Disease relevance of IGKV2-10

• Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding [1].
• By contrast, S11 and L7 ribosomal proteins were rarely associated with the ribosomes of colorectal epithilia except immature mucosal cells, whereas their expression levels were significantly enhanced in colorectal cancer cells [2].
• Upon stable transfection of L7 cDNA into Jurkat lymphoma cells two major proteins disappear, namely one nuclear protein and one which associates with the nucleus [3].
• Nucleic acid vaccination of Brucella abortus ribosomal L7/L12 gene elicits immune response [4].
• Characterization of eukaryotic protein L7 as a novel autoantigen which frequently elicits an immune response in patients suffering from systemic autoimmune disease [5].

High impact information on IGKV2-10

• Identification of a transcript that is down-regulated in senescent human fibroblasts. Cloning, sequence analysis, and regulation of the human L7 ribosomal protein gene [6].
• These results suggest that L7 can interfere with the translation of proteins which control cell cycle progression and/or the initiation of the apoptotic pathways [7].
• Treatment of the L7 transfectants with the inhibitor of translation cycloheximide, at doses which do not affect untransfected cells, enhances their sensitivity to the induction of apoptosis [7].
• In this report we show that the constitutive expression of protein L7 in Jurkat cells leads to an arrest in G1 of the cell cycle and induces apoptosis as a consequence of cell-to-cell contact [7].
• An antigen that is dependent on the glycose lacto-N-neotetraose induces IgG in humans that is bactericidal for L2, L3, L4, and L7 strains [8].

Biological context of IGKV2-10

• The L7/L12 gene of B. melitensis was amplified by PCR and subcloned in the Escherichia coli pQE30 plasmid [9].
• L7 protein is a coregulator of vitamin D receptor-retinoid X receptor-mediated transactivation [10].
• We also demonstrate that L7 repressed binding of VDR-RXR heterodimers to a vitamin D response element [10].
• Surprisingly, L7 recruited RXR to the same response element in the presence of 9-cis retinoic acid [10].
• Our data suggest, that protein L7 is a coregulator of VDR-RXR mediated transactivation of genes, that modulates transcriptional activity by interfering with binding of the receptors to genomic enhancer elements [10].

Anatomical context of IGKV2-10

• Utilizing rabbit anti-L7 serum, autoimmune sera and affinity-purified anti-L7 autoantibodies in immunoblotting, and rabbit and chicken anti-L7 antibodies in indirect immunofluorescence, we detect L7 protein in the nuclei and in the cytoplasm of various cell-lines [5].

Associations of IGKV2-10 with chemical compounds

• Furthermore, similar to the other higher eukaryote r-protein-encoding genes characterized so far, the human L7 alpha gene has a C as the major transcriptional start point localized in a pyrimidine-rich region and lacks a canonical TATA sequence [11].

Analytical, diagnostic and therapeutic context of IGKV2-10

• Anti-L7 autoantibodies belong to the IgG-class and detect specifically at least two epitopes on the L7 molecule, as shown by immunoprecipitation and immunoblotting [5].

References