Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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 effect of RNase on the transformation of progesterone receptor from rabbit uterus was studied by density-gradient centrifugation and DNA-cellulose binding assay. The 7S form of the receptor in crude cytosol was RNase sensitive, and converted to the 4S form after RNase treatment. This reaction was prevented by an RNase inhibitor and reversed by the addition of ribosomal RNA. RNase treatment also caused a two-fold increase in the DNA binding of cytosolic receptor, and reduced the time required for heat-induced transformation. However, sucrose-gradient-purified progesterone receptor (7S) did not undergo transformation by warming unless exogenous RNase was added, thereby suggesting that a cytosolic factor, which might be endogenous RNase, is necessary for the heat-induced transformation of progesterone receptor. Furthermore, degradation of the receptors which occurred after prolonged warming at 25 degrees C in the presence of RNase could be prevented by the addition of DNA-cellulose to the reaction mixture. These results indicate that RNA is associated with the 7S form of progesterone receptor, and that its hydrolysis by RNase might be involved in the transformation of this receptor.
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PMID:Ribonuclease-induced transformation of progesterone receptor from rabbit uterus. 242 51

The cytosolic untransformed molybdate-stabilized glucocorticoid-receptor complex from rat liver was eluted as a heterogenous peak containing two components with Stokes radii (Rs) of 8.3 nm and 7.1 nm when analyzed by size-exclusion HPLC even in the absence of molybdate. In contrast, the highly purified glucocorticoid receptor yielded a sharp symmetrical peak of Rs = 7.1 nm. We demonstrate that the 7.1-nm component could not result from a proteolytic degradation of the 8.3-nm receptor form. The same receptor heterogeneity was observed in thymus cytosol which contains less proteases than liver. After labeling with [3H]dexamethasone 21-mesylate and SDS/PAGE the same 94-kDa receptor band was revealed in both the 8.3-nm and 7.1-nm forms. Immunoblotting experiments showed that both the 94-kDa hormone-binding subunit and the 90-kDa heat-shock protein were present in the two different receptor forms. The 8.3-nm receptor form was converted to the 7.1-nm receptor form after treatment by ribonuclease A in the presence of molybdate and this effect was dose-dependent, being completely prevented by placental ribonuclease inhibitor (RNasin). In contrast, in the presence of molybdate, the 7.1-nm receptor form was ribonuclease-insensitive. Treatment of cytosol with RNase A in the absence of molybdate, partially shifted the untransformed receptor towards the 5.2-nm transformed receptor form. This effect was abolished by placental ribonuclease inhibitor. RNase S protein, an enzymatically inactive proteolytic fragment of RNase A, or S1 nuclease, which is specific for single-stranded nucleic acids, were ineffective when used instead of RNase A. In contrast, cobra venom endonuclease, which preferentially attacks double-stranded regions of small RNAs, caused a complete conversion of the 7-8-nm untransformed receptor to the 5.2-nm transformed receptor form. These results were not observed in the presence of molybdate. Addition of RNasin prior to heating cytosol in the absence of molybdate did not prevent the receptor from dissociating to the 5.2-nm form, suggesting that an endogenous RNase is not involved in the transformation process. The 7.1-nm receptor form was shifted to a 9.2-nm complex when incubated with an excess of GR 49 antireceptor antibody, whereas the 8.3-nm receptor form did not bind to the antibody.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:RNA binding to the untransformed glucocorticoid receptor. Sensitivity to substrate-specific ribonucleases and characterization of a ribonucleic acid associated with the purified receptor. 246 3

Acidic and alkaline RNase activity from healthy humans and gastric cancer patients has been studied. A decrease in daily saliva production and an increase in RNase activity was detected saliva of cancer patients. This suggests the existence of RNase inhibitors in healthy humans. This supposition is further confirmed by comparative analysis of total, joint fractional and reconstituted RNase activity. A considerable increase in acidic RNase inhibitors and disappearance of alkaline RNase inhibitor was observed in cancer patients. The specificity, mechanisms and clinical significance of this phenomena has been discussed.
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PMID:[Regulation of the RNAse activity of the saliva in healthy subjects and in stomach cancer]. 271 95

Human poly (C) avid serum ribonuclease (RNase) differs in physico-chemical, electrophoretic, and catalytic properties from ribonuclease activity encountered in liver preparations. The first is reported as "secretory type", the latter, because it is undetectable in body fluids, as "nonsecretory type". We determined RNase activity in 11 hepatoma patients. A statistical difference from a normal control of corresponding age was encountered in both age groups investigated (51-60 years, P less than 0.05; 61-70 years, P less than 0.01). The circumstances mentioned above make the tumor itself unlikely to be the source of RNase elevation. Besides a diminished synthesis of RNase inhibitor by hepatoma cells, tumor-derived polyamines could contribute to enhanced RNase activity. The influence of polyamines on RNase activity has already been demonstrated by in vitro experiments. Simultaneous estimation of polyamines and RNase is required to elucidate in vivo circumstances.
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PMID:Estimation of poly (C) avid serum ribonuclease in hepatoma patients. 303 38

Messenger RNAs in eukaryotic cells exhibit a broad range of stabilities in vivo. Globin mRNA has a half life in excess of 50 h, but the half life of the c-myc oncogene mRNA is less than 20 min. Regulation of gene expression may be accomplished by a variety of mechanisms, including altering mRNA stability. We have examined the nuclear and cytoplasmic fractions of cells for factors affecting the metabolism of mRNA. Here we report that a HeLa whole-cell extract contains a factor that protects beta-globin mRNA from attack by RNases in a mouse erythroleukemia cell cytoplasmic extract. The factor is non-dialysable, inactivated by proteinase K and heat treatment, and resistant to RNase and DNase digestion. The HeLa cell factor resembles placental RNase inhibitor in that the mRNA-protecting activity is effective against RNase A and that treatment of the extract with N-ethylmaleimide completely destroys the protective activity. However, purified placental RNase inhibitor was unable to inhibit the RNase activity in the MELC cytoplasmic extract. These results suggest that the HeLa cell extract contains an RNase inhibitor (or inhibitors) with an activity or specificity that is distinct from that of placental RNase inhibitor.
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PMID:Cellular factor affecting the stability of beta-globin mRNA. 316 61

The primary structure of the ribonuclease inhibitor from pig liver has been determined by amino acid sequence analysis. The N alpha-acetylated polypeptide chain of 456 amino acids consists of 15 homologous leucine-rich repeats, characterized by leucyl residues at constant positions. Two types of alternating repeats occur, 29 (A) and 28 (B) residues long. The degree of identity between repeats of a given type ranged from 25 to 60%. Only one deletion in the B-repeat was necessary to perfectly align the leucyl residues between the two repeats. Leucine-rich repeats have previously been found in four membrane-bound proteins and one extracellular protein, and their amphiphilic character suggested that they could be involved in membrane binding. Ribonuclease inhibitor is the first example of a cytoplasmic protein containing this type of repeat. It seems likely, therefore, that leucine-rich repeats can have functions other than forming membrane binding structures.
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PMID:Amino acid sequence of the ribonuclease inhibitor from porcine liver reveals the presence of leucine-rich repeats. 321 61

After inactivation of RNase inhibitor by parachloromercuribenzoate, total alkaline RNase activity was found to be two fold higher in white matter as in grey matter extracts from human brain tissue. This activity was lower in human purified myelin. Two human cerebrospinal fluid (CSF) RNase isoenzymes of group 3 (a minor one, RNase 3.1, and a major one, RNase 3.2) were found to be present in human grey and white matter extracts and in purified myelin, but absent in human serum, peripheral nerve, liver, and spleen extracts. A RNase isoenzyme similar to central nervous system (CNS) RNase 3.2 was present in human kidney extracts but it differed in its carbohydrate structure. RNase isoenzymes 3.1 and 3.2 were not found in mouse, rat, and bovine brains. Thus, RNases 3.1 and 3.2 seem specific to human CNS. RNases of group 3 are the predominant RNase isoenzymes in CSF and one of the two predominant RNase groups in brain tissue. However, the proportion of RNases of group 3 is different in CSF and in brain extracts: RNases 3.1-3.2 are the major constituents of group 3 RNases in brain tissue, while another RNase isoenzyme of group 3, RNase 3.0, which is more glycosylated than RNases 3.1-3.2, is only a minor part of RNase of group 3 in brain extracts. Conversely, RNases 3.1-3.2 are lower or equivalent to RNase 3.0 in control CSF since the ratio of RNases 3.1-3.2 to RNase 3.0 did not exceed 1.0. This ratio decreased in pathological CSF including multiple sclerosis or infectious CNS diseases that were free of transudation phenomena. In conclusion, CSF RNases 3.1-3.2 seem to originate in brain tissue and could be markers of RNA catabolism from brain cells.
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PMID:Specific RNase isoenzymes in the human central nervous system. 344 Dec 68

A ribonuclease was isolated from serum-free supernatants of the human colon adenocarcinoma cell line HT-29. It was purified by cation-exchange and C18 reversed-phase high-performance liquid chromatography. The protein is basic, has a molecular weight of approximately 16,000, and has an amino acid composition that is significantly different from that of human pancreatic ribonuclease. The amino terminus is blocked, and the carboxyl-terminal residue is glycine. The catalytic properties of this ribonuclease resemble those of the pancreatic ribonucleases in numerous respects. Thus, it exhibits a pH optimum of approximately 6 for dinucleotide cleavage and employs a two-step mechanism in which transphosphorylation to a cyclic 2',3'-phosphate is followed by slower hydrolysis to produce a 3'-phosphate. It does not cleave NpN' substrates in which adenosine or guanosine is at the N position and prefers purines at the N' position. Like bovine ribonuclease A, the HT-29-derived ribonuclease is inactivated by reductive methylation or by treatment with iodoacetate at pH 5.5 and is strongly inhibited by the human placental ribonuclease inhibitor. However, in contrast, the tumor enzyme does not cleave CpN bonds at an appreciable rate and prefers poly(uridylic acid) as substrate 1000-fold over poly(cytidylic acid). It also hydrolyzes cytidine cyclic 2',3'-phosphate at least 100 times more slowly than uridine cyclic 2',3'-phosphate and is inhibited much less strongly by cytidine 2'-monophosphate than by uridine 2'-monophosphate. Other ribonucleases known to prefer poly(uridylic acid) were isolated both from human serum and from liver and were compared with the tumor enzyme. The physical, functional, and chromatographic properties of the serum ribonuclease are essentially identical with those of the tumor enzyme. The liver enzymes, however, differ markedly from the HT-29 ribonuclease. The potential utility of the tumor ribonuclease in the diagnosis of cancer is considered.
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PMID:Isolation and characterization of a human colon carcinoma-secreted enzyme with pancreatic ribonuclease-like activity. 346 90

Human placental ribonuclease inhibitor (PRI) abolishes both the ribonucleolytic activity of angiogenin toward 28S and 18S rRNA and its angiogenic activity on the chicken embryo chorioallantoic membrane. Treatment of the angiogenin-PRI complex with p-hydroxymercuribenzoate releases enzymatically active angiogenin. Assays measuring competition between angiogenin and bovine pancreatic ribonuclease A for PRI reveal that binding of the inhibitor to angiogenin is extremely tight, with a Ki value well below 0.1 nM. The stability of the angiogenin-PRI complex was assessed by cation-exchange HPLC quantitation of free angiogenin. No significant dissociation was detected after 17 hr at 25 degrees C in the presence of a large excess of bovine ribonuclease, which serves as a scavenger for free inhibitor. The results of these experiments, based on the predictive capacity of the angiogenin/RNase homology, suggest that PRI and related inhibitors may participate in the in vivo regulation of angiogenin and that this might have pharmacologic and/or therapeutic implications.
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PMID:Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin. 347 Jul 87

A single-strand-specific, nucleolar exoribonuclease from Ehrlich ascites tumor cells has been isolated and purified free from other nucleases. The exonuclease degraded single-stranded RNA processively from either a 5'-hydroxyl or a 5'-phosphorylated end and released 5'-mononucleotides. The enzyme digested single-strand poly(C), poly(U), and poly(A) equally well but did not degrade duplex poly(C).poly(I) or poly(A).poly(U). Less than 0.2% of duplex DNA or 1.5% of heat-denatured DNA was degraded under the conditions which resulted in greater than 26% degradation of RNA. The ribonuclease required Mg2+ (0.2 mM) for optimum activity and was inhibited by ethylenediaminetetraacetic acid but not by human placental RNase inhibitor. The native enzyme had a Stokes radius of 42 A and a sedimentation coefficient (S20,w) of 4.3 S. From these values, an apparent molecular weight of 76 000 was derived by using the Svedberg equation. The localization and unique mode of degradation suggest a role for the 5'----3' exoribonuclease in ribosomal RNA processing.
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PMID:Isolation and properties of a single-strand 5'----3' exoribonuclease from Ehrlich ascites tumor cell nucleoli. 620 56


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