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)

Nitric oxide gas (NO) increased guanylate cyclase [GTP pyrophosphate-lyase (cyclizing), EC 4.6.1.2] activity in soluble and particulate preparations from various tissues. The effect was dose-dependent and was observed with all tissue preparations examined. The extent of activation was variable among different tissue preparations and was greatest (19- to 33-fold) with supernatant fractions of homogenates from liver, lung, tracheal smooth muscle, heart, kidney, cerebral cortex, and cerebellum. Smaller effects (5- to 14-fold) were observed with supernatant fractions from skeletal muscle, spleen, intestinal muscle, adrenal, and epididymal fat. Activation was also observed with partially purified preparations of guanylate cyclase. Activation of rat liver supernatant preparations was augmented slightly with reducing agents, decreased with some oxidizing agents, and greater in a nitrogen than in an oxygen atmosphere. After activation with NO, guanylate cyclase activity decreased with a half-life of 3-4 at 4 degrees but re-exposure to NO resulted in reactivation of preparations. Sodium azide, sodium nitrite, hydroxylamine, and sodium nitroprusside also increased guanylate cyclase activity as reported previously. NO alone and in combination with these agents produced approximately the same degree of maximal activation, suggesting that all of these agents act through a similar mechanism. NO also increased the accumulation of cyclic GMP but not cyclic AMP in incubations of minces from various rat tissues. We propose that various nitro compounds and those capable of forming NO in incubations activate guanylate cyclase through a similar but undefined mechanism. These effects may explain the high activities of guanylate cyclase in certain tissues (e.g., lung and intestinal mucosa) that are exposed to environmental nitro compounds.
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PMID:Nitric oxide activates guanylate cyclase and increases guanosine 3':5'-cyclic monophosphate levels in various tissue preparations. 2 Jun 23

As it was shown previoulsy by others, the membrane-bound phosphodiesterase (cyclic adenosine 3':5'-monophosphate phosphodiesterase) of rat epididymal fat cells was stimulated when intact cells were exposed to insulin. The levels of stimulation observed in the present study in the cell homogenate and microsomal fraction were approximately 2.0- to 2.5-fold and 2.5- to 3.0-fold, respectively, when the initial substrate level was 100 nM and insulin concentration was 1 to 3 nM. When the microsomal fraction was subjected to a sucrose density gradient centrifugation, most of the insulin-sensitive phosphodiesterase activity was fractionated into the "light" microsomal fraction which was rich in NADH2:potassium ferricyanide:oxidoreductase) and low in 5'-AMPase, adenylate cyclase, and insulin-binding activities. The latter three activities were mostly fractionated into the "heavy" microsomal fraction. Both basal and insulin-stimulated phosphodiesterase activities were low when cells were homogenized in the presence of N-ethylmaleimide or p-chloromercuribenzoate. The insulin-stimulated enzyme activity was also low when cells were homogenized in the presence of --SH compounds (e.g. dithiothreitol) or certain metal-chelating agents (e.g. ethylene glycol bis(beta-aminoethyl ehter)-N,N'-tetraacetate (EGTA)), or in a nitrogen atmosphere. The effect of EGTA was prevented by the addition of certain heavy metal ions but not by the addition of Ca2+ or Ca2+ plus Mg2+ ions. When cells were homogenized in the presence of certain oxidants (e.g. diamide, sodium tetrathionate, or air), a high plus-insulin activity was observed; this activity was not lowered by subsequent treatment of the enzyme with N-ethylmaleimede, EGTA, or fresh cell homogenate that was prepared in the presence of EGTA. However, the activity of an apparently oxidized enzyme could still be lowered by treatment woth dithiothreitol. A partially purified enzyme in the enzyme in the microsomal fraction was fairly stable both in basal and insulin-stimulated states (fully active after 35 days when kept at -20degrees). EGTA added to the homogenization buffer lowered the basal phosphodiesterase activity, but this effect was reversed by the addition of Ca2+ ions. EGTA also decreased the enzyme activity that was stimulated by norepinephrine. However, neither EGTA nor dithiothreitol had any effect on the activities of 5'-AMPase, NADH-dehydrogenase, and malate dehydrogenase of fat cells. The above data indicate that most of the insulin-sensitive phosphodiesterase and the so-called "cell membrane markers" are associated with different subcellular particles in the cell homogenate. In addition, the data seem to indicate that the insulin-stimulated phosphodiesterase has certain --SH groups and that the activity of the enzyme is stabilized when the --SH groups are oxidized by certain oxidants including molecular oxygen. It is suggested that the air oxidation of the enzyme is catalyzed by a trace of certain heavy metal ions and, therefore, can be blocked by a metal-chelating agent.
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PMID:Insulin-sensitive phosphodiesterase. Its localization, hormonal stimulation, and oxidative stabilization. 17 Feb 71

Protein changes in epididymal and ejaculated spermatozoa were studied in bulls treated orally on alternate days with a total of 10 doses (each of 4 mg/kg body weight) of ethylene dibromide. No significant changes were found in the total nitrogen, amino acid or lipoprotein contents of the spermatozoa collected either from the epididymis 1 day after the last dose, or from ejaculates 9-13 days after the end of the treatment. Significant changes were found in the percentage composition of amino acids of the sperm proteins and lipoproteins but the changes differed in the caput, cauda and ejaculated spermatozoa.
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PMID:Changes in total nitrogen, lipoproteins and amino acids in epididymal and ejaculated spermatozoa of bulls treated orally with ethylene dibromide. 77 80

We have studied the effects of subcutaneous administration of monosodium-L-glutamate (MSG) to neonatal rats on nitrogen metabolism and on general parameters at several intervals after MSG treatment. As MSG-treated rats were hypophagic, all experiments were performed both in control rats pair-fed with the MSG-treated rats and in control rats fed ad libitum. Lee index, total serum lipids and weight of the epididymal fat depots were higher in MSG-treated rats. Body and tissue weights and the amount of protein in several tissues were lower in adult MSG-obese rats than in control rats. Locomotor activity was decreased following MSG administration. Creatinine clearance was diminished by about 50% in rats treated with MSG. Urinary nitrogen and urea excretion were lower, except at four weeks, and serum urea was higher in MSG-obese rats. Considering liver size, urea synthesis by isolated hepatocytes and urea cycle enzyme activities were increased in weanling MSG obese rats and diminished in adult MSG-obese rats when compared with ad libitum controls but were not changed compared with their pair-fed controls. It is concluded that administration of monosodium-L-glutamate shortly after birth induced an increase in urea synthesis in weanling rats that was followed by a reduction in the amount of tissue proteins, suggesting that more amino acids were used for lipid synthesis and urea production in treated rats. The accelerated amino acid degradation slowed down in adult MSG-obese rats which showed an in vitro capacity to synthesise urea similar to that of their pair-fed controls.
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PMID:Nitrogen metabolism in obesity induced by monosodium-L-glutamate in rats. 132 85

Previously, we established an anti-androgen receptor (AR) monoclonal antibody. Using the antibody, we investigated immunohistological AR localization in human testes, epididymides, seminal vesicles and scrotal skins. The testes, epididymides and scrotal skins were obtained from a prostate cancer patient without pre-hormonal therapy undergoing bilateral orchiectomy. The seminal vesicles were obtained from a bladder cancer patient undergoing radical cystectomy. The tissues were immediately frozen in liquid nitrogen and kept at -80 degrees C until used. Cryostat-frozen sections were cut at 5 microns and stained by an indirect method. We obtained the following results. 1) In the testes, nuclei of Leydig cells were stained though Sertoli cells were not stained. AR localization in Leydig cells which produce testosterone suggests autocrine or intracrine mechanism in the testis. 2) In the epididymides, nuclei of epithelial cells of epididymal ducts were stained, while muscles and connective tissues were not stained. In the seminal vesicles, nuclei of glandular epithelial cells were stained. 3) In the scrotal skins, the cells of squamous cell layer have positive stainings. The cells in the upper portion of squamous cell layer were stained more intensely than the cells in the lower portion. The basal layer was not stained. The cells of the outer root sheath of hair follicles in the scrotal skins were also stained. 4) In androgen target organs, AR-positive cells and AR-negative cells were mixed in the epithelium of a glandular duct, which suggests heterogeneity of AR localization in the androgen target organs.
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PMID:[Localization of androgen receptor in male sex organ, accessory sex organs and external genital skin]. 147 18

Plasma membranes isolated from cauda epididymal and ejaculated boar sperm were inserted into planar lipid bilayers and examined for the presence of ion channels. Channel fusion was frequently observed; the most prominent was a nonselective cation channel which conducted K, Na, Cs, Ca, and Ba. Channel opening did not show a strict dependence on voltage but was partially blocked by verapamil, nitrendipine, and ruthenium red. A channel with these characteristics was observed when plasma membranes were isolated by high-pressure nitrogen cavitation (650 psi, 78% sperm head plasma membranes) or at very low nitrogen pressures (50 psi, 90% sperm head plasma membranes), suggesting that this channel may be present in the plasma membrane overlying the sperm head.
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PMID:Ion channels in boar sperm plasma membranes: characterization of a cation selective channel. 172 6

Certain amiloride analogues 3',4'-dichlorobenzamil 2',4'-dimethylbenzamil and alpha',2'-benzobenzamil hydrochloride (ATBB) stimulate calcium accumulation and motility by epididymal bovine spermatozoa. This stimulation can be seen at a range of 0.1-0.4 mM, while at higher concentration there is inhibition of calcium uptake by these amiloride analogues. The amiloride derivative 5-(4-chlorobenzyl)-2',4'-dimethylbenzamil (CBDMB), which bears a 4-chlorobenzyl substituent on the 5-amino nitrogen atom, did not stimulate calcium uptake. The amiloride analogue 3',4'-dichlorobenzamil inhibits the Na+/Ca2(+)-exchange activity in isolated plasma membrane vesicles, and the stimulatory effect of 3',4'-dichlorobenzamil on calcium uptake into epididymal sperm could be seen in Na(+)-free medium. Thus, the stimulation of Ca2+ accumulation in the cells caused by 3',4'-dichlorobenzamil is not a result of inhibiting the Na(+)-dependent Ca2+ clearance. There is no stimulation of Ca2+ uptake into ejaculated cells by adding 3',4'-dichlorobenzamil, which is not due to the presence of the calcium-transport inhibitor (caltrin) in these cells [Rufo, G.A., Schoff, P.K. & Lardy, H.A. (1984) J. Biol. Chem. 259, 2547-2552]. The stimulatory effect of 3',4'-dichlorobenzamil on Ca2+ uptake is inhibited by the voltage-dependent Ca2(+)-channel blockers nifedipin and diltiazem. This indicates that the stimulation of Ca2+ uptake by the amiloride analogues is due to the activation of a voltage-dependent Ca2+ channel of the plasma membrane.
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PMID:Stimulation of Ca2+ uptake into epididymal bull spermatozoa by analogues of amiloride. 220 10

When mouse epididymal spermatozoa were rapidly frozen in two steps (37 to -70 degrees C for solid CO2 and -70 to -196 degrees C for liquid nitrogen) as pellets, 18% raffinose provided the greatest protection to ICR mouse spermatozoa against cold-shock; sperm motility and fertilizing ability were 43% and 22.4%, respectively. A small proportion of spermatozoa frozen with 10% sucrose was motile but incapable of fertilizing ovulated oocytes. Glycerol and dimethylsulphoxide were less effective at any concentration examined. However, the fertilizing ability of frozen-thawed ICR spermatozoa was significantly improved (35.5%) by addition of glycerol (1.75% final concentration) to medium containing 18% raffinose. Spermatozoa from one outbred (ddY) and 5 inbred (C57BL/6N, C3H/HeN, DBA/2N, BALB/c and kk) strains of mice were successfully frozen in the presence of 18% raffinose and 1.75% glycerol, although the fertilization rates of frozen-thawed spermatozoa varied among strains (13% for C57BL/6N to 64% for DBA/2N). A small fraction of mouse eggs resulting from fertilization by frozen-thawed spermatozoa developed normally in vitro (37% in C57BL/6N to 71% in ICR) to the blastocyst stage and in vivo (19% for C57BL/6N spermatozoa and ddY oocytes) to Day 18 of gestation.
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PMID:Cryopreservation of mouse spermatozoa in the presence of raffinose and glycerol. 240 78

Ram spermatozoa were obtained from different regions (caput, corpus, and cauda) of the epididymis and their plasma membrane was removed using a nitrogen cavitation treatment (750 psi, 10 min equilibration at 4 degrees C). Membrane was recovered after sucrose gradient centrifugation and identified using 125I-succinylated concanavalin A (125I-succConA) as a surface marker. Based on fluorescein isothiocyanate-succConA (FITC-succConA) labeling and electron microscopy, cavitation removed plasma membrane from the anterior sperm head in the area overlying the acrosome. Cholesterol was the major sterol in plasma membrane, with desmosterol present in sperm entering the epididymis (caput sperm) but negligible in sperm after epididymal transit (cauda sperm). Ethanolamine and choline phosphoglycerides represented 70-80% of membrane phospholipids, with the ethanolamine fraction decreasing relative to choline phosphoglycerides during epididymal transit. The molar ratio of cholesterol to phospholipid increased in the plasma membrane during maturation. The bulk phospholipid-bound fatty acids consisted primarily of palmitoyl acyl groups (16:0) in caput sperm and docosahexaenoyl acyl groups (22:6) in cauda sperm. The choline phosphoglyceride fraction was purified and analyzed. It consisted of a mixture of ether acyl glycero-3-phosphocholine and diacyl phosphoglyceride, with the dominant acyl residue, at all stages of epididymal maturation, being 22:6 throughout epididymal transit. The significance of these findings relative to acquisition of fertilization capacity by sperm during epididymal maturation is discussed.
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PMID:Development changes occurring in the lipids of ram epididymal spermatozoa plasma membrane. 315 56

Cauda epididymal rat spermatozoa were isolated by flushing the excised epididymis and the plasma membrane was detached by a nitrogen cavitation treatment (500 psi, 10 minutes equilibration at 4 C). Membrane vesicles were recovered after sucrose gradient centrifugation. Portions of the sperm surface releasing the plasma membrane were assessed by light microscopy of fluoroscein isothiocyanate-succinylated concanavalin A-treated spermatozoa and by transmission electron microscopy. Plasma membrane was detached from the region overlying the acrosome from most spermatozoa and from the middle-piece overlying the mitochondria from some cells. Thus, the fraction analyzed was derived from at least two portions of the sperm surface. The fractions from the sucrose density gradient were analyzed for gross chemical composition (phospholipid, protein and sterol) and the protein components were detected after electrophoresis under denaturing conditions; the peak fractions (at density approximately 1.13 g/ml) were judged homogeneous. Replicate analyses of such preparations established mass ratios of protein to phospholipid of 0.63, total sterol to phospholipid of 0.18, and demosterol to cholesterol of 0.32. The molecular composition of the phospholipid fraction was determined to be 10% phosphatidylserine (mole percent), 3% phosphatidylinosital, 3% sphingomyelin, 31% phosphatidylethanolamine, 27% phosphatidylcholine, 10% diphosphatidylglycerol and 5% of an unknown component. Fatty acyl analyses of the phospholipid fraction revealed that approximately 70% of the residues consisted of palmitoyl (16:0) and stearoyl (18:0) acyl groups, with the balance distributed among various unsaturated acyl groups (18:1, 22:3, 22:4 and 22:5); about 40% of the recovered phospholipids represented ether acyl phosphatides. Differences in the lipid composition of rat vesicles described here and similar vesicles isolated from ram and boar spermatozoa (described previously) are discussed. The partitioning of the nitroxyl spin label 3-doxylheptane into vesicles isolated from rat and ram spermatozoa was assessed by electron paramagnetic resonance spectroscopy at temperatures between 4 C and 26 C; no difference in the response of the spin label in the two vesicle preparations was detected.
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PMID:Isolation and characterization of the plasma membrane of rat cauda epididymal spermatozoa. 340 61


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