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)

Androgen-binding protein (ABP) was purified from caput epididymis of the rat by sequential chromatography on DEAE-Sepharose, hydroxylapatite, dihydrotestosterone-17 beta-hemisuccinyl-1,6-diaminohexane-Sepharose, and Sephadex G-150. The final product migrated as a single band corresponding to a peak of protein-bound [3H]dihydrotestosterone on polyacrylamide gel electrophoresis. A molecular weight of 100,000 was estimated by sedimentation equilibrium. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, subunits of Mr = 47,000 and 41,000 were observed. Amino acid analysis indicated ABP to be rich in leucine while nonpolar aminoacids totaled only 51%. Its carbohydrate content is 25%. Antibodies to purified ABP were raised in a rabbit and evaluated by immunodiffusion, immunoelectrophoresis, binding inhibition, radioimmunoassay, and immunocytochemistry. Immunoperoxidase staining localized ABP in the basal and adluminal regions of seminiferous tubules of rat testis and in secretory granules of cultured Sertoli cells. In principal cells of caput epididymis, ABP is concentrated in the supranuclear region known to contain morphological specializations for absorption. These immunocytochemical results confirm that ABP synthesized and secreted by Sertoli cells in the testis is transported to the epididymal duct via testicular fluid and is taken up by epithelial cells of the proximal segments.
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PMID:Androgen-binding protein. Purification from rat epididymis, characterization, and immunocytochemical localization. 719 73

A method for the purification of androgen binding protein (ABP) from the rabbit epididymis is presented. Epididymal extracts were submitted to sequential ammonium sulfate precipitation, androgen affinity chromatography, concanavalin A (Con A) affinity chromatography, and preparative polyacrylamide gel electrophoresis. Since the blood protein testosterone-estradiol binding globulin (TeBG) was a possible component of the epididymal extract, ABP was differentiated and separated from TeBG by affinity chromatography on Con A-Sepharose since the latter protein was shown to be completely absorbed by the lectin while the former was not. The final product was shown to be pure by polyacrylamide gel electrophoresis. Electrophoresis in the presence of sodium dodecyl sulfate revealed that ABP is comprised of subunits.
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PMID:Purification and characterization of androgen binding protein from rabbit epididymis. 720 23

Lipid analysis of bovine epididymal spermatozoa showed relatively large amounts of alkylacyl- and alk-1-enylacylglycerols in their choline and ethanol-amine phospholipids and alkylacylglycerol as the major constituent of a glycolipid tentatively identified as a monogalactosyl sulfate. The ether lipids exhibited remarkably simple molecular structures, i.e., the phospholipids had only 16:0 as alkyl and alk-1-enyl groups and their constituent fatty acids were almost exclusively 22:5 (n-6) and 22:6 (n-3). The glycolipid had mainly 16:0 as both alkyl and acyl moieties. In contrast, the diacyl choline and ethanolamine phosphoglycerides exhibited a much more complex fatty acid composition. 1,2-Diacylglycerols were the major nonpolar glycerolipid class and their acyl groups consisted almost exclusively of 14:0, 16:0 and 18:0. Labeled glycerol and dihydroxyacetone added to the incubation medium were readily incorporated into sperm lipids under both aerobic and anaerobic conditions. In each case, diacylcholine phosphoglycerides, diacylglycerols and phosphatidic acid were the major labeled lipids. Distribution of label among the molecular species of diacylglycerols and choline phosphoglycerides resembled somewhat their natural abundance. No radioactivity was found in alkylacyl or alk-1-enylacyl glycerolipids. The ether lipids may provide stable structural components of sperm membrane while the diacyl analogs undergo degradation and resynthesis.
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PMID:Structure and metabolism of phospholipids in bovine epididymal spermatozoa. 737 37

Spermatozoa from four regions of the epididymis and from ejaculated semen were evaluated for their resistance to cold shock, progressive motility, and structural stability. Spermatozoa were incubated at 38 C and their percentage of eosinophilia was compared with that of spermatozoa cooled to 0 C in 2 minutes, 10 C in 12 minutes, or 4 C in 22 minutes. Spermatozoa motility was estimated visually under phase-contrast microscopy and was recorded by cinematography. Structural stability of spermatozoa incubated in 0.05 M sodium borate buffer, 0.035 M sodium dodecyl sulfate (SDS), 0.002 M dithiothreitol (DTT), or SDS+DDT was evaluated by phase-contrast and electron microscopy. The percentage of eosinophilic spermatozoa did not differ among regions of the epididymis and was not increased by cold shock. Cooling ejaculated spermatozoa to 0 C in 2 minutes increased (P < 0.01) the occurrence of eosinophilia (32% vs 73%). Spermatozoa released from the caput or proximal corpus epididymidis into 0.154 M NaCl were not progressively motile; only 4% of the spermatozoa from the distal corpus were motile Cauda epididymal and ejaculated spermatozoa exhibited similar motility (41% vs 47%). Stability of chromatin was greater in spermatozoa from the distal corpus than those from the caput epididymis. Chromatin of spermatozoa from the distal corpus was resistant to 7.5 minutes of SDS+DTT treatment, whereas virtually all spermatozoal nuclei from the caput were decondensed by SDS alone. Tail organelles of spermatozoa acquired stability between the proximal corpus and the cauda epididymidis. All tail organelles of spermatozoa from the proximal corpus were dissolved by 7.5 minutes of SDS treatment, whereas tail organelles of distal corpus epididymal spermatozoa had dissolved after 7.5 minutes of SDS+DTT treatment. Stability of tail organelles in cauda epididymal and ejaculated spermatozoa was similar. Seemingly, equine spermatozoa are infertile until they enter the cauda epididymidis.
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PMID:Maturation of equine epididymal spermatozoa. 744 13

The genetically obese Zucker rat is a well-characterized model of early-onset human obesity. The 120 kDa protein was recently found in the liver cytosol of obese Zucker rats at levels higher than that in lean Zucker rats. We isolated this protein using precipitation with ammonium sulfate, DEAE-Sephacel chromatography, and preparative polyacrylamide gel electrophoresis; the product showed a single band on SDS-polyacrylamide gel electrophoresis. Immunoblotting analysis revealed that the 120 kDa protein was predominantly localized in the liver cytosol of obese Zucker rats. The amount of this protein in lean Zucker rats was less than one-fifth of that found in obese Zucker rats. Further, there were only trace amounts of this protein in the lung tissues, and no detectable amount in other tissues, such as kidney, epididymal adipose tissue, brain, spleen, skeletal muscle, or serum, in either strain of rat. These data suggest that the 120 kDa protein contributes to the abnormal lipid metabolism in obese Zucker rats.
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PMID:Isolation and localization of the 120 kDa protein in the liver of genetically obese Zucker rats. 818 33

A protein was purified from rabbit seminal plasma using preparative acrylamide disc electrophoresis, ammonium sulfate precipitation and gel filtration. The protein inhibited the in vitro fertilization of mouse ova inseminated with epididymal sperm and with capacitated sperm. The inhibition was not observed, however, when only ova were exposed to the protein prior to mixing with sperm. The partial protein sequence analysis revealed the strong homology of the rabbit fertilization inhibitory protein to human annexin V.
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PMID:Characterization of capacitation inhibitory protein from rabbit seminal plasma: homology with human annexins. 836 90

Cyclic AMP-dependent changes in phosphorylation of epididymal mouse sperm suspensions were examined in media designed to manipulate capacitation and the expression of parameters associated with full fertilizing ability, i.e. hyperactivated motility and the acrosome reaction. After initial assessment of cAMP-dependent protein kinase activity in frozen-thawed and lyophilized sperm suspensions using exogenous substrate, phosphorylation of endogenous sperm phosphoproteins was examined using sodium dodecyl sulfate polyacrylamide gel electrophoresis followed by autoradiography or immunoblotting. Numerous phosphoproteins were detected in both incapacitated and capacitated suspensions, the majority of which were probably concerned with motility; full expression of fertilizing ability appeared to involve an increase in the amount of endogenous phosphorylation as deduced from the decreased amount of 32P incorporation in these suspensions. The addition of the cAMP-dependent protein kinase inhibitors, H8 and PKI (6-22) amide, demonstrated that most of the phosphoproteins detected were phosphorylated in a cAMP-dependent manner. Of particular interest was a phosphoprotein with an M(r) of about 95,000 which was consistently observed in capacitated suspensions. Evidence suggests that this may be phosphorylated on tyrosine residues, since the inclusion of orthovanadate, a phosphoryltyrosine phosphatase inhibitor, altered phosphorylation of this protein. Furthermore, immunodetection using the antiphosphotyrosine antibody, PY-20, identified five proteins with approximate M(r) 116,000, 105,000, 95,000, 86,000, and 76,000, and possibly a sixth at 54,000. The 95,000 protein was consistently diminished in ionophore-treated spermatozoa, indicating that the protein was located in the acrosomal cap region. These results suggest that the protein may be the same phosphotyrosine-containing protein as that described by Leyton and Saling (1989) which has been proposed to play a role in acrosomal exocytosis.
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PMID:Cyclic AMP-dependent phosphorylation of epididymal mouse sperm proteins during capacitation in vitro: identification of an M(r) 95,000 phosphotyrosine-containing protein. 838 23

Mice with a temporally regulatable ovine metallothionein 1a--ovine growth hormone transgene (oMT1a-oGH) were utilized to study the effects of withdrawal of elevated circulating levels of growth hormone (GH) on growth and body composition. The transgene was activated from 21-42 days of age by provision of zinc sulfate in the drinking water. At 42 days, mice were allocated to either activated transgenic (remain on zinc sulfate) or inactivated transgenic (removal of zinc sulfate) groups, and to receive either ad libitum or restricted (80-90% of ad libitum) access to feed. Non-transgenic control mice were treated similarly. Body weights and intakes were recorded weekly. Mice were killed at 70 d and epididymal and subcutaneous fat pads, trimmed hind carcass and various organs were weighed. The main findings of this study are: (1) food-restricted mice possessing an activated oMT1a-oGH transgene fail to demonstrate increased growth, but exhibit significantly reduced levels of fat (P < 0.05) relative to all other genotype x feed level combinations; and (2) inactivation of the oMT1a-oGH transgene, following a period of elevated GH levels, leads to development of obesity as evidenced by two to three fold increases in epididymal and subcutaneous fat pad weights (P < 0.01) relative to both activated transgenic and non-transgenic control mice. These large increases in fat deposition also occurred when intake was restricted to 80-90% of ad libitum levels, indicating that metabolic changes independent of intake occur in these inactivated transgenic mice. It is possible that highly elevated production of GH in activated oMT1a-oGH transgenic mice leads to (1) enhanced promotion of preadipocyte differentiation, leading to increased numbers of adipocytes that, upon cessation of oGH production, are available for lipid deposition resulting in obesity, or (2) alterations in production of or responsiveness to insulin, leading to increased fat deposition upon removal of the chronic anti-lipogenic actions of GH. The oMT1a-oGH transgenic mouse line should provide a new genetic model with which to investigate the mechanisms by which growth hormone affects obesity.
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PMID:Development of obesity following inactivation of a growth hormone transgene in mice. 858 37

In the microvascular system, pericytes are located at the abdominal side of capillary endothelial cells. To discover the role of pericytes in the microvascular system, we have analyzed the extracellular proteins secreted from pericytes isolated from microvessel fragments of rat epididymal fat pads and found that they synthesize substantial amounts of basement membrane components such as type IV collagen and laminins. Secretion of type IV collagen was markedly stimulated by ascorbic acid phosphate. Reducing and nonreducing sodium dodecyl sulfate gel electrophoresis showed that pericytes produce six laminin chains assembled into different trimeric isoforms. Two of them were similar to laminin variants produced by aortic and pulmonal endothelial cells but others were suggested to be novel variants.
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PMID:Pericytes from microvessel fragment produce type IV collagen and multiple laminin isoforms. 870 15

The expression and androgen regulation of beta-glucuronidase molecular forms were examined in mouse epididymis, liver, and kidney. Two-dimensional polyacrylamide gel electrophoresis performed under nondenaturing conditions showed that, compared to liver and kidney, which contain four microsomal (M1-M4) and a major lysosomal (L) form of beta-glucuronidase, the epididymis revealed regional differences and tissue specificity in the expression of the various molecular forms of the enzyme. Only the lysosomal form (pI 5.4-6.1) is present in the caput epididymidis while the corpus/cauda contains the lysosomal form, the free X form (pI 5.9-6.3) and the four microsomal forms (X form complexed with egasyn). Mutant mice that lack egasyn have no microsomal forms in the distal epididymis. In epididymal fluid, the lysosomal form is found throughout the epididymis, whereas the X form appears only in the corpus/cauda epididymidis. Sodium dodecyl Sulfate (SDS)-gel electrophoresis and western blot analysis of immunoprecipitated beta-glucuronidase revealed only one band corresponding to the L form (apparent molecular weight 74 kDa) in the caput epididymidis and two bands in the corpus/cauda (apparent molecular weights 73 and 75 kDa), corresponding to L and X forms, respectively. Castration of mice led to the suppression of the regional differences in the appearance of X and M forms in the epididymis. Testosterone supplementation to castrated mice restored the characteristic electrophoretic pattern of beta-glucuronidase in the caput epididymidis. In the liver and kidney, castration has no effect on the expression of the molecular forms, whereas androgen treatment induced the X form in the kidney. Histochemical localization of beta-glucuronidase confirmed the region specificity seen in the epididymis and in addition revealed cell specificity in the expression of beta-glucuronidase. These results indicate that beta-glucuronidase shows tissue specificity and, in the case of the epididymis, region and cell specificity. In addition, the enzyme in the different tissues responds differentially to androgens.
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PMID:Androgen regulation of molecular forms of beta-D-glucuronidase in the mouse epididymis: comparison with liver and kidney. 879 10


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