Disease relevance of SPATA1

• In immunoperoxidase assays, SP-2 reacted with 81 of 90 specimens of human breast cancer [1].
• Hybridomas were generated by fusing SP2/0 mouse myeloma cells with spleen cells from mice that had been immunized with cultured human melanoma cells [2].
• DESIGN: Two cross-sectional HIV seroprevalence sample surveys (SP-1 and SP-2) of drug users, including IDU at various stages of treatment [3].
• This information is relevant to the understanding of abnormal spermatogenesis associated with infertility and to germ cell tumors in adult life [4].
• Higher-titered neutralizing antibody responses to HTLV-I (1:10 to 1:640) were detected with pseudotype and syncytium inhibition assays in four goats immunized with a combined inoculum containing peptides SP-2, SP-3, and SP-4A linked to tetanus toxoid [5].

High impact information on SPATA1

• BP/SP-1 and BP/SP-2 were assigned to rat chromosomes 10 and X, respectively [6].
• Linkage studies in crosses between the stroke-prone spontaneously hypertensive rat and the normotensive control strain Wistar-Kyoto have led to the localization of two genes, BP/SP-1 and BP/SP-2, that contribute significantly to blood pressure variation in the F2 population [6].
• This membrane antigen has been defined by a monoclonal antibody raised by the fusion of SP 2/0-Ag14 myeloma cells with spleen cells from mice immunized with myotubes derived from the myogenic E63 line [7].
• Spleen cells from mice immunized with a 0.15 M NaCl extract of synchronized mitotic HeLa cells were fused with SP2/0-Ag14 mouse myeloma cells, and hybrids were selected in medium containing hypoxanthine, methotrexate, thymidine, and glycine [8].
• After cloning by limiting dilution, the cell lines (designated SP2/0-4A5, P3-8C8, SP2/0-8D3, and SP2/0-9A7) were expanded into suspension culture [9].

Chemical compound and disease context of SPATA1

• The authors developed the first rabbit anti-PgR mAb (clone SP2) used in IHC on formalin-fixed, paraffin-embedded tissue sections from breast carcinomas [10].

Biological context of SPATA1

• Two large compound chimeric vectors each containing the genetic information to produce a single antibody specificity were sequentially electroporated into the murine nonsecreting hybridoma SP2/0 [11].
• Bone mineral density was measured using Lunar SP2 and DP3 densitometers [12].
• Plasmids containing the IgG1 (or IgG4) heavy chain and the kappa L chain were cotransfected into SP2/0 mouse myeloma cells [13].
• Peptides SPwt and SP-2 but not SP-3 or SP-4 were able to promote lipid mixing as assessed by fluorescence energy transfer assay and dye leakage in a vesicle leakage assay [14].
• When a relevant immune response was obtained for antibody affinity and specificity, hybridization of spleen activated lymphocytes with SP2/O/Ag myeloma cells was performed [15].

Anatomical context of SPATA1

• Splenic lymphocytes, derived from two male Lewis rats expressing serum antireceptor activity after repeated immunization with a partially purified preparation of this protein, were fused with two nonsecreting murine myeloma cell lines, SP2/0-Ag14 and P3-X63-Ag8.653 [9].
• The genes encoding the murine heavy and light chain variable regions of the MOv18 and MOv19 MAbs were cloned from the parental hybridomas, fused with genes encoding the human heavy (gamma 1) and light (kappa) chain constant regions, respectively, and expressed in the SP2/0 murine myeloma cell line [16].
• Disruption of an SP2/KLF6 Repression Complex by SHP Is Required for Farnesoid X Receptor-induced Endothelial Cell Migration [17].
• Growth of the murine B-lymphocyte cell line CC9C10 and the myeloma SP2/0 was enhanced significantly by the presence of the unsaturated fatty acids, oleic and linoleic acids in serum-free culture [18].
• LOU/CN rats were immunized with 3F8 and their spleens were used in somatic-cell hybridization, using SP2/0, P3 and Y3 as fusion partners [19].

Associations of SPATA1 with chemical compounds

• Antibody-induced alterations in the sedimentation pattern of the native 1,25-(OH)2D3 receptor, coupled with Ouchterlony double-diffusion techniques, indicate that SP2/0-4A5 secretes an IgG2a, SP2/0-9A7 produces an IgG2b, and P3-8C8 secretes an IgG [9].
• The calcium ionophore A23187 markedly stimulated production of SP-1 and SP-2 [20].
• Formation of SP-1 and SP-2 was inhibited by storage at 4 degrees C as well as by treatment of the concentrates with leupeptin, N-ethylmaleimide, and EDTA; DFP and PPACK had no effect [20].
• Replacement of all lysine residues in only one of the domains had minor effects on virus release, while cumulative mutations in NC and SP2 or in NC and p6 resulted in an accumulation of late budding structures, as observed by electron microscopy analysis [21].
• To directly address the function of Gag ubiquitination, we constructed Gag variants in which lysine residues in the NC, SP2, and p6 domains were mutated to arginine either in individual domains or in combination [21].

Other interactions of SPATA1

• It is possible that the underlying cause in decreased spermatogenesis associated with both an elevated FSH and a decreased transferrin concentration is impaired Sertoli cell function [22].

Analytical, diagnostic and therapeutic context of SPATA1

• Blood supply as measured by cold challenge plethysmography ('Medimatic SP2') was also improved by CL115,347, as were hand temperatures [23].
• Two-dimensional peptide mapping and amino acid sequencing identified SP-1 and SP-2 as fragments of actin formed by cleavage on the N-terminal side of residues Thr-106 and Ala-114, respectively [20].
• The gene constructs were introduced by electroporation into SP2/0, a non-Ig-producing murine myeloma [24].
• Small interference RNA-based silencing studies in combination with promoter, gel shift, and chromatin immunoprecipitation assays indicate that SP2 and KLF6 bind to the matrix metalloproteinase-9 promoter and together function to maintain this gene in a silenced state [17].
• We measured the nasal conductance in response to increasing doses of SP 2 h after oral administration of either placebo or the ACE inhibitor, cilazapril (5 mg), or the NEP inhibitor, acetorphan (300 mg), given in a randomized, double-blind, cross-over manner [25].

References