Disease relevance of IGKV2D-30

• The gonococcus and meningococcus, which infect human mucosal surfaces, elaborate a highly specific proteolytic enzyme which cleaves the immunoglobulin A1 subclass of the principal mucosal antibody, immunoglobulin A (IgA) [1].
• Greater impetus still was given by the discovery that mutations in the gene encoding the ATP-binding cassette transporter, class A1 (ABCA1) are the cause of Tangier disease, a rare recessive disorder with near-absent plasma HDL [2].
• Selective deposition of immunoglobulin A1 in immunoglobulin A nephropathy, anaphylactoid purpura nephritis, and systemic lupus erythematosus [3].
• J-chain expression is more prominent in immunoglobulin A2 than in immunoglobulin A1 colonic immunocytes and is decreased in both subclasses associated with inflammatory bowel disease [4].
• Tissue typing showed homozygosity of HLA A1, B8, DR3, the haplotype associated with IgA deficiency in healthy people [5].

High impact information on IGKV2D-30

• Entry of cholera toxin into polarized human intestinal epithelial cells. Identification of an early brefeldin A sensitive event required for A1-peptide generation [6].
• Polymorphism in a DNA sequence has been observed on the 3'-flanking region of the human apoprotein-A-1 gene [7].
• Elements of the maize A1 promoter required for transactivation by the anthocyanin B/C1 or phlobaphene P regulatory genes [8].
• In maize flavonoid biosynthesis, the A1 gene is independently regulated in the anthocyanin and phlobaphene pathways [8].
• Molecular polymorphism and epidemiology of Neisseria meningitidis immunoglobulin A1 proteases [9].

Chemical compound and disease context of IGKV2D-30

• In lung cancer, we have evaluated the expression and cellular localization of several members of the hnRNP family, hnRNP A1, A2, B1, C1, C2 and K [10].
• The immunoglobulin A1 proteinase from Streptococcus pneumoniae is inhibited by tetracycline compounds [11].

Biological context of IGKV2D-30

• The N and A1 domains show 45% and 51% amino acid sequence identity with the corresponding domains of the three CEA family members whose sequences have been determined [12].
• Two black blood samples with phenotype A2B contained A1-enzyme, but not A2-enzyme, and exhibited several times higher B-enzyme activity than control AB and B blood [13].
• Binding sites for high molecular weight kininogen (HK) and for factor XIIa are present in the Apple 1 (A1) and the A4 domains of factor XI, respectively [14].
• These results suggest that perturbations in RNA splicing mechanisms may contribute to malignant transformation and provide direct evidence that the A1 protein is not required for cell growth [15].
• Platelet adhesion to damaged vessel wall and shear-induced platelet aggregation necessitate binding of the von Willebrand factor (VWF) A1 domain to platelet GPIbalpha [16].

Anatomical context of IGKV2D-30

• In these two cases, therefore, the A2 character was not caused by the subactive A2-enzyme, but because of an insufficient formation of the A-substances in red cell membranes presumably caused by the competition between the A1-enzyme and the super active atypical B-enzyme at the common H-sites [13].
• In one erythroleukemia cell line, A1 expression was undetectable as a result of F-MuLV integration in one allele and loss of the other allele [15].
• We indeed observed a lower level of hnRNP A1 in in vitro HTLV-1-transformed virus-producing T cells than that detected in Jurkat cells [17].
• Furthermore, A1 proteins from Jurkat cells were acting in a concentration-dependent manner, suggesting that the amount of these RNA-binding proteins is a critical parameter in controlling Rex activity [17].
• Monocyte-derived dendritic cells infected with a recombinant canarypoxvirus (ALVAC) containing the entire MAGE-A1 gene were used to stimulate CD8+ T lymphocytes from the blood of individuals without cancer [18].

Associations of IGKV2D-30 with chemical compounds

• The His563Arg, Ile566Leu, and Asp570Ala mutations also impaired the binding of heparin, which competes with AJvW-2 for binding to A1 [16].
• The number of ADP-ribose moieties incorporated into ech A1 peptide was dependent on incubation conditions and time as well as toxin concentration [19].
• The formation of mono- and multi-(ADP-ribosylated) A1 peptides was prevented by the addition of arginine, an alternative ADP-ribose acceptor [19].
• The mono- and multi-(ADP-ribosylated) A1 peptides catalyzed the NAD-dependent ADP-ribosylation of arginine methyl ester [19].
• Triton X-100 polyacrylamide gel electrophoresis separated the A1 peptide of choleragen from the B complex and multi-(ADP-ribosylated) A1 peptides from unmodified A1 [19].

Analytical, diagnostic and therapeutic context of IGKV2D-30

• OBJECTIVE: To determine whether levels of HDL are associated with viral load response in HIV-treated patients, and to seek an explanation based on amino acid sequence similarity between the key apolipoprotein A1 and HIV proteins concerned in viral replication [20].
• In addition, nested RT-PCR analysis revealed the mRNA expression of Eph A1, one of the representative receptors for ephrin A1, in human blastocysts obtained from patients undergoing in vitro fertilization treatment [21].
• Purification, properties and extended solution structure of the complex formed between human immunoglobulin A1 and human serum albumin by scattering and ultracentrifugation [22].
• METHODS: Oligonucleotide primers based on the cytochrome P450 L1 A1 demethylase gene were used to successfully amplify by PCR a single 1.0-kb and a single 500-bp DNA fragment from C. albicans, C. tropicalis, C. krusei, C. glabrata, C. parapsilosis, and C. pelliculosa genomic DNA [23].
• Sequence analysis of selected clones revealed that one of the cDNAs encoded porcine apolipoprotein (apo) A-1 [24].

References