Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.64 (MPP)
 1,876 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Drosophila Crumbs (Crb), Stardust (Sdt), Discs large (Dlg), Scribble (Scrib) and Lethal giant larvae (Lgl) are involved in the establishment and the maintenance of apicobasal polarity in epithelial tissues. Because epithelial polarity is disrupted in tumors, human homologs of Drosophila crb, sdt, dlg, scrib, and lgl are potential cancer-associated genes. MPP1/EMP55, MPP2, MPP3, MPP4, MPP5/PALS1 and MPP6/PALS2 genes are human homologs of Drosoplila sdt. Here, we identified and characterized a novel member of MPP gene family, MPP7, by using bioinformatics. Uncharacterized FLJ32798 cDNAs (BC038105 and AK057360) were derived from human MPP7 gene. BC038105 was a representative MPP7 cDNA, while AK057360 was an aberrant MPP7 cDNA with a frame shift. Human MPP7 mRNA was expressed in placenta, brain, testis as well as in uterus tumor, bladder tumor, and lymphoma. Microsatellite marker D10S588, linked to IDDM and hereditary thrombocytopenia, was located within the MPP7 gene at human chromosome 10p12.1. Nucleotide sequence of mouse Mpp7 cDNA was determined in silico by assembling 3'-truncated cDNA AK078849, genome clone RP24-255J24, and EST AV260217. Human MPP7 showed 92.9% total-amino-acid identity with mouse Mpp7, and 75.7% total-amino-acid identity with zebrafish humpback. MPP7 orthologs were MAGUK proteins with two L27 domains, PDZ domain, SH3 domain, and GuKc domain. MPP7 was most related to MPP3 among MPP family members, functioning as adopter molecules assembling Crb homologs (CRB1, CRB3), Dlt homologs (INADL/PATJ, MPDZ/MUPP1), and Lin-7 homologs (LIN7A, LIN7B, LIN7C). This is the first report on identification and characterization of human MPP7 and mouse Mpp7 genes.
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PMID:Identification and characterization of human MPP7 gene and mouse Mpp7 gene in silico. 1471 43

Toxicity to o-sec-butylphenyl methylcarbamate compound (BPMC) was analyzed in the rice brown planthopper, Nilaparvata lugens, using a differential proteomics approach of identifying proteins on two dimensional-polyacrylamide gel electrophoresis (2D-PAGE). Proteome analysis from BPMC-treated brown planthopper resulted in the modulation of 22 proteins at the expression level as compared to control samples on coomassie brilliant blue (CBB) stained gels. Out of total 22 proteins, 10 proteins showed elevated expression, eight proteins showed decreased expression and four proteins showed specific expression after insecticide treatment. The N-terminal sequences of seven out of 22 proteins were determined by a gas-phase protein sequencer. The internal amino acid sequences of the 15 proteins were determined by the sequence analyses of peptides obtained by Cleveland peptide mapping method and were compared with those of the known proteins available in public databases and the EST database of the brown planthopper in our laboratory to understand the nature of the proteins. Sequence analyses revealed that the expression of putative serine/threonine protein kinase, paramyosin, HSP 90, beta-tubulin, calreticulin, ATP synthase, actin and tropomyosin was elevated, and that of beta-mitochondrial processing peptidase, dihydrolipoamide dehydrogenase, enolase and acyl-coA dehydrogenase was reduced due to the exposure of BPMC. The differential expression of these proteins reflects the overall change in cellular structure and metabolism after insecticide treatment.
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PMID:Proteomic analysis of brown planthopper: application to the study of carbamate toxicity. 1511 Aug 63