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 1,423 records · Page 79Linked to original sources
PubMed1995

Rat sperm plasma membrane mannosidase: localization and evidence for proteolytic processing during epididymal maturation.

Previous studies from this laboratory have identified a novel alpha-D-mannosidase on the sperm plasma membranes of several species, including man, which may have a role in fertilization. The polyclonal antibody raised against an isoform of the enzyme purified from rat epididymal fluid was found to cross-react with the alpha-D-mannosidase activity present in the detergent-solubilized spermatozoa and sperm plasma membranes. In the present study, we have used affinity-purified as well as monospecific anti-mannosidase IgG to demonstrate that the sperm mannosidase is an integral plasma membrane component of the rat sperm and is localized on the periacrosomal region of the sperm head. In addition, we demonstrate proteolytic processing of the membrane-bound alpha-D-mannosidase during maturation of spermatozoa. The membrane fractions prepared from testis, and spermatozoa from the caput, corpus, and cauda regions of the epididymis, were solubilized in SDS and resolved by SDS-PAGE. The resolved polypeptides, when subjected to Western blot analysis using affinity-purified anti-mannosidase IgG as the primary antibody, revealed the presence of three specific immunoreactive bands (apparent M(r), 135, 125, and 115 kDa) in the membranes from testis, caput, and corpus spermatozoa. However, the cauda sperm plasma membranes showed only one immunoreactive band of apparent M(r) 115 kDa. The disappearance of the 135-and 125-kDa forms and the appearance of a sharp 115-kDa band on cauda spermatozoa suggests a precursor-product relationship between various molecular forms of the enzyme. Trypsin treatment of testicular and caput sperm membranes largely converted the precursor forms to the mature (115-kDa) form. The in vitro proteolysis resulted in an elevated level of the alpha-D-mannosidase activity in the caput (but not cauda) sperm plasma membrane. Inclusion of trypsin inhibitors (benzamidine and aprotinin) largely prevented the conversion of precursor form to the mature form. These data are consistent with the observed increase in the levels of sperm enzyme activity as spermatozoa move from the caput to the cauda region and suggest that the increase is due to the conversion of enzymatically inactive/less active high molecular weight precursor forms (135 and 125 kDa) into enzymatically active mature form (115 kDa) during sperm maturation.

Animals↗
PubMed2000

Zona pellucida protein binding ability of porcine sperm during epididymal maturation and the acrosome reaction.

In many mammals, the first interaction between gametes during fertilization occurs when sperm contact the zona pellucida surrounding the egg. Although porcine sperm first contact the zona pellucida via their plasma membrane, the regions of the sperm surface that display zona receptors have not been determined. We have used the Alexa 488 fluorophore conjugated to solubilized porcine zona pellucida proteins to observe zona receptors on live boar sperm. Zona proteins bound live, acrosome-intact sperm on the anterior portion of the sperm head, concentrated in a thin band over the acrosomal ridge. When sperm membranes were permeabilized by fixation or acrosome reactions induced by the ionophore A23187, zona binding was extended to a broad area covering the entire acrosomal region. Zona binding proteins were present in the acrosomes of sperm from all regions of the epididymis. In contrast, zona binding sites were found on the plasma membrane of most sperm from the corpus and cauda epididymis, but on only 6% of caput epididymal sperm. In conclusion, acrosome-intact boar sperm exhibit concentrated zona protein binding over the acrosomal ridge and acquire this binding in the corpus region of the epididymis, correlating with the developmental stage at which sperm gain the ability to fertilize oocytes.

Acrosome Reaction↗
PubMed1995

Exposure to TCDD during development permanently alters reproductive function in male Long Evans rats and hamsters: reduced ejaculated and epididymal sperm numbers and sex accessory gland weights in offspring with normal androgenic status.

Prenatal administration of relatively low doses of TCDD alters reproductive development and fertility of the progeny. Fertility was reduced in the progeny of Wistar rats exposed to 0.5 micrograms TCDD/kg/day from Gestational Day (GD) 6 to GD 15. In a three-generation reproduction study, TCDD reduced fertility of Sprague-Dawley rats in the F1 and F2 but not the F0 (no developmental exposure) generation at 0.01 microgram/kg/day in the diet. Furthermore, administration of TCDD on GD 15 (at 0.064 to 1 microgram/kg) both demasculinized and feminized morphology and behavior of Holtzman male rat offspring. Our objectives were to expand the observations of Mably et al. (1992, Toxicol, Appl. Pharmacol. 114, 97-107, 108-117, 118-126) on the effects of gestational administration of a single dose of TCDD to another strain of rat and another species, the hamster. In the first study, Long Evans (LE) hooded rats were dosed by gavage with 1 microgram TCDD/kg on GD 8 (during the period of major organogenesis) or GD 15 (the gestational day used by Mably et al.). In the second study, pregnant Syrian hamsters, a species relatively insensitive to the lethal effects of TCDD, were dosed on GD 11, equivalent to GD 15 in the rat, with TCDD at 2 micrograms/kg. When LE rats were dosed on GD 15, or when hamsters were dosed on GD 11, puberty (preputial separation) was delayed by about 3 days, ejaculated sperm counts were reduced by at least 58%, and epididymal sperm storage was reduced by 38%. Testicular sperm production was less affected. The sex accessory glands were also reduced in size in LE rat offspring treated on GD 15 despite the fact that serum testosterone (T), T production by the testis in vitro, and androgen receptor (AR) levels were not reduced. Some reproductive measures, such as anogenital distance and male sex behavior, were altered by TCDD treatment in rat but not hamster offspring. Since T and AR levels appeared normal in the sex accessory glands and the epididymis following perinatal TCDD exposure, the alterations in these tissues are not likely to have resulted from an alteration of the androgenic status of the male offspring.

Aging↗
PubMed1974

Studies on the correlation between androgen binding and activation of rat epididymal tubules in culture.

Rat epididymal tubules maintained in organ culture for 3 or 7 days in media containing androgen showed a marked increase in the incorporation of radioactive amino acids and uridine into acid insoluble material. When the tubules were exposed to these hormones for brief periods, the incorporation of precursors was inhibited initially. In studying the time course of binding of 3H testosterone to the cytoplasmic receptor, a significant amount of radioactivity bound to the receptor was detected only after 12 hr of exposure to the hormone which increased three-fold after 24 hr. The time lag in the binding corresponded closely to the shortest times of observed hormone action wherein a significant increase in the incoporation of uridine (16 hr) and amino acids (24 hr) was produced. Evidence is presented demonstrating that testosterone is bound with high affinity by components of the fetal calf serum present in the culture medium.

Animals↗
PubMed1993

Facilitatory and inhibitory modulation by endogenous adenosine of noradrenaline release in the epididymal portion of rat vas deferens.

The present study aimed at determining the modulation by adenosine of the release of noradrenaline in the epididymal portion of the rat vas deferens. The tissues were treated with pargyline and perifused in the presence of desipramine and yohimbine. Up to four periods of electrical stimulation were applied (5 Hz, 9 min). The A1-adenosine receptor selective agonist R-N6-phenylisopropyladenosine (R-PIA; 100-900 nmol.l-1) reduced, whereas the A2A-receptor selective agonist 2-p-(2-carboxyethyl)phenethylamino-5'-N-ethylcarboxamidoadenosine (CGS 21680; 3-30 nmol.l-1) increased the electrically-evoked noradrenaline overflow in a concentration-dependent manner. The nonselective agonist 5'-N-ethylcarboxamidoadenosine (NECA; 30-300 nmol.l-1) reduced noradrenaline overflow, but the effect did not depend on the concentration. Adenosine deaminase at the concentration of 0.5 mu.ml-1 decreased but at that of 2.0 mu.ml-1 increased noradrenaline overflow. The inhibitors of adenosine uptake, S-(4-nitrobenzyl)-6-thioinosine (NBTI; 50 nmol.l-1) and dipyridamole (3 mumol.l-1), increased the electrically-evoked noradrenaline overflow. The A1-adenosine receptor antagonist 1,3-dipropyl-8-cyclopentylxanthine (DPCPX; 20 nmol.l-1) caused an increase whereas the A2-adenosine receptor antagonist 3,7-dimethyl-1-(2-propynyl)xanthine (DMPX; 0.1 mumol.l-1) caused a decrease. NBTI (50 nmol.l-1), partially antagonized the effect of both DPCPX (20 nmol.l-1) and DMPX (0.1 mumol.l-1).(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine↗
PubMed1983

Scanning electron-microscopical study of epididymal secretions in the lizard Lacerta vivipara (Reptilia, Squamata) and of their relationships with spermatozoa.

During the breeding season (April, May) the epididymis of the lizard Lacerta vivipara produces voluminous secretory granules which are abundantly discharged into the lumen of the duct where they mingle with spermatozoa. The mode of secretion appears quite unusual with respect to the method by which the cells discharge their products, the granules coming out of the cells like bullets out of a gun barrel. Spermatozoa come into close relationships with discharged granules, dipping into their outer layers. This is probably the way in which the heads of spermatozoa become covered with the epididymal soluble protein (protein L). This mode of secretion in Lacerta is discussed with regard to possible artifacts and compared with that encountered in the epididymis of some other species including mammals.

Animals↗
PubMed1976

The effects of testosterone, 5alpha-dihydrotestosterone, 3alpha-androstanediol, and 3beta-androstanediol on the maturation of rabbit epididymal spermatozoa in organ culture.

The fertilizing ability of spermatozoa from epididymal tubules maintained in organ cultures from 1 to 7 days was assessed after artificial insemination into receptive does. It was found that spermatozoa from the distal corpus which were already capable of fertilizing eggs prior to the cultures retain this ability for 1 day without addition of hormone and for 3-4 days when testosterone (0.5 mug/ml) or 5alpha-dihydrotestosterone (0.5 mug/ml) is added to the culture medium. Spermatozoa from the proximal corpus which were not capable of fertilizing eggs prior to the cultures remain so after 1 day in cultures without addition of hormone. Testosterone, 5alpha-dihydrotesterone, 3alpha-androstanediol, or 3beta-androstanediol was added to cultures of proximal corpus at a concentration of 0.5 mug/ml. Only with 5alpha-DHT is the mean percentage of fertilization significantly higher than the percentage obtained without addition of hormone. Insulin does not potentiate the effect of 5alpha-DHT on sperm fertilizing ability. Epithelial growth factor is ineffective. Spermatozoa from the caput epididymidis kept in cultures for 1 to 4 days remain infertile. The results are discussed in light of the morphological findings presented in the preceding communication and in relation to the physiological requirement for sperm maturation in the epididymis.

Androstane-3,17-diol↗
PubMed1987

Filipin-sterol complexes in golden hamster sperm membranes with special reference to epididymal maturation.

The distribution of membrane filipin-sterol complexes (FSCs) was qualitatively surveyed on freeze-fracture replicas of spermatozoa from the male reproductive tract and ejaculates of golden hamster. In the head, the acrosomal plasma membrane showed the strongest filipin labeling on the principal segment, but it was absent in the "quilt-like pattern" areas. These latter were observed in both caput and corpus epididymal spermatozoa, but were absent in mature spermatozoa. The postacrosomal plasma membrane had few FSCs and both the outer and inner acrosomal membranes were always negative to filipin. The nuclear membrane of the principal segment was constantly filipin-positive. The nuclear membrane of the postacrosomal region had more FSCs than that of the principal segment, particularly in mature spermatozoa. Many linear, "rod-like FSCs" were observed on the postacrosomal nuclear membrane of mature spermatozoa, especially in the uterine spermatozoan samples. In the neck, the plasma membrane had only a few FSCs. The redundant nuclear membrane was slightly filipin-positive, while the membrane scroll of mature spermatozoa was heavily labeled. In the tail, the plasma membrane of both the middle and principal piece was moderately labeled.

Animals↗
PubMed1976

Ultrastructural changes in spermatozoa of the brush-tailed possum, Trichosurus vulpecula (Marsupialia), during epididymal transit. Part II: The acrosome.

The acrosome in spermatozoa from the caput epididymidis of the Australian Brush-tailed possum, Trichosurus vulpecula, typically forms a cup-like structure, sitting on the anterior third of the dorsal surface of the nucleus. The base of the acrosomal 'cup' is narrowly separated from the nuclear surface, while the body of the 'cup' projects voluminously away from the nucleus. During epididymal transit these pronounced marginal extensions of the acrosome are retracted towards the nucleus, and the electron dense acrosomal material undergoes a process of compaction within the plasma membrane of the head to produce the convex ovate form of the definitive acrosome. During this process a variety of bizarre forms of the acrosome are produced before its final configuration is attained.

Acrosome↗
PubMed1975

Ultrastructural changes in spermatozoa of the brush-tailed possum, Trichosurus vulpecula (Marsupialia), during epididymal transit. Part I: The flagellum.

During epididymal transit, a fibre network and an array of vesicles develop in the posterior two-thirds of the midpiece in sperm of the Brush-tailed possum, Trichosurus vulpecula. The fibre network is developed by the time the sperm reach the corpus epididymidis, and is composed of evenly spaced, helically arranged fibres lying immediately beneath the plasma membrane. The angle of these fibrous helices is always counter to that of the underlying mitochondrial helix. Separating the fibre network from the mitochondria is a layer of granular material which develops at the same time, and over the same length of the midpiece as the fibre network. A somewhat tenuous fibre network is found between the fibrous sheath and plasma membrane in the anterior principal piece of sperm from all regions of the epididymis. The array of vesicles is developed by the time sperm reach the cauda epididymidis. The vesicles resemble pinocytotic vesicles; some appear as invaginations of the plasma membrane, and are open to the medium surrounding the spermatozoon by a narrow neck, while others are entirely enclosed within the spermatozoon, and lie at varying distances between the plasma membrane and the layer of granular material.

Animals↗
PubMed1989

Immature rat epididymal epithelial cells grown in static primary monolayer culture on permeable supports. I. Vectorial secretion.

A cell culture system is characterized for monolayers of immature rat epididymal epithelial cells grown on permeable supports. Cover of the filters was achieved by days 4-5 and was maintained for 9-12 days. The secretion of acid phosphatase (ACP), alkaline phosphatase (AKP) and N-acetylglucosaminidase (NAG) into apical and basal compartments of culture chambers was monitored with time in culture for cells from the proximal and distal epididymis of 37-day-old animals. There was independent secretion of the three enzymes: secretion of NAG and AKP was mainly apical, that of ACP basal; daily secretion of ACP and AKP was constant throughout culture, that of NAG declined; there was greater secretion of NAG and AKP by cells from the proximal than the distal region. The initial high apical secretion of NAG is thought to reflect loss of enzyme from unattached cells, whereas the later AKP secretion is truly directional. Secretion was not influenced by the enzymes used in cell preparation. The cytotoxic agent Thimerosal inhibited secretion of all enzymes when placed beneath the cultures, indicating that secretion depended on viable cells, but initially stimulated release of AKP when applied above the cells possibly reflecting release from the cell membrane.

Acetylglucosaminidase↗
PubMed1995

Extracellular ATP activates both Ca(2+)- and cAMP-dependent Cl- conductances in rat epididymal cells.

Activation of Ca2+ and cAMP-dependent Cl- conductances by extracellular ATP was studied using the whole-cell patch clamp technique. Immediately after addition of extracellular ATP (10 microM), activation of whole-cell Cl- current exhibiting delayed inactivation and activation kinetics at hyperpolarizing and depolarizing voltages, respectively, was observed. After prolonged activation, the kinetic characteristics of the ATP-induced Cl- current became time- and voltage-independent. When applied to the later phase of the ATP-activated whole-cell current, the disulfonic acid stilbene DIDS (200 microM) could only inhibit 64% of the current while diphenylamine-dicarboxylic acid (DPC, 1 mM) completely inhibited it. Inclusion of a peptide inhibitor for protein kinase A (PKI, 10 nM) in the pipette solution blocked ATP-induced time- and voltage-independent current activation but did not affect the delayed activating and inactivating current activation but did not affect the delayed activating and inactivating current which could be totally blocked by DIDS. Anion selectivity sequence was determined in the presence of either PKI or DIDS and found to be significantly different. Increased pipette EGTA (10 mM) or treatment of the cells with trifluoperazine (40 microM), an inhibitor of calmodulin, suppressed both types of ATP-induced Cl- currents. No current activation by ATP was observed when cells were dialyzed with the IP3 receptor blocker, heparin (10 ng/ml). These results suggest that extracellular ATP activates IP3-linked Ca(2+)-dependent regulatory pathway, which in turn activates cAMP-dependent pathway, leading to activation of both Ca2+ and cAMP-dependent Cl- conductances in epididymal cells.

Adenosine Triphosphate↗
PubMed1980

Anti-insulin receptor antibodies mimic the effects of insulin on the activities of pyruvate dehydrogenase and acetylCoA carboxylase and on specific protein phosphorylation in rat epididymal fat cells.

Previous studies have shown that autoantibodies against insulin receptors found in certain patients with severe insulin resistance stimulate glucose transport and metabolism in fat cell and muscle preparations. The present studies show that preincubation of rat epididymal adipose tissue with 1 : 1000 dilution on one such serum results in a two fold increase in the initial activities of pyruvate dehydrogenase and acetylCoA carboxylase. These increases are similar to the maximum effects of insulin. Incubation of isolated fat cells with the serum at the same concentration also resulted in the increased phosphorylation of three intracellular proteins with subunit molecular weights of 130,000, 35,000 and 22,000 to the same extent as observed with insulin. These findings lend further support to the view that the short term effects of insulin do not involve the entry of the insulin molecule (or part thereof) into cells of target tissues.

Acetyl-CoA Carboxylase↗
PubMed1989

Intracellular pH measurement in primary monolayer cultures of rat epididymal cells.

Intracellular pH (pHi) of primary monolayer cultures of the rat epididymal cells has been measured using fluorescent dye 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein (BCECF). When incubated in normal Krebs-Henseleit (K-H) solution containing 25 mM HCO3, cell monolayers exhibited a basal pHi of 7.17 +/- 0.08. Amiloride (0.5 mM) added to the cell monolayers caused an immediate and sustained fall in pHi by 0.43 +/- 0.05 pH unit. Similar effects were produced when extracellular Na ions were substituted by N-methyl-D-glucamine. Addition of SITS (0.5 mM) or DPC (0.6 mM) resulted in a transient intracellular alkalosis. Adrenaline (0.23 microM) caused a fall in pHi by 0.33 +/- 0.05 pH unit. The fall was slow and was achieved after 30 min (half time 9.9 min). The effect of adrenaline was reversible upon washing and was blocked by propranolol (2 microM). The effect of adrenaline was mimicked by forskolin (10 microM) and Br-cAMP (0.5 mM) which caused a fall in pHi by 0.35 +/- 0.03 and 0.35 +/- 0.02 pH unit respectively. Addition of diphenylamine-2-carboxylate (DPC, 0.6 mM) to the cuvette completely blocked the intracellular acidification produced by adrenaline or forskolin. However, addition of SITS (0.5 mM) did not prevent the intracellular acidosis induced by these agonists. If monolayers were first treated with forskolin (10 microM), the intracellular pH fell, when stabilized, subsequent addition of amiloride caused a further fall in pHi. When incubated in a Cl-free solution (Cl substituted by gluconate), cell monolayers exhibited a pHi of 7.23 +/- 0.07 (values not significantly different from monolayers incubated in HCO3 solution).(ABSTRACT TRUNCATED AT 250 WORDS)

4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfo↗
PubMed1977

Lipolysis and cyclic AMP levels in epididymal adipose tissue of obese-hyperglycaemic mice.

Glycerol release from epididymal fat fragments of young adult (3-month old) ob/ob mice was three times lower than normal, on a tissue weight basis. Dose-response curves in response to isoproterenol and ACTH-(1--24) indicated that the capacity of the lipolytic process was reduced. However, the sensitivity to both hormones was normal, i.e. greater for ACTH than for isoproterenol. The burst of cyclic AMP observed at 7 minutes was affected even more than the lipolytic capacity in adipose tissue from obese mice. This was already observed in 1-month old animals, i.e. at a time when total body weight was still normal. It is concluded that the adenylate cyclase system is defective in adipose tissue of ob/ob mice. Besides, glucagon, vasoactive intestinal polypeptide, and secretin failed to stimulate glycerol release and cyclic AMP accumulation in both ob/ob, ob+/ob+, and HA-ICR mice, suggesting that mouse adipose tissue does not possess receptors for this group of hormones.

Adipose Tissue↗
PubMed1977

Scanning electron microscopic observation of spermiophage cell within the lumen of the epididymal duct of the vasectomized Japanese monkey (Macacus fuscatus).

The spermiophagic process by intraluminal macrophages in the epididymal ducts of the vasectomized Japanese monkey was well visualized with scanning electron microscope. The fragments of disintegrated spermatozoa were seen in the phase enveloped in bulk by flap-like cytoplasmic extensions or in the phase ingested within the cytoplasm.

Animals↗
PubMed1979

Cellularity and composition of epididymal adipose tissue from cold-acclimatized rats.

Cold acclimatization induces morphological and compositional modifications of rat epididymal adipose tissue: a decrease in fat cell size, an increase of fat cell number per g of tissue, but no significant increase in total fat cell number in the tissue; finally, an increase in protein content and a decrease in triglyceride content.

Acclimatization↗
PubMed1981

The effects of sodium and amiloride on the motility of the caudal epididymal spermatozoa of the rat.

The forward motility of the rat caudal epididymal spermatozoa has been studied in different Na+ concentrations. When spermatozoa were suspended in a completely Na+-free solution, the forward motility suffered a progressive fall and after 3 h was completely suppressed. This effect was fully reversible on resuspending the spermatozoa in a solution containing Na+. Amiloride caused a fall in motility and the effect was similar to that of Na+ removal. The inhibition by amiloride of the motility was concentration dependent and the dose response curve showed an IC50-value of about 5 x 10(-5) M. The role of Na+ influx in the maintenance of sperm motility was discussed.

Amiloride↗