Disease relevance of Rnase1

• METHODS: After induction of trinitrobenzene sulfonic acid (TNBS) colitis in SJL/J mice, plasma hormone and cytokine levels were measured, adrenal structure was analyzed by immunohistochemistry and electron microscopy, and adrenal cytokine/cytokine receptor expression were studied by RNase protection [1].
• When the truncated RNase was stably expressed to high levels in murine cells, it prevented specific rRNA cleavage in response to 2-5A transfection and the cells were unresponsive to the antiviral activity of interferon alpha/beta for encephalomyocarditis virus [2].
• Characterization and mapping of RNase T1-resistant oligonucleotides derived from the genomes of Akv and MCF murine leukemia viruses [3].
• To assess if Tat can carry other molecules into cells, we chemically cross-linked Tat peptides (residues 1-72 or 37-72) to beta-galactosidase, horseradish peroxidase, RNase A, and domain III of Pseudomonas exotoxin A (PE) and monitored uptake colorimetrically or by cytotoxicity [4].
• Northern blot hybridization and RNase protection assay revealed that Cart-1 RNA was present at high levels in a well-differentiated rat chondrosarcoma tumor and in a cell line derived from this tumor [5].

High impact information on Rnase1

• We have now used an RNase protection assay that can distinguish between H19 alleles in four subspecies of Mus, to demonstrate that the H19 gene is parentally imprinted, with the active copy derived from the mother [6].
• RNase mitochondrial RNA processing correctly cleaves a novel R loop at the mitochondrial DNA leading-strand origin of replication [7].
• A partial cDNA encoding AP-2 was isolated from a mouse embryo cDNA library and used to prepare probes to measure AP-2 mRNA levels by RNase protection and RNA in situ hybridization [8].
• For two unrelated model antigens (RNase and horseradish peroxidase), we found that only the less digestible forms were immunogenic, inducing far more efficient T cell priming and antibody responses [9].
• T cell lineage choice and differentiation in the absence of the RNase III enzyme Dicer [10].

Chemical compound and disease context of Rnase1

• Using RNase protection assay for screening of the melanoma progression profile, and Western blotting for subsequent result validation, we looked for molecular progression markers affected by melanoma histamine secretion [11].
• We have extensively purified from Krebs II ascites cells, although not until homogeneity, a ribonuclease which preferentially cleaves natural or synthetic double-stranded RNA substrates (RNase D); this specificity is also supported by its sensitivity to inhibition by 10(-5) M ethidium bromide [12].
• Polyacrylamide gel electrophoretic analysis of the RNase-treated 40S structure revealed at least three viral structural proteins in the same ratio as was present in the intact virions [13].
• Lipopolysaccharide (LPS) of Burkholderia cepacia was purified by the conventional phenol-water extraction method (preparation BcLPS-1), followed by enzymatic treatments with DNase, RNase, trypsin, and proteinase K (preparation BcLPS-2), and finally by deoxycholate-phenol-water extraction (preparation BcLPS-3) [14].
• Poly ADP-ribosylation of two mouse lymphoma cell lines, L5178Y (LS) and the radiation and alkylating agent resistant derivative AII, was investigated by uptake of [3H]NAD by permeabilised cells into acid-precipitable material that was sensitive to phosphodiesterase but insensitive to DNase and RNase [15].

Biological context of Rnase1

• The results indicated that the gene coding for pancreatic ribonuclease (Rib-1) can be assigned to mouse chromosome 14 [16].
• This study was performed to map the tissue distribution and to quantify the 3 receptor isoforms by heterologous competitive Reverse Transcriptase-Polymerase Chain Reaction (RT-PCR) and RNase Protection Assay (RNase PA) [17].
• Expression of IGF-I mRNA was identified by both RNase protection assay and reverse transcription/polymerase chain reaction [18].
• Expression of the lacZ transgene was assayed by measuring beta-galactosidase enzyme activity in fetal liver extracts, the levels of which correlated with the quantity of lacZ mRNA determined using RNase protection assays [19].
• Antisense RNA complementary to exons 3 and 7, which correspond to the inverted segment, was detected by RNase protection studies [20].

Anatomical context of Rnase1

• Analysis of the congenic strain B10.D2(57N)Sn confirmed this assignment and indicated that Rib-1 is closely linked to the genes encoding the T-cell receptor alpha subunit (Tcra) and nucleoside phosphorylase-2 (Np-2) [16].
• Rib-1 transcripts were detected in parotid gland as well as in pancreas [21].
• Onconase is a 12 kDa protein homologous to pancreatic RNase A isolated from amphibian oocytes which shows cytostatic and cytotoxic activity in vitro, inhibits growth of tumors in mice and is in phase III clinical trials [22].
• METHODS: TRAIL and TRAIL-receptor expression were analyzed in normal, inflammatory ileum/colon and human intestinal epithelial cell (IEC) lines (HIEC), Caco-2, and HT-29 using RNase protection assay, real-time and reverse-transcription polymerase chain reaction (RT-PCR), immunohistochemistry, and Western blot analysis [23].
• Furthermore, apoptosis was substantially suppressed in RNase L-/- thymocytes and fibroblasts treated with different apoptotic agents [24].

Associations of Rnase1 with chemical compounds

• These nuclear synaptonemal complex-matrices are prepared by extracting Triton X-100-treated nuclei with low (0.2 M) and high (1.0 or 2.0 M) NaCl, DNase I, and RNase A to remove 85% of the nuclear proteins, 97% of the RNA, and 99% of the DNA [25].
• The data indicate that no reiteration can be detected by RNase or by hydroxylapatite for the genes corresponding to the entire sequence of MOPC 41 L-chain mRNA, including the untranslated segments, within the limits of detectability of short reiterated segments [26].
• Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase [27].
• RNase protection and primer extension analyses revealed a single transcriptional start site located 299 bp upstream from the translational start site in an initiator-like pyrimidine-rich sequence [28].
• RNase protection assays demonstrated that Epo or dimethyl sulfoxide induction increased steady-state mRNA levels 10- to 20-fold after 24 to 48 hours [29].

Physical interactions of Rnase1

• The reassociation of the 4-5 S receptor to form the 8 S complex is inhibited by RNase [30].

Regulatory relationships of Rnase1

• Chemokine gene expression in accepted and rejected allografts and appropriate control specimens was determined by a multiprobe RNase protection assay system [31].
• The presence of point mutations in the K-ras gene was examined in murine thymic lymphomas induced by a single dose of N-methylnitrosourea by the RNase A mismatch cleavage method and by allelic-specific oligonucleotide hybridization of in vitro amplified DNA by polymerase chain reaction [32].
• In C2C12 cells RNase protection assays revealed the M promoter is induced within 24 hr of the onset of myogenic differentiation, and both M- and H-specific mRNAs accumulate over 5 days in culture [33].
• One of the RNase 1 genes of R. norvegicus is expressed in the pancreas [34].

Other interactions of Rnase1

• This and other evidence suggests that the RNase A superfamily originated from an RNase 5-like gene and expanded in mammals [35].
• The data suggest that Rib-1 is transcribed in pancreas and parotid from the same promoter [21].
• Three PurBPs of 35, 38 and 40 kDa were found mostly in the nuclear extract (N.Ext.) and they were not detected by the pretreatment of N.Ext. with trypsin, but not with RNase or DNase [36].
• DSG3 -/- mice had no DSG3 mRNA by RNase protection assay and no Dsg3 protein by immunofluorescence (IF) and immunoblots [37].
• In this study, we have used an RNase protection assay to demonstrate that IL-4 induces expression of germ-line gamma 1 transcripts in B cells within 4 hr of culture; induction is dose-dependent and is inhibited by interferon gamma [38].

Analytical, diagnostic and therapeutic context of Rnase1

• In shiverer adult, K+ channel expression is up-regulated in both axons and glia, as revealed by immunocytochemistry, RNase protection, and in situ hybridization studies [39].
• A null mutation was confirmed by Southern blotting, RNase protection assay, immunohistochemistry, and flow cytometry [40].
• Mouse c-myb gene transcripts in various cells of haemopoietic origin were analysed using S1 nuclease and RNase mapping techniques and by Northern blotting [41].
• Evidence that the normal growth factor coding sequence was unaltered derived from RNase protection studies and immunoprecipitation analysis [42].
• Several neomycin-resistant clones were analyzed for H-2Kb and H-2Db expression by RNase protection and flow cytometry assays [43].

References