Disease relevance of Ivns1abp

• A novel 6:10 chromosomal translocation in the murine plasmacytoma NS-1 [1].
• Inhibition of respiratory syncytial virus infection with intranasal siRNA nanoparticles targeting the viral NS1 gene [2].
• A quantitative assay of the suppressor tRNA activity in these mammalian cells is described; it is based on the amount of tRNA-mediated readthrough of a terminating codon in the influenza virus NS1 gene after the cells are infected with virus [3].
• Expression of the 6C3 antigen on murine hematopoietic neoplasms. Association with expression of abl, ras, fes, src, erbB, and Cas NS-1 oncogenes but not with myc [4].
• The v-cbl oncogene is the transforming gene of the murine Cas NS-1 retrovirus which induces pre-B cell lymphomas and myeloid leukaemias [5].

High impact information on Ivns1abp

• Here we describe a novel 6:10 chromosomal translocation in the murine plasmacytoma cell line NS-1 which juxtaposes the immunoglobulin Ck gene with a single-copy sequence of unknown function [1].
• The NS-1 plasmacytoma is a frequently used fusion partner in hybridoma production and is known to contain a rearranged c-myc gene and a genetic element which transforms normal mouse fibroblasts in DNA-mediated transfection assays [1].
• Using lymphocytes from regional lymph nodes, peripheral blood and tumor infiltrates, 158 fusions were performed with SKO-007 (human myeloma line), LICR-LON-HMy2 (LICR-2), GM 4672 (human lymphoblastoid lines), or NS-1 (mouse myeloma line) [6].
• This antibody (anti-PAA) was produced by the fusion of myeloma cells NS-1 with spleen cells from a BALB/c mouse, which were sensitized with activated human T-cells generated by allogeneic stimulation in mixed-lymphocyte culture (MLC) [7].
• However, #71295 was not found in NS-1, D14, and BALB/c normal thymus, liver, colon, and kidney tissues [8].

Chemical compound and disease context of Ivns1abp

• Splenic lymphocytes of BALB/c mice immunized with a glycoprotein-enriched fraction of human ovarian adenocarcinoma were fused with the mouse myeloma cell line P3/NS1/1-Ag4 in the presence of polyethylene glycol (Mr 4,000) [9].
• A hybridoma produced by the polyethylene glycol fusion of the NS-1 variant of the P3x63Ag8 BALB/c plasmacytoma to splenocytes harvested from a BALB/c mouse immunized with whole gonococci was found to be producing antibody to a common region on gonococcal lipopolysaccharide (LPS) [10].
• Using an SV40-based expression system, we previously analysed dimerization and secretion of the NS1 protein of dengue virus type 2 (DEN-2) with mutations in the conserved Cys residues, or within hydrophilic or hydrophobic regions, or at glycosylation sites [11].
• However, previous work has reported that substitution of a conserved proline by leucine at residue 250 in NS1 of Kunjin virus (KUNV) eliminated dimerization, but allowed virus replication to continue [12].
• Thus, Nd1-L plays a critical role in protecting the heart from doxorubicin-induced cardiomyopathy [13].

Biological context of Ivns1abp

• Overexpression of Nd1-L in NIH3T3 cells delayed cell growth by affecting the transition of cytokinesis [14].
• These results suggest that Nd1-S may play a role in cell cycle progression in the nucleus [15].
• We characterized the genomic organization of the Nd1 gene, and found that Nd1-L and Nd1-S consist of 16 and nine exons respectively, and that exons I-VIII are shared between them [16].
• Spleen cells of (BAB/ 25 X AKR/J) F1 mice, immunized with dansyl-keyhole limpet hemocyanin (DNS-KLH), were hybridized with NS-1 to generate hybridomas producing monoclonal anti-DNS antibodies of either the b or d haplotype of the BAB/25 or AKR/J parent, respectively [17].
• The KUN viral cDNA encoded in the plasmid contained the mutation in the NS1 protein (Pro-250 to Leu) previously shown to attenuate KUN virus in weanling mice [18].

Anatomical context of Ivns1abp

• Nd1-L colocalizes with actin filaments detected using a confocal microscope, and its kelch repeats bind to them in vitro [14].
• These data suggest that Nd1-L functions as a stabilizer of actin filaments as an actin-binding protein and may play a role in the dynamic organization of the actin cytoskeleton [14].
• PEMM stimulated with poly I . poly C destroyed allogeneic tumor cells (NS-1) when separated by cell-impermeable Millipore filters in vitro; in contrast, PEMM not stimulated with poly I . poly C were incapable of lysing targets when separated by membranes [19].
• Thioglycollate-elicited C57BL/6 peritoneal exudate macrophage monolayers (PEMM) stimulated with poly I . poly C or LPS released a macrophage cytotoxin (MCT) that rapidly bound to syngeneic (EL 4) or allogeneic (NS-1, YAC-1) tumor cells but did not bind to normal splenocytes [19].
• A monoclonal antibody designated anti-Cl was obtained from a hybridoma clone isolated from a fusion of NS1 myeloma with spleen cells from BALB/c mice injected with homogenate of white matter from bovine corpus callosum [20].

Associations of Ivns1abp with chemical compounds

• Spleen cells of C57BL/6 mice immunized with a highly tumorigenic, chemically induced murine cultured colon 36 tumor (C-C36) of BALB/c origin were hybridized with NS-1, a hypoxanthine phosphoribosyltransferase-deficient myeloma line of BALB/c mice [8].
• A preliminary probe of the benzyl derivative of vitalethine in a myeloma model (NS-1) suggests efficacy (100% survival) as well [21].
• In one series of experiments, the growth response of NS-1 cells to several of the intermediates of cholesterol biosynthesis was studied in serum-free medium [22].
• The major labelled sterol product (greater than 80%) in NS-1 cells after a 24-h exposure to [2-14C]acetate was lanosterol [22].
• These mutations ablated (i) the TBEV pre-M cleavage site, (ii) the TBEV E glycosylation site, or (iii) the first DEN4 NS1 glycosylation site [23].

Analytical, diagnostic and therapeutic context of Ivns1abp

• Western blot analysis showed that a monoclonal antibody against recombinant mouse CD14 (mCD14), designated rmC5-3, specifically reacted with mouse macrophage cell line J774, but not myeloma cell line NS1 [24].
• Southern blot analysis of PstI-digested DNA indicated that in contrast to the parental NIH/3T3 transformed cell lines (pT, T12N/5a, NS-1) all the nude-passaged immunogenic variants (pT-nude, T12N/5a-nude, NS-1-nude) contained newly acquired ecotropic-related proviruses [25].
• Immunoprecipitation and SDS-PAGE analysis identified 20.5- and 18-kDa proteins with mAb H1-229 or H2-439, respectively, in cellular extracts of 125I-surface labeled NS-1 transfected with the corresponding genes [26].
• By site-directed mutagenesis, we showed that this residue is essential for NS1 helicase activity but not promoter regulation, suggesting a possible modulation of NS1 functions by PKClambda phosphorylation at residue S473 [27].
• Thus, because of its T-cell immunogenicity and antigenic simplicity, the NS1 delivery system could serve as a priming agent for heterologous prime-boost vaccination regimens [28].

References