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At least 991 records · Page 55Linked to original sources
PubMed1996

Effect of prostaglandin F2 alpha and methylxanthines on enzymic release of bull epididymal spermatozoa in vitro.

The in vitro effect of PGF2 alpha and methylxanthines (theophylline and caffeine) on enzymatic release of bull epididymal spermatozoa was investigated. Epididymal spermatozoa were diluted with egg yolk citrate-based diluent to a concentration of 50 x 10(6) spermatozoa per ml. Aliquots were supplemented with PGF2 alpha at levels of 0, 300, 600 and 1200 micrograms/ml, theophylline or caffeine was added at levels of 0, 500 and 1000 micrograms/ml and incubated at 37 degrees C for 4 h. Spermatozoal motility was decreased with increasing level of PGF2 alpha and the activities of transaminases in the extracellular medium showed a continuous increase. Addition of theophylline or caffeine at both dose levels significantly increased the sperm motility; the activities of transaminases either were not significantly changed or were significantly decreased during the 4 h incubation. These results suggest that supplementation of bull spermatozoa with high levels of PGF2 alpha suppressed motility and induced sperm membrane damage and permeability. However, supplementation of bull spermatozoa with methylxanthines enhanced sperm motility and was not harmful to the integrity of the sperm membrane.

Alanine Transaminase↗
PubMed1987

Spatial and temporal expression of cell surface galactosyltransferase during mouse spermatogenesis and epididymal maturation.

We have previously shown that sperm-egg recognition in the mouse is mediated by the binding of galactosyltransferase (GalTase) on the sperm surface to its appropriate glycoside substrate in the egg zona pellucida [L. C. Lopez, E. M. Bayna, D. Litoff, N. L. Shaper, J. H. Shaper, and B. D. Shur (1985) J. Cell Biol. 101, 1501-1510]. In the present study, we have defined the spatial and temporal expression of surface GalTase during spermatogenesis and epididymal maturation. Purified populations of spermatogenic cells were isolated by unit gravity sedimentation, and surface GalTase expression was determined by indirect immunofluorescence and by direct enzymatic assay. GalTase is present on the surface of all spermatogenic cells assayed. During differentiation, there is a progressive redistribution of GalTase from an initially diffuse and uniform localization on the surface of primary spermatocytes to a restricted plasma membrane domain overlying the dorsal aspect of the mature acrosome. This apparent redistribution of surface GalTase was confirmed by direct enzymatic assays, which show that surface GalTase activity, normalized per cell, remains relatively constant throughout spermatogenesis, despite a drastic reduction in cell surface area. When normalized to the relevant cell surface area, the GalTase concentration per square micrometer increases 77-fold from pachytene spermatocytes to cauda epididymal sperm. Cell surface GalTase is thought to be a cytoskeletally associated transmembrane protein [N. L. Shaper, P. L. Mann, and J. H. Shaper (1985) J. Cell Biochem. 28, 229-239]; consequently we examined whether cytoskeletal components may be involved in the redistribution of GalTase during spermatogenesis. beta-Tubulin, monomeric actin, and filamentous actin were found to be present during spermatogenesis, as assayed by indirect immunofluorescence and by Western immunoblotting. alpha-Actinin and vinculin were not detectable under these conditions and served as negative controls. During spermatogenesis, the distribution of tubulin coincides with the appearance of the mitotic spindle, flagellum, and manchette. On the other hand, the distribution of filamentous actin coincides with surface GalTase, suggesting that actin-containing microfilaments may participate in the redistribution of surface GalTase during spermatogenesis.

Animals↗
PubMed1982

Mechanism and contribution of the pentose phosphate cycle to glucose metabolism in epididymal fat tissue.

1. Glucose 6-phosphate, fructose 6-phosphate and altroheptulose 7-phosphate are the major products formed non-oxidatively from ribose 5-phosphate by rat epididymal fat pad enzymes. 2. Arabinose 5-phosphate was detected among the reaction products and significant activity of the new enzyme of the L-type pentose pathway, D-glycero D-ido octulose 1,8-bisphosphate: D-altroheptulose 7-phosphotransferase was found. 3. The glucose moieties of glucose 1-phosphate, glucose 6-phosphate and glucose 1,6-bisphosphate were degraded and showed that epididymal fat pad enzymes relocate 14C from [2-14C]glucose into C-1, C-2, and C-3 of each hexose-phosphate. 4. The 14C-distribution patterns in the hexose-phosphates revealed that these intermediates were not in isotopic equilibrium and the rate of the transaldolase exchange reaction was relatively small. 5. The 14C-distribution data suggest that glucose 1-phosphate, rather than glucose 6-phosphate, is the first intermediate in the path of glycogen synthesis from glucose in this tissue. 6. The data provide the first proof of the mechanism of the pentose pathway in adipose tissue.

Adipose Tissue↗
PubMed1985

Structural conversion of cytosolic steroid receptors by an age-dependent epididymal protease.

Epididymides from sexually mature rabbits contain a factor that induces a discrete reduction in the sedimentation coefficient of cytosolic estrogen receptors from various tissues (rabbit epididymis and accessory sex organs; rabbit, rat and mouse uterus) and of cytosolic progesterone receptors from the rabbit uterus. The factor is not species-specific since a similar activity was detected in extracts of mature rat epididymides. Although present in cytosol, the factor is obtained in much higher yield in hypertonic extracts of the nucleomyofibrillar fraction of mature rabbit epididymal tissue. Using rabbit uterine estrogen receptor as substrate, we have determined the following details about the rabbit epididymal factor: (1) it is tissue-specific (undetectable in extracts from rabbit accessory sex organs, testis, uterus, liver, lung, kidney and intestine); (2) it is age-dependent (undetectable in extracts from sexually immature rabbit epididymides); (3) its maintenance is testis-independent following its post-pubertal induction or activation; (4) it is primarily localized in the caput region of the epididymis; (5) it is inactivated by elevated temperature; (6) it is macromolecular in nature; (7) it is DNase- and RNase-resistant; (8) it is irreversibly inactivated by leupeptin, indicating that it is a protease; and (9) it is effective on unoccupied and occupied receptors.

Aging↗
PubMed1987

The mechanism of rat epididymal 4-ene steroid 5 alpha-reductase.

Epididymal nuclear 4-ene steroid 5 alpha-reductase catalyses the bisubstrate reaction between testosterone and NADPH to produce 5 alpha-dihydrotestosterone (DHT) and NADP+. Previous studies from this laboratory have demonstrated that the 4-ene steroid 5 alpha-reductase reaction proceeds through the direct transfer of protons from NADPH to testosterone, and that while the product DHT does not affect 4-ene steroid 5 alpha-reductase activity, NADP+ is a potent inhibitor of this enzyme. In the present studies we have investigated the mechanism of 4-ene steroid 5 alpha-reductase with respect to the binding of the substrates, testosterone and NADPH. Kinetic analyses revealed that testosterone does not alter the Kmapp for NADPH, and that NADPH does not alter the Kmapp for testosterone. These findings excluded the possibility that the mechanism of 4-ene steroid 5 alpha-reductase is of the ping-pong variety, and that the sequential addition of both substrates is required before any products are released. The lack of change in Kmapp, observed for either substrate, further suggests that both testosterone and NADPH are able to bind to the free enzyme, negating the possibility that substrate addition occurs in an ordered manner. Indeed the kinetic profiles are entirely consistent with the mechanism of 4-ene steroid 5 alpha-reductase being a rapid equilibrium random sequential process in which the binding of the first substrate has no affect on the binding of the second. Mean values for the dissociation constants, Ktestosterone and KNADPH, were 200 nmol/l and 50 nmol/l, respectively. These findings, coupled with those from earlier studies, suggest that the mechanism of epididymal nuclear 4-ene steroid 5 alpha-reductase is a rapid equilibrium random bireactant process, with the possible dead-end complex: testosterone-4-ene steroid 5 alpha-reductase-NADP+.

Animals↗
PubMed1985

The effect of Synacthen administration on lipoprotein lipase activity in the epididymal fat pad of the rat.

Conflicting data have been reported on the influence of (excess) glucocorticoids on lipoprotein lipase (LPL) activity in adipose tissue. To solve this problem hypercorticism was induced in rats by treatment for varying periods with Synacthen, a synthetic corticotrophin-1-24 preparation, and LPL was measured in the epididymal fat pads using different methods. In extracts of defatted tissue preparations from overnight fasted rats treated for 3 days with Synacthen we observed an increase in LPL activity (acetone-ether powder LPL) to values similar to those found in normally fed controls. In contrast, the heparin-elutable part of LPL activity in the tissue was not influenced by the Synacthen treatment. This activity remained significantly lower in overnight fasted animals, Synacthen treated or not, than in normally fed rats. Adrenalectomy lowered the acetone-ether powder LPL activity of the epididymal adipose tissue in fasted as well as in fed rats. In fasted rats it prevented the stimulation of the LPL activity by Synacthen.

Adipose Tissue↗
PubMed1987

Regional differences in the replication rate of cultured rat microvascular endothelium from retroperitoneal and epididymal fat pads.

Study of the vascular endothelium has been greatly facilitated by the development of specific cell culture systems isolated from various tissues. We report herein a simple method for establishing a propagating cell culture system of microvascular endothelial cells derived from rat adipose tissue. In addition to the characteristic cobblestone appearance on light microscopy, the microvascular endothelial cells in culture also demonstrated the presence of other markers for large vessel endothelia. Electron microscopy revealed endothelium-specific Weibel-Palade bodies and abundant pinocytotic vesicles. Both retroperitoneal and epididymal endothelia demonstrated the presence of factor VIII antigen by immunofluorescent staining and prostacyclin production. Although there was no appreciable morphological difference between cultured retroperitoneal and epididymal microvascular endothelia, the replication rate of the former was significantly higher than that of the latter (P less than .05). Excessive replication of endothelial cells may play a role in the regional differences of adipose tissue mass in an organism.

Adipose Tissue↗
PubMed1987

Effects of synacthen on lipid metabolism in the perfused epididymal fat pad of the rat.

Rats were treated with Synacthen, a synthetic corticotrophin analogue, to induce hypercorticism. The epididymal fat pad was selectively cannulated and perfused. In fasted rats acetone ether powder lipoprotein lipase (LPL) activity rose during treatment to levels found in fed controls. In fed animals no further rise in LPL activity was observed during Synacthen treatment. However, the heparin-elutable LPL activity did not change during this treatment in fasted nor fed animals. Pharmacologic levels of insulin in the perfusion medium caused an increase in heparin-releasable LPL activity as a percentage of total fat pad LPL activity (15% v 48%). Hydrolysis of chylomicrons was higher in fasted three days treated animals then in controls (10 +/- 4% v 2 +/- 2%). In this group a higher uptake of liberated free fatty acids was found (2.6 +/- 1.5% v 1.0 +/- 0.5% in controls). The increase in hydrolysis rate and uptake of fatty acids in the treated fasted animals could not be explained by an increase in releasable LPL activity. Fatty acid release from the fat pad was lower in treated animals than in controls (fasted and fed), basally as well as after adrenalin stimulation. The observation that the epididymal fat pad retains its weight during hypercorticism may therefore be ascribed to an increased influx of fatty acids from increased hydrolysis of TG-rich particles and to an inhibited efflux of fatty acids from the adipocyte. The discrepancy between the LPL activity extractable from an acetone ether powder and the heparin releasable LPL activity suggests impairment of the transport of LPL from the adipocyte to the heparin releasable pool at the endothelium.

Adipose Tissue↗
PubMed1993

Identification and characterization of angiotensin II receptors in rat epididymal adipocyte membranes.

To better understand the role of the mitogenic vasoactive peptide angiotensin II (AII) in growth and differentiation, we have investigated the existence of membrane receptors for this peptide in rat adipocytes. Following isolation of epididymal fat cells, membrane protein was removed and incubated with varying concentrations of 125I-AII with or without submicromolar concentrations of unlabeled AII. Binding of AII was highly specific, rapid, and reversible. Scatchard analysis indicated that adipocyte membranes contain a high-affinity AII receptor with a Kd of 0.90 nmol/L and a binding site concentration (Bmax) of 53.7 fmol/mg protein. Additional pharmacologic analyses resulted in a rank order potency for peptide agonists and antagonists similar to that reported for the vascular receptor. Determination of subtype specificity with selective organic compounds indicated that the epididymal adipocyte receptor was displaced at low concentrations of DuP753, a selective AT1 subtype antagonist. These studies have successfully identified and characterized a high-affinity membrane receptor for AII in fat cells, further establishing adipose tissue as a peripheral site containing regulatory components of the local renin-angiotensin system.

1-Sarcosine-8-Isoleucine Angiotensin II↗
PubMed1977

Partial characterization of epididymal 5 alpha reductase in the rat.

Epididymal 5alpha reductase activity was found distitributed in the crude nuclear fraction (44 percent) and microsomal fraction (41 percent). Spermatozoa contaminating the nuclear preparation accounted for only 3 percent of its activity. There were no regional differences in the distribution of total 5alpha reductase activity. However, the nuclear enzyme was more active in caput than in other regions. Maximal activity was found at pH 6.2 and at 32 degrees C. Both enzymes had an absolute requirement of reduced dinucleotides. The microsomal preparation could only us NADPH while the nuclear enzyme could use NADPH and NADH. The apparent Km for the microsomal preparation was 0.62 +/- 0.05 X 10(-6)M and Vmax was 555 +/- 38 pmoles/mg protein/hour. The nuclear enzyme presented similar values. The reaction was not inhibited by accumulation of product in the medium, but other steroids such as progesterone, epitestosterone (17alpha-hydroxy-4-androsten-3-one) and 3-oxo-4-androstene-17beta-carboxylic acid were potent competitive inhibitors. The reaction was strongly inhibited by Hg, Zn and Cu. The properties of the epididymal reductase are similar to those of the prostatic enzyme.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗
PubMed1990

The effect of submandibular gland removal on testicular and epididymal parameters.

The effect of sialoadenectomy (submandibular gland removal) for four weeks duration was studied in five C3H mice and four sham-operated controls. This preliminary experiment using small numbers of animals indicated that sperm production parameters were lowered in sialoadenectomized animals although there were no significant differences between the sialodenectomized and sham-operated group. In a second experiment using larger numbers of animals, significant differences in testicular weights, epididymal weights, and testis weights were noted. These parameters were reduced only 10-14% from control levels. Epididymal sperm head counts were reduced 10% after sialoadenectomy but the two groups were not significantly different (P less than 0.05). No difference in testicular histology was observed. The present report contrasts to that of Tsutsumi et al. (1986) who indicate that submandibular removal with subsequent depletion of epidermal growth factor (EGF), is extremely deleterious (40-55% decreases in spermatid and sperm content) to the progress spermatogenesis.

Animals↗
PubMed1990

Immunoelectron microscopic distribution of actin in hamster spermatids and epididymal, capacitated and acrosome-reacted spermatozoa.

The distribution of actin in hamster sperm cells was studied during spermiogenesis, epididymal transit, in vitro capacitation and acrosome reaction by immunogold procedures using a polyclonal and two monoclonal antiactin antibodies. A predominant actin labeling (F-actin) was detected in the subacrosomal space of spermatids. Actin labeling was also observed under the plasma membrane of intercellular bridges and along the outer acrosomal membrane. In late spermatids there was both F-actin depolymerization and a loss of actin immunolabeling, thus suggesting a dispersion of G-actin monomers. No obvious labeling was evidenced in residual bodies. This pattern was observed with the three antiactin probes. In contrast, an actin labeling reappeared over the fibrous sheath of the flagellum in epididymal spermatozoa but only when the polyclonal antibody was used. Only one single actin reactive band was detected by immunoblotting of sperm extracts. Since the sperm tails were NBD phallacidin negative they were considered to contain either G-actin or actin oligomers rather than bundles of actin filaments. It is suggested that G-actin originating in the head of late spermatids was redistributed to the flagellum of epidymal spermatozoa. No further changes were noted after capacitation and acrosome reaction thus indicating no apparent effect on actin polymerization and distribution.

Acrosome↗
PubMed1992

Ectopic aberrant adrenals with epididymal abnormality.

We report a rare case of ectopic aberrant adrenals associated with epididymal abnormality found during exploration for a left undescended testis. Two ectopic adrenals were found, one on the epididymis and the other adjacent to the spermatic cord. We believe the simultaneous occurrence of epididymal abnormality and ectopic aberrant adrenals has not been reported before.

Adrenal Glands↗
PubMed1979

The effect of scrotal insulation on spermatozoal morphology and the rates of spermatogenesis and epididymal passage of spermatozoa in the bull.

In five beef bulls spermatogenic cells labelled with (3)H-thymidine were used to estimate the duration of one cycle of the seminiferous epithelium (S.E.) and epididymal passage (E.P.) of spermatozoa after 10 or 20 hr of scrotal insulation designed to increase testicular temperature. From six autoradiographic estimates in three bulls, the mean value for 1 S.E. cycle was 13.4 days (range 12.9 to 13.6 days). Two estimates of E.P. were both 13.5 days. Scrotal insulation altered both semen quality (lowered percentage live and motile spermatozoa, raised percentage abnormal spermatozoa and lowered concentration per ml spermatozoa) and the histological appearance of the seminiferous epithelium. However, the rate of spermatogenesis and epididymal transport was unchanged.

Journal Article↗
PubMed1992

Identification of an abundant monkey epididymal transcript encoding a homologue of human CAMPATH-1 antigen precursor.

A number of cDNA clones encoding a small (0.5-0.6 kb) transcript have been isolated from a monkey (Macaca fascicularis) epididymal cDNA library. DNA sequence analysis indicates that this abundant epididymal transcript is homologous to the human CAMPATH-1 (CDw52) antigen precursor, a GPI-anchored membrane glycoprotein previously described on lymphocytes and monocytes.

Amino Acid Sequence↗
PubMed1985

Effects of ethylene glycol monomethyl ether (EGME) on mating performance and epididymal sperm parameters in F344 rats.

Previous histologic studies on the effects of EGME identified dividing spermatocytes as a primary target cell type in the testis. The following studies were undertaken to assess possible effects of EGME on late-stage and epididymal spermatids, and spermatogonia. Adult male F344 rats (n = 20/group) of proven fertility were dosed po with 0, 50, 100, or 200 mg EGME/kg/day for 5 days. Each male was then mated with two females/week for 8 weeks. Females were sacrificed ca. 2 weeks after removal from the male, and number of live and dead fetuses, resorption sites, and corpora lutea were noted. Additional males were treated similarly, sacrificed at weekly intervals, and measures of epididymal sperm count, motility, and morphology were made. The fertility of males treated with 200 mg EGME/kg declined at Week 4, and remained low for the rest of the study. There was a modest but significant increase in the number of resorption sites at Weeks 5 and 6 in the high dose group. There was a decrease in the number of litters sired at Week 5 after dosing in the 100-mg EGME/kg group. There were time- and dose-related decreases in sperm concentration and motility, primarily in the 100- and 200-mg/kg groups, as well as concurrent elevations in the number of abnormal sperm forms in the epididymis. These studies show that EGME is a very weak inducer of dominant-lethal mutations, and produces previously undescribed effects on late-stage spermatids and spermatogonia.

Animals↗
PubMed1985

Comparison of basal metabolic activities and hormonal sensitivities between mesenteric and epididymal adipocytes.

The mesenteric adipose tissue, which is present in a considerable amount in the rat but had not been used for the experiments, contained a larger number of adipocytes than the epididymal adipose tissue per wet weight of the tissue. The basal metabolic activities and the responses to epinephrine and insulin in the mesenteric adipocytes were essentially equal to those in the epididymal adipocytes. The mesenteric adipocytes are useful for elucidation of metabolism in white adipose tissue.

Adipose Tissue↗
PubMed1979

Isolation and characterization of specific rat epididymal proteins.

The partial purification and characterization of specific rat epididymal proteins (SEP) is reported. Starting from the cytosol fraction obtained from epididymal homogenates, protein C was purified 15-fold and proteins D--E were purified 19-fold. The molecular weight, determined by molecular sieving, of protein C was 22,400 while that of D--E was 37,000. These proteins stained as glycoproteins with periodic acid--Schiff reagent. The isoelectric point of protein D was 5.13 while that of protein E was 4.95. Protein C separated into 3 bands during isoelectric focussing. The major component focussed at 5.56 and the two minor components at pH 5.38 And 5.79. Using a specific antiserum we could confirm the organ specificity of SEP and their androgen-dependence.

Animals↗