Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.1 (RNase)
16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of 5'-nucleotidase (EC 1.3.5), cyclic nucleotide phosphodiesterase (EC 2.1.4.17), non-specific phosphodiesterase (EC 3.1.4.1) and ribonuclease (EC 1.7.7.16)has been investigated in the seminal plasma of whole semen and in the secretions of the seminal vesicle, prostate and epididymis of the bull, boar, ram, stallion, jackass, rabbit and man. Bull seminal plasma showed the highest activity for 5'-nucleotidase, cyclic nucleotide phosphodiesterase and ribonuclease; in contrast, stallion and jackass semen were very poor in these enzymes. Ram, rabbit and boar seminal plasma showed intermediate levels for all enzymes studied. In the bull and ram, nucleolytic enzymes were found to be secreted by the seminal vesicles but in the boar, rabbit and stallion they originate mostly from the epididymis. In human seminal plasma all of the enzymes studied exhibited activity but the levels were generally lower than those recorded for the other species.
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PMID:The activity of some nucleolytic enzymes in semen and in the secretion of the male reproductive tract. 19 15

The pattern of proteins in the soluble fraction of the cytoplasm of the rat epididymis was studied by acrylamide gel electrophoresis. The components of five distinct bands, labelled A, B, C, D and E, were found to be sensitive to changes in androgen in the blood. Castration for 14 days produced a sharp decrease in the colour intensity of bands B-E when stained with Amido black. After 21 days of castration, bands D and E were undetectable, bands B and C were severely diminished and band A was more intense. Seven days of replacement with testosterone (1 mg/day) induced a return towards a normal pattern. The degree of restoration was inversely proportional to the duration of castration. Quantitation by densitometry showed that the relative contributions of bands B-E to the region A-E were 61% in the control rat, only 27% after 21 days of castration and 35% when testosterone was given between days 14 and 21 of castration. The components of bands A-E are presumed to be proteins since the electrophoretic pattern was altered by digestion with pronase but not by ribonuclease, phospholipase C or neuraminidase. Epididymides from castrated and androgen-treated castrated rats were incubated with 14C- and 3H-labelled mixed amino acids respectively. After co-electrophoresis the ratio 3H: 14C rose from a baseline of 2-5 in band B, 32 in band C and 7 in bands D and E. Molecular weights were estimated as 27900 for B, 23100 for C and 34400 for D. Band A had the same electrophoretic mobility as serum albumin. Bands B and C were also present in testicular cytosol. Bands D and E were only found in the epididymis, localized mainly within the lumen of the tubules. Bands B-E increased with age during sexual maturation, bands D and E became detectable in the 20-day-old rats. Preliminary evidence indicates that the proteins in bands C, D and E can be removed from caput spermatozoa by washing.
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PMID:Androgen-controlled specific proteins in rat epididymis. 127 Sep 59

A study was conducted to determine the levels of cellular retinol-binding protein (CRBP) mRNA and protein in various tissues of the rat, to explore relationship between CRBP mRNA and protein levels in different tissues, and to examine the effects of changes in retinol nutritional status on the tissue distribution and levels of CRBP mRNA. Previous studies have shown that tissue CRBP protein levels are reduced in totally retinoid-deficient rats, but are otherwise minimally affected by changes in retinoid status. Three groups of male rats were compared: normal controls, retinoid-deficient, and retinol-repleted deficient rats. CRBP mRNA levels were measured by RNase protection assay and CRBP protein levels by radioimmunoassay in seven tissues. High levels of both CRBP mRNA and CRBP protein were found in the proximal epididymis, kidney, and liver; lower levels were seen in lung, testis, spleen, and small intestine. Tissue CRBP mRNA and protein levels were highly correlated (P less than 0.01) with each other. Retinoid deficiency did not alter the levels of CRBP mRNA found in the proximal epididymis, kidney, and liver. In contrast, CRBP mRNA levels in the lung, testis, spleen, and small intestine were reduced substantially in retinoid-deficient rats, to values that were only 23% to 50% of the corresponding values in the tissues of control rats. After oral repletion with retinol (4-18 h earlier), CRBP mRNA levels for these latter four tissues were found to have risen to control or near-control levels. The suggestion is raised that retinol repletion may have directly induced the expression of the CRBP gene in these particular tissues.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Cellular retinol-binding protein messenger RNA levels in normal and retinoid-deficient rats. 238 Jun 30

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.
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PMID:Structural conversion of cytosolic steroid receptors by an age-dependent epididymal protease. 391 13

Spermatozoa from the cauda of the epididymis of the hamster and rat were incubated with [5-(3)H]uridine and glucose. By using a procedure avoiding bacterial and other cellular contamination, sonic extracts were prepared and digested with deoxyribonuclease and Pronase. Radioactive RNA of high molecular weight was isolated by two methods: (a) gel filtration on Sephadex G-75 columns and (b) polyacrylamide-gel electrophoresis in which it migrated in the region of 28S and 23S RNA markers. The macromolecules were alkali-labile and hydrolysed by ribonuclease. From (3)H radioactivity and E(260) of the isolated RNA the rate of incorporation of uridine into RNA of spermatozoa was calculated to be 0.1-0.5nmol/h per mg of RNA.
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PMID:Ribonucleic acid synthesis by spermatozoa from the rat and hamster. 474 26

A biochemical study was made on the effects of low doses of alpha-chlorohydrin on the protein and nucleic acid metabolism of the rat testis and epididymis. RNA and protein levels were decreased both in the testis and epididymis. The DNA content of the testis and epididymis did not change after exposure of the animals to the drug. The reduced concentrations of RNA and protein were closely paralleled by the increased activity of proteinase (protein hydrolyzing enzyme) and ribonuclease (RNA degrading enzyme) in the testis and epididymis. The gamma-glutamyl transpeptidase activity of both the testis and epididymis was also reduced indicating the slow transfer of amino acids across the cell membranes of testis and epididymis and thus low protein synthesis. The DNAase levels of rat testis and epididymis did not show any appreciable change in response to the alpha-chlorohydrin treatment. These studies indicate that although there may not be any histological damage in the tissue the metabolic pathways may become defective much earlier before any visible morphological change is discernible.
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PMID:Biochemical observations on the protein and nucleic acid metabolism of the rat testis and epididymis after treatment with low doses of alpha-chlorohydrin. 616 92

Wistar male rats received an intratesticular injection (at 114 and 265 days of age) of 3 mg of partially purified bull seminal ribonuclease (AS RNase) or saline. It was found that sexual behaviour (initiation of copulation as well as copulatory behavioural pattern) of experimental males was not changed, but the ability of these males to fertilize females was evidently suppressed. In addition to significantly lower weights of testes and epididymis, inhibition of seminiferous epithelium development (aspermatogenesis) associated with the absence of spermatozoa was determined in cauda epididymidis in experimental animals. However, Leydig cells remained without changes. Plasma testosterone levels of AS RNase treated males were not altered in comparison with the controls. Thus AS RNase specifically impaired spermatogenesis but did not influence androgen action and sexual behaviour.
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PMID:The effect of bull seminal ribonuclease on reproductive organs and sexual behaviour in male rats. 645 96

Cytosols of whole testicular homogenates from the Syrian golden hamster contained specific binding sites for [3H]triamcinolone acetonide that exhibited limited capacity and high affinity binding characteristic of glucocorticoid receptors in other target tissues. The receptor complex sedimented as an 8.6S binder in low salt 5-20% linear sucrose gradients and as 6.2S and 4.0S moieties in 0.15M and 0.4 M KCl, respectively. The Ka at equilibrium was 3.1-3.3 X 10(9) M-1 at 4 C in intact and adrenalectomized males. The testicular glucocorticoid binder was vulnerable to proteolytic degradation while being completely resistant to the action of RNase and DNase. In addition the binding protein exhibited the usual steroid specificities for type I glucocorticoid receptor: triamcinolone acetonide greater than dexamethasone greater than cortisol greater than corticosterone greater than progesterone greater than aldosterone greater than prednisone greater than 5 alpha-dihydrotestosterone greater than diethylstilbestrol. Unexpectedly, 17 beta-estradiol competed for receptor binding to the same extent as prednisone. A 3.2 S nuclear receptor was extracted from purified testicular nuclei after incubation of whole suspensions in culture media containing 5 nm radiolabeled triamcinolone acetonide at 32 C. Although the glucocorticoid receptor concentrations in prepubertal, adrenalectomized, and hypophysectomized animals were markedly higher in the testis compared to the concentration in the normal adult hamster (52 +/- 4 fmol/mg cytosol protein), the greatest total amount of receptor per testis was found in the mature intact animal. Moreover, under the conditions studied, the concentration of glucocorticoid receptor substantially exceeded the levels of either androgen or estrogen receptor when determined simultaneously. In contrast, no measurable cytoplasmic [3H]triamcinolone acetonide binding was detected in adjacent urogenital organs such as the epididymis and seminal vesicle. It is therefore unlikely that the testicular glucocorticoid receptor is associated with the spermatid or present as a secretory product in the seminiferous tubule lumen.
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PMID:Characterization of specific glucocorticoid receptor in the Syrian hamster testis. 729 80

Differential screening of a human epididymal cDNA library led to the isolation and characterization of a major epididymis-specific cDNA clone family, referred to as HE3. More detailed sequence and PCR analysis identified two different but homologous gene transcripts, HE3 alpha and HE3 beta. The former represents an mRNA of ca. 1 kb, encoding a putative small secretory polypeptide of 14903 MW. The HE3 beta transcript was only found as incomplete 3' fragments. Analysis of human genomic DNA by Southern blotting suggested the presence in the human genome of at least three independent HE3-related genes. Isolation of genomic clones for the HE3 alpha gene showed this to contain a single intron of 1.4 kb in the 5' noncoding region. Although genomic clones corresponding to HE3 beta could not be found, a third highly homologous gene, HE3 gamma, was identified as a potential pseudogene. Neither nucleotide nor encoded amino acid sequences of the HE3 gene family are related to any other known sequence in the central databases, and thus represents a novel human gene family, with at least three nonallelic members. Northern hybridization analysis showed that HE3 gene products are specifically expressed in the human epididymis, and not in any other tissue examined. Furthermore, except for the pig, no other nonprimate species has been identified to express homologous sequences in the epididymis. RNase protection assays showed that both the HE3 alpha and HE3 beta, but not the HE3 gamma genes, are expressed in the human epididymis.
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PMID:Major human epididymis-specific gene product, HE3, is the first representative of a novel gene family. 751 8

We have isolated and characterized two molecular types of guinea pig (GP) apolipoprotein D (apoD) cDNA. The sequences of cDNA clones GP APO D-20 and -38 are 100 % homologous in their putative exons 2-5, as determined by analogy within human apoD gene, but they differ totally in their putative exon 1. RNase protection assays showed the presence of both apoD RNA types 20 and 38 in cauda epididymis. Northern blot analysis revealed four polyadenylated apoD bands at 3.2, 2.7, 1.7, and 1.0 kb. Types 20 and 38 specific probes hybridized with the major 1-kb mRNA and two of the three other minor RNA transcripts, respectively. Southern blot analysis revealed that the guinea pig genome probably contains one apoD gene. Our data also demonstrated that the cauda epididymis and fallopian tubes had an apoD mRNA concentration 100-fold higher than the liver, suggesting that the apoD gene expression could be associated with the presence of steroids. The levels of the 1-kb mRNA increased in the fallopian tubes and ovaries during gestation and were lower in fetal reproductive tissues and liver than in mature animals. No positive correlation was found between apoD and 3 beta-hydroxysteroid dehydrogenase/delta5-delta4 isomerase (3 beta-HSD) mRNA levels in these tissues, thus suggesting that high amounts of apoD mRNA are not necessarily associated with in situ progesterone synthesis. Taken together, our results indicate that both the guinea pig epididymis and fallopian tubes are excellent models to study the local role of apoD in steroid target tissues.
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PMID:Guinea pig apolipoprotein D RNA diversity, and developmental and gestational modulation of mRNA levels. 766 86


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