spermatozoa induced by testicular irradiation in mice.

The mouse epididymal duct can be histologically divided into five segments (I-V), and the principal cells in segment II appear to secrete periodic acid-Schiff (PAS)-positive material into the lumen. In this study, male dd-mice received one, two, or four 800-R doses of radiation beginning at age 50 days. Mice receiving multiple doses were irradiated at 1-week intervals. After irradiation, marked depletion of spermatozoa, or aspermia, occurred in the epididymal duct for 2 to 16 weeks after a latency period of 3 to 4 weeks according to the times of irradiations. During oligospermia or aspermia, PAS-positive inclusions appeared in the principal cells in segment IV. The inclusions occupied a supranuclear position and appeared as round granules and globules measuring 2-15 micron in diameter, and increased in number, size, and staining intensity with time. They disappeared after reappearance of spermatozoa. The findings suggest that PAS-positive material may bind to spermatozoa and, if not bound, is reabsorbed by the principal cells in segment IV and deposited as intracellular inclusions, and the principal cells in segment IV are capable of digesting the accumulated PAS-positive material.

Animals↗
PubMed1991

Interactions between rat epididymal epithelium and spermatozoa.

We studied in the rat epididymis the presence of membrane-bounded vesicles in the stereociliar areas of the epithelial cells. The intimate contact between principal cell stereocilia and luminal spermatozoa was also explored. The epididymidis of adult male albino rats were fixed with Mollenhauer's fixative via the thoracic aorta; they were removed and the caput and the cauda were separated and fixed for 4 additional hours at 4 degrees C. After fixation, the samples were processed with routine techniques for transmission and scanning electron microscopy. The study showed membrane-bounded vesicles in the lumen of the caput and cauda epididymidis. They are present between stereocilia, in the most peripheral regions of the epididymal lumen, and in a stereocilia-free zone in the apical plasma membrane of the principal cells. The smaller vesicles are located near the apical surface of the latter, and the larger ones are located near the tips of the stereocilia. Their contents are electron lucent in some images and electron dense in others. In several thin sections some of the vesicles are observed to have a stalk. This suggests that the possible mode of production may be an exocytotic process. Some membrane-bounded vesicles were found to be in contact with the head or the tail of maturating spermatozoa. Moreover, an intimate contact was found to exist in the epididymidis between the plasma membranes of the spermatozoa and the stereocilia. These observations seem to suggest two possible mechanisms for sperm-epididymal cell relations: 1) release of a secretion product via the membrane-bounded vesicles and 2) direct contact between stereocilia and spermatozoa.

Animals↗
PubMed1992

Evolution of the flagellar waveform of ram spermatozoa in relation to the degree of epididymal maturation.

Motility and flagellar movement of ram spermatozoa along the epididymis were analysed in vitro. From the caput to the cauda of the epididymis, the percentage of motile and progressive spermatozoa increases. No flagellar bending was observed in spermatozoa from the testis or the epididymal anterior caput. When spermatozoa reached the distal caput of the epididymis, a static curvature, associated with an initiation of the flagellar beating, appeared on the flagella. This curvature normally disappeared during epididymal transit. Its disappearance was associated with an increase in the flagellar beat efficiency. Our results suggest that the initiation of motility is related to two mechanisms involving: (1) the presence of a transient static curvature, and (2) the establishment of a symmetric regular beating of the flagellum.

Animals↗
PubMedDate not supplied

Effect of gossypol acetate on guinea pig epididymal spermatozoa in vivo and their susceptibility to capacitation in vitro.

To determine the effects of gossypol acetate on guinea pig epididymal and vas deferens sperm maturity and in vivo susceptibility to in vitro capacitation and the acrosome reaction, we examined spermatozoa removed from 37 animals fed gossypol acetate (10-15 mg/kg/day) for 5 to 9 weeks, and 15 vegetable oil-fed, age-paired control animals. In gossypol-treated, reproductively immature guinea pigs, the number of spermatozoa in the epididymis was markedly reduced (P less than 0.01) compared to controls, whereas the presence of spermatids and spermatocytes increased in the epididymis with the duration of gossypol administration. In sexually mature guinea pigs (given 15 mg/kg/day for 5 weeks), the epididymal sperm survival and forward motility were decreased significantly (P less than 0.025 and P less than 0.01, respectively), although the density of mature spermatozoa was the same as in control animals. The percentage of induced acrosome reactions (26.4 +/- 12%) was almost three-fold lower than that of control animals (72.8 +/- 4.6%). Also, in 31.5 +/- 3.8% of spermatozoa from gossypol-treated animals, as compared to only 2.4 +/- 0.7% of controls, the cytoplasmic droplet failed to migrate to its proper position in the midpiece and was retained in the neck region. With a few exceptions, spermatozoa from both experimental and control groups had comparable patterns of freeze-fractured membrane differentiations. Susceptibility to the induced acrosome reactions and the position of the retained cytoplasmic droplet reversed within 3 weeks after the end of gossypol feeding. This study helps establish the suitability of the guinea pig for studies on gossypol-induced infertility.

Acrosome↗
PubMedDate not supplied

Decreased fertility and motility of spermatozoa from rats immunized with a prealbumin epididymal-specific glycoprotein.

This study investigated the effects on the progressive motility, zona-binding capacity, and fertility of spermatozoa from the cauda epididymidis of adult male rats that were actively immunized against an acidic glycoprotein secreted by the epididymis. The percentage of motile spermatozoa was less than 5% in nine of ten rats that received the epididymal antigen, and 40 to 50% in eight of the 10 control rats. In animals immunized against the antigen, there was a dramatic decrease, but not a complete suppression, in the capacity of epididymal spermatozoa to bind the zona pellucida as compared with the nonimmunized controls. Fertility was decreased two weeks after the end of the treatment, but partial restoration of fertility was observed 6 months later.

Androgen-Binding Protein↗
PubMed1990

Characterization of anti-sticking factor-II from goat epididymal plasma.

A previous study has characterized the major 47 kDa anti-sticking factor (ASF-I) from goat cauda-epididymal plasma (Roy, N., and Majumder, G.C., Biochim. Biophys. Acta, 991:114-122, 1989). This study reports the purification and characterization of ASF-II, another anti-sticking factor from the goat epididymal plasma. ASF-II was purified to apparent homogeneity by using concanavalin A-agarose affinity chromatography, DEAE-cellulose chromatography, alumina gel adsorption, and isoelectric focussing techniques. It showed a single protein band by both non-denaturing and SDS-polyacrylamide gel electrophoresis. ASF-II showed a molecular weight of 36,000 and a sedimentation constant of 2.4S. ASF-II is largely stable to heat treatment and it is a specific glycoprotein having high affinity and specificity for its anti-sticking action. At saturating concentration (1 nM) it inhibited adhesion of nearly 50% of spermatozoa to the glass surface of the haemocytometer counting chamber. Both the protein and sugar parts of the factor are essential for the anti-sticking activity since it lost its activity completely when treated with trypsin, L-fucosidase, or mannosidase. ASF-II does not coat the glass surface and it binds to spermatozoa. Data are consistent with the view that ASF-II has not been derived from the larger ASF-I molecule due to its enzymic modifications. Both ASF-I and -II had no effect on sperm forward motility as evidenced by spectrophotometric motility assays, indicating thereby the suitability of the factors to improve the existing sperm motility assays by eliminating the possibility of cell-sticking artifacts.

Adsorption↗
PubMed1976

Effects of epididymal occlusion on sperm maturation in the hamster.

Hamster epididymal spermatozoa were isolated in the caput, corpus and cauda regions for one, two and three days. Sperm suspensions from these regions were assessed for morphology, motility, viability; and for fertility by A.I. The ability to capacitate was tested by checking for acrosome reactions when the sperm were cultured under defined capacitating conditions at 37 degrees C in vitro. Normal, mature cauda sperm were highly fertile (overall 77% of ova fertilized) and showed 50-80% incidence of acrosome reactions after six hours in culture. Isolation for up to three days had no effect. Immature sperm from the caput and corpus were poorly motile, infertile, and did not manifest an acrosome reaction. Isolation for one and two days produced improvements in motility, and distal migration of the cytoplasmic droplet skin to normal maturation, however the sperm remained infertile and did not capacitate in vitro. Survival after three days isolation was poor. Thus the development of fertilizing ability in hamster epididymal spermatozoa is closely related to the ability to manifest an acrosome reaction in vitro; however it is only poorly correlated with motility and morphology. Completion of sperm maturation in this species appears to require the environment of the cauda epididymidis.

Animals↗
PubMed2003

HE6, a two-subunit heptahelical receptor associated with apical membranes of efferent and epididymal duct epithelia.

Human Epididymis-specific protein 6 [HE6 (GPR64)] is a highly conserved, tissue-specific seven-transmembrane receptor of the human epididymis. The rodent counterparts were cloned and 5'-inverse PCR employed to confirm that the cDNA sequences were full length. Downstream from the highly conserved signal peptide-coding sequence, the 5'-regions contained at least six mini-exons of less than 50 nucleotides. Multiple splice variants involving these mini-exons were cloned in the human, the majority of which was also found in rodents. Northern blot analysis showed that the tissue distribution of the mRNA was very similar in human and rodents. The human HE6 gene was assigned to the X chromosome in a region, which is syntenic to the mouse. The HE6 sequence predicted a two-subunit receptor of the LNB-TM7 subfamily. A membrane preparation and protein solubilization method was adopted to identify the endogenous epididymal proteins. Two sets of peptides were chosen for antibody production, assuming that protein scission had occurred within the conserved GPS-motif. Western blot analysis revealed abundant two-subunit proteins in human and rodents, comprising an approximately 180 kDa hydrophilic ectosubunit and a <40 kDa hydrophobic endosubunit. Deglycosylation experiments showed that the large ectosubunits were highly glycosylated, the carbohydrate side chains dramatically increasing the apparent molecular mass. Immunohistochemical studies revealed that both subunits were associated with apical membranes of efferent ductule and proximal epididymal duct epithelia.

Amino Acid Sequence↗
PubMed1991

Distribution of filipin-sterol complexes in the plasma membrane of stallion spermatozoa during the epididymal maturation process.

The presence and distribution of cholesterol in mature and immature epididymal spermatozoa was analyzed using filipin as a cytochemical tool in freeze-fracture replicas and thin section preparations. The polyenic-antibiotic filipin formed complexes with 3, beta -OH sterols, producing characteristic protrusions, or pits, that were heterogeneously distributed in the plasma membrane of stallion spermatozoa, revealing a specific organization in a functionally specialized area of the gamete. The acrosomal region of the sperm head presented a significantly higher density of filipin sterol complexes than the postacrosomal region, which was usually free of these complexes. The plasma membrane of the flagellum also showed filipin sterol complexes randomly distributed in freeze-fracture replicas. The strong filipin labeling observed in the membrane of spermatozoa obtained from the caput region of the epididymis decreased significantly during epididymal passage. The significance of these changes is not completely understood, but they might contribute to establishing the molecular organization necessary for sperm transit and storage in the epididymis as well as to development of motile spermatozoa that are able to fertilize the oocyte and induce normal embryonic development.

Animals↗