Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Following the administration of 3-H-testosterone to adult male rats radioactivity appeared in epididymal fluid and at 60 minutes was in excess of the level in tissue of the cauda epididymidis and blood plasma. Ligation of the arterial blood supply to this region caused a significant decline in the radioactive content of epididymal fluid and cauda tissue. It is concluded that direct transfer occurs from the systemic circulation into the cells of the cauda epididymidis and thence into the lumen of the duct. The major radiometabolite of 3-H-testosterone identified in chloroform extracts of epididymal tissue (60.6%) and epididymal fluid (72.8%) was 17-beta-hydroxy-5-alpha-androstan-3-one.
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PMID:The presence of metabolites of 3-H-testosterone in the lumen of the cauda epididymidis of the rat. 114 77

Crude chloroform extract of C. papaya seeds (5 mg/animal/day, po, for 20, 40 and 60 days) was investigated for contraceptive efficacy and related side effects in male albino rats. The crude extract reduced fertility to zero per cent by 40 to 60 days of treatment. Suppression of cauda epididymal sperm motility was the most pronounced effect of the drug administration. Scanning electron microscopic observations revealed treatment induced abnormalities in sperms. Cauda epididymal and testicular sperm counts decreased following treatment. Clinical parameters did not show any alterations. Results suggest that the contraceptive effects of chloroform extract of papaya seeds are mainly post-testicular in nature without influencing toxicological profile and libido of the animals.
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PMID:Antifertility investigations on the crude chloroform extract of Carica papaya Linn. seeds in male albino rats. 129 29

5-Br-4-Cl-3-Indoxyl-alpha-D-gluco(pyrano)side was found to be the most suitable synthetic substrate for the demonstration of alpha-D-glucosidases in situ. Using an azoindoxyl procedure with hexazotized pararosaniline or new fuchsine at pH 5 in freeze-dried celloidine-mounted cryostat sections acid alpha-D-glucosidase (EC 3.2.1.20) was shown for the first time in lysosomes of many cells of fetal and adult rat, mouse, guinea-pig, marmoset and human organs. At pH 6.5, in chloroform-acetone pretreated cryostat sections plasma membrane alpha-D-glucosidases were shown in the brush border of enterocytes of the small and large intestine, in the brush border of proximal renal tubule cells and in the stereocilia of the epididymal duct. In an indigogenic procedure with ferricyanide/ferrocyanide as redox catalysator plasma membrane alpha-D-glucosidases were depicted as well as with the azo-indoxyl method; the demonstration of the acid alpha-D-glucosidase was inferior to that achieved with the azo-indoxyl procedure. Using tetrazolium salts as capture reagent intracellular localization was unsatisfactory. In enterocytes, a localization in the Golgi apparatus was shown by the azo-indoxyl procedure only. Analytical isoelectric focusing revealed organ-dependent differences of plasma membrane and lysosomal alpha-D-glucosidases. Compared with the already existing methods the azo-indoxyl and indigogenic procedures are by far the most suitable techniques.
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PMID:Histochemical detection of alpha-D-glucosidases and their molecular forms with 5-Br-4-Cl-3-indoxyl-alpha-D-glucoside. 310 70

New lanthanide methods for the histochemical detection of non-specific alkaline phosphatase in the light microscope are described and compared with already existing techniques for the light microscopical demonstration of this enzyme. To avoid formation of insoluble lanthanide hydroxide at alkaline pH citrate complexes with the capture ions cerium, lanthanum and didymium were used. A molar ratio of 11 mM citrate/14 mM capture reagent is proposed. For preincubated sections, pretreatment in chloroform-acetone and fixation in glutaraldehyde, for non-preincubated sections fixation in glutaraldehyde yielded the best results. 4-Methylumbelliferyl and 5-Br-4-Cl-3-indoxyl phosphate were found to be the most suitable substrates. For routine purposes 4-nitrophenyl, 1-naphthyl, 2-naphthyl and 2-glycerophosphate were also sufficient; naphthol AS phosphates were inferior but still suitable. After incubation for 5-60 min at 37 degrees C lanthanide phosphate was converted into lead phosphate which was visualized as lead sulfide. At pH 9.2-9.5 enzyme activity was demonstrated at many sites such as intestinal, uterine, placental, renal and epididymal microvillous zones, plasma membranes of arterial, sinus and capillary endothelial cells, vaginal and urethral epithelium, smooth muscle cells, myoepithelial cells as well as excretory duct cells of salivary and lacrimal glands and in secretory granules of laryngeal glands. In comparison with Gomori's calcium, Mayahara's lead, Burstone's and Pearse's azo-coupling, McGadey's tetrazolium salt and Gossrau's azoindoxyl coupling technique the lanthanide methods detected alkaline phosphatase activities at identical or additional sites depending on the respective procedure.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Light-microscopic histochemistry of non-specific alkaline phosphatase using lanthanide-citrate complexes. 323 44

The authors studied anesthetic mutagenesis following exposure in vivo by use of an adaptation of the mouse spermatozoa morphology assay of Wyrobek and Bruce. The epididymal spermatozoa of (C57B1/C3H)F1 mice were examined for morphologic abnormalities following exposure to near-0.1 MAC and greater concentrations of general anesthetics. Twenty exposure hours (4 hr/day x 5 days) were conducted for nitrous oxide, diethyl ether, chloroform, trichlorethylene, halothane, methoxyflurane, enflurane, and isoflurane, each at two concentrations. Twenty-eight days after exposure, epididymal spermatozoa were examined. Statistically significant increases in the percentages of abnormal spermatozoa were found for chloroform, trichloroethylene, and enflurane, compared with controls. These data suggest that direct examination of reproductive cells following exposure to general anesthetics in vivo may be useful in the investigation of the genetic toxicities of these compounds.
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PMID:Morphologic changes in mouse spermatozoa after exposure to inhalational anesthetics during early spermatogenesis. 610 70

The ejaculated porcine spermatozoa were fractionated into the cytosol, membrane, midpiece plus tail (flagella) and head fractions, and their adenylate cyclase activities were measured. About 65% of the total activity was located in the flagella fraction. For all the fractions, Mn2+-dependent adenylate cyclase activity was about 20 times higher than Mg2+-dependent activity, and guanine nucleotides, fluoride, and other reagents tested did not activate adenylate cyclase. The results suggest that the GTP-dependent regulatory subunit is absent in porcine spermatozoa. The porcine seminal plasma was found to stimulate the adenylate cyclase activity in spermatozoa. The stimulating factor in porcine seminal plasma was partially purified by gel filtration and the molecular weight of the factor appeared to be between 200 and 300. The partially purified factor is heat stable and is not inactivated by treatment with Pronase, trypsin, phospholipase A2 or D but is inactivated by acid hydrolysis. It is easily soluble in water, partially soluble in methanol, and insoluble in ethanol, ethyl ether, chloroform, or acetone. The activation of sperm adenylate cyclase by the factor occurred without a time lag. The activating effect was dose-dependent, saturated at high dose, and ascribed to the increase of the maximal velocity (Vmax). The effect of the factor appears to be limited to adenylate cyclase in spermatozoa; the factor activated adenylate cyclase both in porcine and bovine spermatozoa but failed to activate those in other porcine tissues. The factor was shown to activate the enzyme not only in the ejaculated spermatozoa but also in the epididymal sperm. The factor was also found to elevate the cAMP level in the intact porcine spermatozoa. The factor enhanced the motility of corpus and cauda epididymal spermatozoa. These findings indicate the possibility that this factor initiates the spermatozoan motility upon ejaculation through directly activating adenylate cyclase.
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PMID:Activation of spermatozoan adenylate cyclase by a low molecular weight factor in porcine seminal plasma. 663 Feb 19

A Mr = 32,000 membrane glycoprotein can be uniquely labeled by galactose oxidase/[3H]sodium borohydride on rat caudal, but not caput, epididymal sperm. It has been suggested that this protein is related to a Mr = 32,000 galactose oxidase-sensitive glycoprotein present in rat caudal epididymal fluid. The tritiated membrane glycoprotein was solubilized and its hydrodynamic properties were determined by conventional gel filtration, high performance gel filtration, sedimentation rate determination in linear sucrose gradients prepared in H2O and D2O, and equilibrium isopycnic centrifugations in CsCl. The Stokes radius and sedimentation coefficient were 4.87 +/- 0.07 nm and 1.73 +/- 0.08 S, respectively. The sedimentation profile in CsCl gradients was asymmetric with a major peak occurring at a density of 1.081 g/cm3 (v = 0.92 cm3/g) and a shoulder at 1.108 g/cm3 (v = 0.90 cm3/g). The glycoprotein did not enter a 5 to 20% linear sucrose gradient prepared in D2O and could be extracted from the intact sperm into acidic chloroform:methanol solutions. These data are consistent with a protein which binds substantial amounts of detergent and/or lipid and has exposed hydrophobic regions. Two-dimensional gel electrophoresis indicated that the membrane protein exhibits charge heterogeneity, with the major components having pI values of 5.4 and 4.9. The fluid glycoprotein was monodisperse on two-dimensional gel electrophoresis having a pI of 3.8. Binding studies failed to demonstrate specific binding of the Mr = 32,000 caudal fluid glycoprotein to caput cells. Moreover, "Western blots" of electrophoretically resolved caput and caudal fluid proteins, followed by immunolabeling with antibodies raised against unfractionated caudal fluid, demonstrated the presence of a Mr = 32,000 protein in caudal fluid which was absent from caput epididymal fluid. Using the same technique, it was shown that antibodies raised against caudal fluid proteins did not cross-react with a Mr = 32,000 caudal membrane glycoprotein. Our data do not support the view that the Mr = 32,000 fluid and membrane proteins are identical.
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PMID:Characterization of a maturation-associated glycoprotein on the plasma membrane of rat caudal epididymal sperm. 669 99

The present report describes in vitro experiments with golden hamster sperm designed to determine whether there is any relationship between sperm phospholipid methylation and capacitation and/or the acrosome reaction. Washed cauda epididymal hamster sperm were incubated in a capacitation medium containing [methyl-3H] methionine. After 0.5, 1.5, 2.5 and 3.5 h of incubation, sperm were extracted with a chloroform:methanol:2 N HCl mixture to extract total phospholipids. Liquid scintillation counting revealed that the methyl-3H-group was incorporated into phospholipids with maximum incorporation at 3.5 h and an increase of 50% between 2.5 and 3.5 h. Uptake of labeled methionine by sperm reached its plateau by 1.5 h of incubation. Some sperm were capacitated by 3.5 h because that is the time at which the rate of acrosome reactions began to increase and because at least 50% of them were able to undergo the acrosome reaction 10 min after the addition of the fusogen lysophophatidylcholine (LPC) at 3.5 h but not at 2.5 h. Homocysteine thiolactone and 3-deazadenosine, inhibitors of transmethylation, inhibited incorporation of methyl-3H into phospholipids at 3.5 h by approximately 90% and also inhibited LPC-induced acrosome reactions by 60%. Separation of methylated sperm phospholipid by thin-layer chromatography demonstrated the presence of 3H-labeled phosphatidyl-N-monomethylethanolamine, phosphatidyl-N,N-dimethylethanolamine, and to a lesser extent phosphatidylcholine. In addition, an unidentified lipid was also highly labeled. These results strongly suggest a positive correlation between phospholipid methylation and capacitation and/or the acrosome reaction of hamster sperm in vitro. Possible mechanisms for phospholipid methylation involvement in these events are discussed.
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PMID:Phospholipid methylation increases during capacitation of golden hamster sperm in vitro. 687 7

Autoantibodies raised in guinea pigs (GP) by hyperimmunization with epididymal sperm recognize antigens present on the plasma membrane of intact sperm and antigens associated with acrosome-reacted sperm. Plasma membrane autoantigens were characterized by SDS-PAGE analysis of immune precipitates from detergent extracts of radiolabeled epididymal sperm. Three major protein bands with approximate molecular weights (MW) of 69,000, 62,000 and 40,000 daltons were exhibited. Galactose oxidase and periodate oxidation followed by tritiation revealed two major plasma membrane glycoprotein autoantigens with MWs of 35,000 and 32,000 daltons and one sialoglycoprotein of 34,000 daltons. Antigenic molecules of similar MW were also detected by autoantisera to guinea pig testicular homogenates. Immune precipitates of radiolabeled detergent extracts of acrosome-reacted sperm analyzed by SDS-PAGE exhibited two major carbohydrate-containing peaks, one with a MW of approximately 42,000 daltons and one of 6,000 daltons. Since the 6,000 dalton peak was immunoprecipitated from the organic phase of both chloroform:methanol 2:1 and n-butanol extracts, the antigen may be a glycolipid. The possible existence of glycolipid autoantigen in GP sperm was further supported by the reaction in a solid phase radioimmunoassay of autoantibodies to GP sperm with glycolipid extracts from GP testis. This study demonstrates the presence of multiple autoantigenic specificities in the sperm-plasma membrane, acrosome-reacted sperm and testis of guinea pigs. It also demonstrates for the first time glycolipid autoantigens in testis and sperm.
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PMID:Immunochemical analysis of guinea pig sperm autoantigens. 703 3

In protein-deficient minimal culture medium, acrosome reactions of motile guinea-pig spermatozoa were first evident after 30 min and maximal by 2 h. Addition of 5% (v/v) of guinea-pig serum filtrate or human plasma filtrate, obtained by passing these fluids through an Amicon UM-2 ultrafiltration membrane, prevented the sperm acrosome reaction during a 4-h incubation, but did not inhibit sperm motility. A similar inhibitory effect was found in porcine epididymal fluid. The factor(s) in porcine epididymal fluid effectively inhibited acrosome reactions if it was added to uncapacitated spermatozoa but failed to decapacitate sperm cells capacitated in Ca2+-free medium. Preliminary characterization of the factor(s) in porcine epididymal fluid indicate that it is a small organic molecule, stable to heat (90 degrees C), soluble in methanol, sparingly soluble in ethanol and insoluble in ether, chloroform or acetone; it also appears to have no net charge at pH values between 4 and 10.
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PMID:Inhibition of the guinea-pig sperm acrosome reaction by a low molecular weight factor(s) in epididymal fluid and serum. 705 91


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