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

Infusion of cycloheximide i.v., an antibiotic known to inhibit synthesis of protein, at a rate of 0.2 mg/kg/hr, reliably caused lysis of fever in 15 chronically febrile patients with Hodgkin's disease who did not have detectable bacterial, fungal, or viral infection. Antipyretic effects were also seen in some patients with reticulum cell sarcoma, lymphosarcoma, acute leukemia, histiocytic medullary reticulosis, plasma cell myeloma, carcinoma of the lung, and carcinoma of the cervix. The drug failed to produce defervescence in four patients with normal granulocyte reserves, who were febrile due to bacterial infection. When infused at a rate of 0.2 mg/kg/hr, the drug apparently caused an acute alteration of protein metabolism in man in that plasma amino acid nitrogen rose acutely while plasma levels of muramidase and ribonuclease fell during the period of the infusion. The data suggest that continuing synthesis of protein may be involved in nonbacterial fever of neoplastic disease. Mammalian granulocytes and monocytes are known to elaborate a pyrogenic protein following appropriate stimulation; it is suggested that in some types of neoplastic disease, particularly Hodgkin's disease, tumor cells may produce and release a pyrogenic protein and that drug-induced inhibition of its synthesis is responsible for the observed lysis of fever.
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PMID:Antipyretic effect of cycloheximide, and inhibitor of protein synthesis, in patients with Hodgkin's disease or other malignant neoplasms. 109 49

Regulation of the expression of the erythropoietin (Epo) receptor (EpoR) gene is under the control of transcriptional regulatory factor GATA-1. GATA-1 is expressed widely among the nonerythroid, factor-dependent subclones of the interleukin 3-dependent mouse cell line 32D. Consequently, to determine whether GATA-1 and EpoR gene expression are linked even in nonerythroid cells, we have studied the correlation of GATA-1 expression with expression and function of EpoR in these cell lines. EpoR mRNA (by RNase protection analysis) and EpoR protein (by specific antibody immunoprecipitation of metabolically labeled EpoR protein) were detectable not only in 32D and 32D Epo (an Epo-dependent subclone) but also in 32D GM, a subclone dependent for growth on granulocyte/macrophage colony-stimulating factor. EpoR mRNA also was detectable by PCR in 32D G, a subclone dependent for growth on granulocyte colony-stimulating factor. However, only 32D Epo cells bound 125I-labeled Epo and expressed EpoR protein on the cell surface, as determined by immunoprecipitation of surface-labeled proteins. These results indicate that, in these factor-dependent cell lines, the major regulatory step determining the erythroid-specific response to Epo is the efficiency of EpoR protein translocation to the cell surface. Mechanisms that could affect lineage-specific translocation are the presence of a chaperone protein, erythroid-specific editing of EpoR mRNA, or altered processing of the EpoR protein to the cell surface. In this model, lineage-restricted responses to growth factors such as Epo are determined not by expression of the genes for growth factor receptors but, rather, by appropriate processing of the receptor protein.
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PMID:Response to erythropoietin in erythroid subclones of the factor-dependent cell line 32D is determined by translocation of the erythropoietin receptor to the cell surface. 172 18

The presence, in granulocytes, of high levels of nuclease activity makes it difficult to isolate intact RNA from these cells. We have developed a method that allows purification of functional RNA from normal granulocytes as determined by capability for reverse transcription and in vitro translation. We have shown that a considerable amount of ribonuclease activity remains in granulocyte lysates, even after the addition of heparin or vanadyl ribonucleoside complexes. RNA isolated from such lysates demonstrates only minimal binding to oligothymidylic-cellulose and does not serve as a template for reverse transcription or in vitro translation. However, the extraction of frozen granulocytes into phenol in the presence of both heparin and vanadyl ribonucleoside allows the purification of relatively large quantities of RNA, which serves as an excellent template for reverse transcription and in vitro translation. Purification of granulocyte RNA by this method will facilitate study of granulocyte gene expression.
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PMID:Purification of functional RNA from human granulocytes. 257 34

A factor, termed neutrophil alkaline phosphatase-inducing factor (NAP-IF), that has the capacity to increase the NAP activity of granulocytes was characterized by using two samples: cystic fluid (CF) and conditioned medium of a tumor cell line (T3M5). The molecular weight of NAP-IF was shown to be between 13,000 and 45,000, and its isoelectric point was between 5.5 and 6.2. It was sensitive to heat and proteolytic enzymes, but was resistant to DNase and RNase, suggesting that NAP-IF is an acidic protein or glycoprotein. These characteristics of NAP-IF seem to be similar to those of granulocyte-macrophage colony-stimulating factor (GM-CSF) that is also present in the CF. NAP-IF rich fractions obtained by isoelectric focusing from CF were also found to be rich in a subclass of GM-CSF: granulocyte-CSF (G-CSF). Furthermore, a high correlation was noted between the activities of G-CSF and NAP-IF (gamma = 0.798, P less than 0.005). These results suggest that the two activities, i.e., G-CSF and NAP-IF, may be attributable to an identical macromolecule.
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PMID:Characterization of neutrophil alkaline phosphatase-inducing factor (NAP-IF). 387 40

Distribution of ribonuclease (RNAase), acid phosphatase (acid Ph-ase) and beta glucuronidase (BGU) between the granule, cytosol-soluble and post-granule fractions in normal human granulocytes and in granulocytes of chronic granulocytic leukemia (CGL) was studied. CGL granulocytes were found to display relative RNAase activity 1.2 times higher, relative acid Ph-ase activity 2.5 times higher than normal granulocytes. The granule fraction of CGL granulocytes showed 1.4 times higher relative RNAase activity but 0.87 times lower acid Ph-ase activity and the same BGU activity as normal granulocytes. On the other hand, the supernatant soluble fraction of CGL granulocytes showed 4.4 times higher relative RNAase activity, 1.2 times higher relative acid Ph-ase activity and BGU 2.2 times higher than in cytosol soluble fraction of normal granulocytes. Thus, cytosol soluble fraction of CGL granulocytes show a relative activity of the lysosomal enzymes studied which is remarkably higher than in normal granulocytes. The percentage distribution of RNAase, acid Ph-ase and BGU showed that CGL granulocytes contain only 36% of total RNAase activity versus 46% of that in normal ones. On the other hand, CGL granulocytes in cytosol soluble fraction will contain 48% of total RNAase versus 29% of total RNAase in cytosol of normal granulocytes. The isoenzyme profiles of RNAase of granule fractions were similar in normal and CGL granulocytes, while the RNAase isoenzyme profiles of cytosol fractions were different for normal and CGL granulocytes, indicating that some essential part of CGL granulocyte cytosol RNAase differs from RNAase contained in granules and in cytosol of normal granulocytes.
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PMID:Differences in distribution of ribonuclease isoenzymes in cytosol and granules in normal human granulocytes and in granulocytes of patients with chronic granulocytic leukemia (CGL). 620 Mar 92

Intranuclear inclusions were found in bone marrow cells of miniature pigs, whose ultrastructure and nature were examined by electron microscope and by cytochemical techniques. The inclusions were found predominantly in the granulocyte series and in a megakaryocyte and plasma cell. The inclusions consisted of closely packed, wavy filaments, 20-40 in number. They varied in size from 0.5-1.0 mum in length and 0.2-0.5 mum in width. The largest inclusion extended across the entire length of the nucleus. Occasionally, an inclusion extending toward the nuclear pore was observed. the intranuclear inclusions showed a tendency to appear frequently in immature granulocytes. The experiment on enzyme digestion for the epoxy sections showed that the inclusions were insoluble in RNase, DNase, pepsin, trypsin and protease solutions. These results seem to suggest that the intranuclear inclusions of blood cells differ from filamentous inclusions which have been noted previously in some neurons.
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PMID:Intranuclear inclusions in the bone marrow cells of miniature pigs. 627 12

Acid-acting (pH 6-7) (presumably lysosomal) ribonuclease and neutral-acting (pH 7-8) calcium-dependent phospholipase A2 (presumably the enzyme releasing arachidonic acid from membrane phospholipids) were demonstrated by the peroxidase-antiperoxidase (PAP) immunocytochemical technique in rabbit professional phagocytes: pulmonary alveolar macrophages (AM), oil-induced peritoneal exudate macrophages (M phi) and glycogen-induced peritoneal exudate polymorphonuclear granulocytes (PMN). All three cell types stained positively with antisera to purified rabbit lung RNase and purified rabbit granulocyte phospholipase A2. The RNase and phospholipase A2 were also demonstrated by the PAP technique in the activated macrophages and granulocytes present in tissue sections of tuberculous (BCG) lesions. The intensity of staining of these two enzymes in individual macrophages did not change appreciably as the BCG lesions developed and regressed, but there were more macrophages rich in both enzymes when the lesions reached their peak size at 21 days. When the anti-RNase serum was fractionated by immunoabsorbent chromatography, the anti-delta RNase serum fraction stained exudate M phi and PMN better than AM; and the anti-beta RNase fraction stained AM better than M phi and PMN. Similar to isolated phagocytes, tissue granulocytes stained best with the anti-delta fraction; and activated tissue macrophages stained best with the anti-beta fraction. Thus, macrophages and granulocytes contain two types of RNase, beta and delta; and the beta RNase is associated with macrophage activation.
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PMID:Immunocytochemical demonstration of rabbit ribonuclease and phospholipase A2 by the peroxidase-antiperoxidase technique in professional phagocytes (pulmonary alveolar macrophages and granulocytic and mononuclear peritoneal exudate cells) and in glycol methacrylate sections of dermal tuberculous (BCG) lesions. 636 Dec 53

The activities of serum acid ribonuclease (RNase) were determined in patients with malignant neoplasm or with renal failure. The levels were markedly increased in myelogenous leukemia and renal failure, and only slightly increased in solid cancers, lymphoid malignancies and multiple myeloma. These increases correlated significantly with serum LDH activity in myelogenous leukemia and with creatinine levels in other malignancies or renal failure. The acid RNase content of granulocytes was 22.7-fold higher than that of lymphocytes. The increase of serum acid RNase may suggest an increased granulocyte destruction in myelogenous leukemia and a reduced glomerular filtration in other malignant neoplasms and renal failure.
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PMID:Activities of serum acid ribonuclease in patients with malignant neoplasms or with renal failure. 658 Sep 78

P-815 mastocytoma cells from DBA/2 mice and a 3-methylcholanthrene-induced fibrosarcoma from C57BL/6 mice produced in culture at least two soluble anti-inflammatory factors that inhibited macrophage accumulation in vivo when the factors were injected sc into syngeneic recipients. One factor was a low-molecular-weight peptide (less than 1,000), as judged by ultrafiltration, failure of extraction by lipid solvents, nonsusceptibility to DNase or RNase, partial inactivation by trypsin, and complete inactivation by carboxypeptidase B. The second anti-inflammatory factor had a molecular weight between 30,000 and 100,000 and was also not extractable with lipid solvents. Production of anti-inflammatory factors by P-815 mastocytoma cells was inhibited by cycloheximide and cell irradiation but not by colchicine pretreatment of the cells, suggesting a relationship to protein synthesis rather than cell growth. Soluble anti-inflammatory factors depressed granulocyte as well as macrophage responses. Anti-inflammatory factors were not found in supernatants from cultures of splenocytes, peritoneal exudate cells, or murine lung fibroblasts.
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PMID:Characterization of anti-inflammatory factors produced by murine tumor cells in culture. 681 63

The cooperation of specific and nonspecific factors of humoral immunity in the regulation of granulocyte locomotion was studied. Bacterial antigens of dental plaque, immunoglobulins, lysozyme, peroxidase, ribonuclease and trypsin were found to moderately stimulate chemotaxis and granulocyte chemokinesis. Of these, the most pronounced chemotactic effect is induced by ribonuclease and chemokinetic one by lysozyme. The strongest chemotactic stimulus is generated during activation of complement by the classical pathway. Production of the complement chemotactic factor by the classical pathway was dramatically increased by lysozyme and decreased by ribonuclease and trypsin. The treatment of granulocytes with antimicrobial enzymes diminishes their susceptibility to the chemotactic factor.
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PMID:[Cooperation of antigens, immunoglobulins, complement and antimicrobial enzymes in the regulation of blood granulocyte locomotion]. 737 68


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