Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.5 (RNase)
 17,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two commonly used brands of reagent strip (dipsticks) were evlauated for their sensitivity to Bence-Jones and seven other urinary proteins. Both brands showed significant differences in sensitivity to albumin, glycoprotein, ribonuclease and lysozyme; both were most sensitive to albumin and least sensitive to globulin. Furthermore, their comparative sensitivities to these proteins also differed markedly. These differences in sensitivity could lead to underestimation of protein content in urine specimens. Tests on urines from patients with multiple myeloma showed that a negative urinary dipstick test result did not rule out the presence of the disease.
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PMID:Sensitivity of in vitro diagnostic dipstick tests to urinary protein. 64 3

Cell systems as different as normal human blood lymphocytes and frog auricles release spontaneously a nucleoprotein complex in their culture medium. This release seems to be an active mechanism that is unrelated to cell death. The presence of RNA in this complex is demonstrated. The amount of extracellular RNA is regulated by the same homeostatic mechanism that has previously been shown to govern DNA release in the same cell systems. This extracellular RNA is linked by hydrogen bonds to the extracellular DNA and cannot be extracted by a usual phenol procedure, due perhaps to the presence of a glycoprotein. Further purifications by chloroform, sodium perchlorate, and hydroxyapatite are necessary to obtain an RNA molecule that is acid precipitable, RNase and KOH sensitive, and orcinol positive. The extracellular RNA sediments between 2.5 and 4S and is not a transfer RNA. It is more highly methylated than the 28S, 18S, and 4 to 5S cellular RNA. It activates DNA synthesis in vitro.
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PMID:Presence of RNA in the nucleoprotein complex spontaneously released by human lymphocytes and frog auricles in culture. 68 40

Exposure of mycobacterial growth inhibitory factor (MycoIF) to trypsin, chymotrypsin, or neuraminidase decrease its ability to produce intracellular inhibition of mycobacterial growth within macrophages, suggesting that MycoIF was a glycoprotein. MycoIF was unaffected by deoxyribonuclease or ribonuclease. Supernatant fluids from antigenically stimulated H37Ra-immunized mouse spleen cells exposed to puromycin were unable to produce significant intracellular inhibition. This indicated that the presence of MycoIF activity in supernatant fluids required protein synthesis. The filtration of MycoIF-containing supernatant fluids on Sephadex G-150 demonstrated that significant MycoIF activity appeared only in those fractions which eluted on the downward side of the serum albumin peak. Based on protein standards filtered through the Sephadex gel, the molecular weight of MycoIF was calculated to be between 20,000 and 35,000. These calculations assumed that MycoIF is a globular protein. Attempts to purify MycoIF by anion exchange chromatography (diethylaminoethylcellulose) was not successful.
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PMID:Molecular weight and other characteristics of mycobacterial growth inhibitory factor produced by spleen cells obtained from mice immunized with viable attenuated mycobacterial cells. 81 60

An ovarian cystadenocarcinoma-associated antigen (OCAA) was found to be common to all serous and mucinous cystadenocarcinomas of the ovary. It was apparently absent in tissues of normal reproductive organs. Furthermore, OCAA was not detected in benign ovarian serous and mucinous cyst-adenomas or in any other gynecologic or nongynecologic cancers thus far tested. The antigenic determinant of OCAA was immunologically unrelated to the carcinoembryonic antigen, other known tumor antigens, or the histocompatibility antigens. We purified and partially characterized OCAA. The antigen was a high-molecular-weight glycoprotein soluble in 0.6 M perchloric acid. It consisted of about 50-60% protein (based on dry wt). Amino acid composition in OCAA was characterized by a high percentage of threonine, serine, proline, and valine. Galactose and N-acetylglucosamine were the principal carbohydrate constituents. The antigenic activity was resistant to treatment with trypsin and protease and also to treatment with DNase, RNase, and N-acetylneuraminidase. The antigenicity was considerably reduced by mild periodate oxidation.
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PMID:Tumor-associated antigen for cystadenocarcinomas of the ovary. 82 81

The enzymes from the venom of Heterometrus scaber, the indole compounds present and the toxic protein of the venom have been studied. The venom contains acid phosphatase, ribonuclease, 5'-nucleotidase, hyaluronidase, acetylcholine esterase and phospholipase. A. The indole compounds present in the venom have been identified as 5-hydroxytryptophan, tryptophan, serotonin and tryptamine, along with two unidentified indole compounds. The venom produces hyperglycaemia in sublethal doses and this has been found to be due to increased adrenaline secretion. The toxic protein of the venom has been obtained in a pure form by (NH4)2SO4 fractionation, followed by fractional precipitation with acetone and chromatography over DEAE-Sephadex. The toxic fraction has been found to be homogeneous on acrylamide gel electrophoresis. It is a glycoprotein (molecular weight 15 000) containing 1.74% glucosamine, 0.87% galactosamine, 0.313% sialic acid, 3.25% fucose and 0.45% of an unidentified neutral sugar. It did not show any enzyme activities, haemolytic activity or inhibition of succinate dehydrogenase activity but it produced hyperglycaemia in sublethal doses. The toxic level (intravenous administration in rats) was found to be 0.72 mg/kg body weight.
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PMID:Investigations on the venom of the South Indian scorpion Heterometrus scaber. 111 82

The kinetic properties of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase (GlcNAc-phosphotransferase) partially purified from the soil amoeba Acanthamoeba castellanii have been studied. The transferase phosphorylated the lysosomal enzymes uteroferrin and cathepsin D 3-90-fold better than nonlysosomal glycoproteins and 16-83-fold better than a Man9GlcNAc oligosaccharide. Deglycosylated uteroferrin was a potent competitive inhibitor of the phosphorylation of intact uteroferrin (Ki of 48 microM) but did not inhibit the phosphorylation of RNase B or the simple sugar alpha-methylmannoside. Deglycosylated RNase (RNase A) did not inhibit the phosphorylation of RNase B or uteroferrin. These results indicate that purified amoeba GlcNAc-phosphotransferase recognizes a protein domain present on lysosomal enzymes but absent in most nonlysosomal glycoproteins. The transferase also exhibited a marked preference for oligosaccharides containing mannose alpha 1,2-mannose sequences, but this cannot account for the high affinity binding to lysosomal enzymes. A. castellanii extracts do not contain detectable levels of N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, the second enzyme in the biosynthetic pathway for the mannose 6-phosphate recognition marker. We conclude that A. castellanii does not utilize the phosphomannosyl sorting pathway despite expression of very high levels of GlcNAc-phosphotransferase.
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PMID:Characterization of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase from Acanthamoeba castellanii. 131 74

We previously cloned, sequenced, and expressed two distinct mammalian Na+/H+ exchanger isoforms (NHE-1 and NHE-2). We report here the cloning of a composite cDNA which encodes a third mammalian isoform (NHE-3), which is expressed specifically in intestine and kidney. The protein deduced from the longest open reading frame of this composite sequence has 832 amino acids with a calculated Mr of 92,747. The hydrophobicity plot of NHE-3 is very similar to that of NHE-1 and NHE-2. NHE-3 is also predicted to have 10-12 membrane-spanning domains and a long cytoplasmic domain which contains putative protein kinase phosphorylation motifs. NHE-3 exhibits overall 41% amino acid identity with NHE-1. NHE-3 is likely a glycoprotein as it has one potential N-linked glycosylation site, which is conserved in all NHEs identified. Northern blot analysis of poly(A+) RNA isolated from rabbit ileum using NHE-3 cDNA as a probe hybridized to a single 5.4-kilobase transcript. More detailed tissue distribution of message was performed by ribonuclease protection assay. It was found that NHE-3 message is only expressed in intestine and kidney, with the kidney cortex having the most abundant message, followed by intestine and kidney medulla. In intestine, ileum and ascending colon have the same amount of message, with much lesser amounts in jejunum. The message is absent from duodenum and descending colon, which lack the neutral NaCl absorptive process. Thus, NHE-3 might be involved in Na+ absorption in intestinal and renal epithelial cells.
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PMID:Cloning and sequencing of a rabbit cDNA encoding an intestinal and kidney-specific Na+/H+ exchanger isoform (NHE-3). 137 92

It was found, in cell-free assays, that the Man8GlcNAc2 and Man7GlcNAc2 isomers having the mannose unit to which the glucose is added were glucosylated by the rat liver glucosyltransferase at 50 and 15%, respectively, of the rate of Man9GlcNAc2 glucosylation. This indicates that processing by endoplasmic reticulum mannosidases decreases the extent of glycoprotein glucosylation. All five different glycoproteins tested (bovine and porcine thyroglobulins, phytohemagglutinin, soybean agglutinin, and bovine pancreas ribonuclease B) were found to be poorly glucosylated or not glucosylated unless they were subjected to treatments that modified their native conformations. The effect of denaturation was not to expose the oligosaccharides but to make protein determinants, required for enzymatic activity, accessible to the glucosyltransferase because (a) cleavage of denatured glycoproteins by unspecific (Pronase) or specific (trypsin) proteases abolished their glucose acceptor capacities almost completely except when the tryptic peptides were held together by disulfide bonds and (b) high mannose oligosaccharides in native glycoproteins, although poorly glucosylated or not glucosylated, were accessible to macromolecular probes as concanavalin A-Sepharose, endo-beta-N-acetylglucosaminidase H, and jack bean alpha-mannosidase. In addition, denatured, endo-beta-N-acetylglucosaminidase H deglycosylated glycoproteins were found to be potent inhibitors of the glucosylation of denatured glycoproteins. It is suggested that in vivo only unfolded, partially folded, and malfolded glycoproteins are glucosylated and that glucosylation stops upon adoption of the correct conformation, a process that hides the protein determinants (possibly hydrophobic amino acids) from the glucosyltransferase.
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PMID:Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. 153 Oct 24

In an effort to better understand the preferential resistance to actinomycin D displayed by the multidrug-resistant Chinese hamster lung cell line DC-3F/ADX, we have cloned from those cells a number of cDNAs representing p-glycoprotein gene transcripts. Of the 12 clones isolated, all represent pgp1 transcripts and one, pADX165, contains a 4304-base pair insert with an open reading frame encoding a 1276-amino acid protein that is the homolog of the mouse mdr3/mdr1a gene product. A domain by domain comparison of this protein with p-glycoproteins capable of supporting multidrug resistance, i.e. human mdr1, mouse mdr1/mdr1b, and mouse mdr3/mdr1a, shows that, in addition to the ATP binding sites, the second, fourth, and eleventh transmembrane domains and the four small intracellular loops, IC-1, IC-2, IC-4, and IC-5, are highly conserved and are therefore likely to be important for the maintenance of p-glycoprotein function. Of the remaining 11 cDNA clones, 9 were found to be truncated versions of pADX165. Two others, however, pADX185 and pADX124, contained internal deletions resulting in open reading frames capable of encoding lnovel forms of p-glycoprotein. S1 nuclease and RNase protection analysis demonstrated that these cDNAs represent transcripts present in a number of different multidrug-resistant Chinese hamster lung cell lines. Hence, both are considered to be splicing variants of the hamster pgp1 gene primary transcript.
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PMID:Full length and alternatively spliced pgp1 transcripts in multidrug-resistant Chinese hamster lung cells. 167 63

Basal and thyroid hormone-regulated expression of constructs containing varying lengths of 5' flanking sequence of the human glycoprotein hormone alpha subunit gene ligated to the reporter gene encoding chloramphenicol acetyl transferase (CAT) were examined in transfected pituitary GH3 cells. CAT gene expression was quantified by measurement of CAT enzyme activity. In addition, an RNase protection assay was used to confirm changes in CAT mRNA levels and to verify regulation of transcription from the authentic alpha gene start site. The pattern of basal alpha promoter activity indicated the presence of inhibitory DNA elements between -98 and -172 and upstream of -846 relative to the transcriptional start site, as well as a stimulatory element between -346 and -846. Each of the transfected constructs exhibited tri-iodothyronine inhibition of alpha promoter activity, suggesting the presence of an inhibitory thyroid hormone response element within 98 bp of the alpha gene transcriptional start site.
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PMID:Multiple DNA elements determine basal and thyroid hormone regulated expression of the human glycoprotein alpha subunit gene in pituitary cells. 169 80


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