Abstract
Information technology has greatly speeded up the discovery in biomedical research. However, most of the modern biomedical scientists are not familiar with the new technology. To overcome the difficulty, an intelligent information system is needed to help scientists in designing and conducting research projects. Previously, we have designed a static knowledge management system for the LARGE-like glycosyltransferase, a novel GlcNAc transferase involved in human diseases such as muscular dystrophy and human meningioma, by integrating data from public databases. According the characteristics of protein structure of LARGE protein family members include an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif and a putative catalytic domain with the conserved aspartate-any residue-aspartate motif and a conserved protein structural domain. In this paper, we have described an intelligent information system for the LARGE-like GlcNAc Transferase Database, by setting up an automatic updating databank for genes of the LARGE family and by integrating several bioinformatics tools which can identify characteristics structural domains of the protein family.
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Abbott KL, Aoki K, Lim JM, Porterfield M, Johnson R, O’Regan RM, Wells L, Tiemeyer M, Pierce M (2008a) Targeted glycoproteomic identification of biomarkers for human breast carcinoma. J Proteome Res 7(4):1470–1480
Abbott KL, Nairn AV, Hall EM, Horton MB, McDonald JF, Moremen KW, Dinulescu DM, Pierce M (2008b) Focused glycomic analysis of the N-linked glycan biosynthetic pathway in ovarian cancer. Proteomics 8(16):3210–3220
Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA (2007) The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol 25:21–50
Barresi R, Michele DE, Kanagawa M, Harper HA, Dovico SA, Satz JS, Moore SA, Zhang W, Schachter H, Dumanski JP, Cohn RD, Nishino I, Campbell KP (2004) LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies. Nat Med 10(7):696–703
Busch C, Hofmann F, Selzer J, Munro S, Jeckel D, Aktories K (1998) A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J Biol Chem 273(31):19566–19572
Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res 37:D233–D238
Coutinho PM, Deleury E, Davies GJ, Henrissat B (2003) An evolving hierarchical family classification for glycosyltransferases. J Mol Biol 328(2):307–317
Gerstein M (2000) Integrative database analysis in structural genomics. Nat Struct Biol 7(Suppl):960–963
Grewal PK, Hewitt JE (2002) Mutation of Large, which encodes a putative glycosyltransferase, in an animal model of muscular dystrophy. Biochim Biophys Acta 1573(3):216–224
Grewal PK, Holzfeind PJ, Bittner RE, Hewitt JE (2001) Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse. Nat Genet 28(2):151–154
Guo JM, Zhang XY, Chen HL, Wang GM, Zhang YK (2001) Structural alterations of sugar chains in urine fibronectin from bladder cancer patients and its enzymatic mechanism. J Cancer Res Clin Oncol 127(8):512–519
Heinrichs DE, Yethon JA, Whitfield C (1998) Molecular basis for structural diversity in the core regions of the lipopolysaccharides of Escherichia coli and Salmonella enterica. Mol Microbiol 30(2):221–232
Holzfeind PJ, Grewal PK, Reitsamer HA, Kechvar J, Lassmann H, Hoeger H, Hewitt JE, Bittner RE (2002) Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle–eye–brain disorders. Hum Mol Genet 11(21):2673–2687
Hwa KY, Pang TL, Chen MY (2007) Classification of LARGE-liked GlcNAc-transferases of Dictyostelium discoideum by phylogenetic analysis. Front Converg Biosci Inf Technol 2007:289–293
Jin XL, Liu HB, Zhang Y, Wang BS, Chen HL (2004) Alteration in N-acetylglucosaminyltransferase activities and glycan structure in tissue and bile glycoproteins from extrahepatic bile duct carcinoma. Glycoconj J 20(6):399–406
Kim YS, Hwang SY, Kang HY, Sohn H, Oh S, Kim JY, Yoo JS, Kim YH, Kim CH, Jeon JH, Lee JM, Kang HA, Miyoshi E, Taniguchi N, Yoo HS, Ko JH (2008) Functional proteomics study reveals that N-acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1. Mol Cell Proteomics 7(1):1–14
Lairson LL, Henrissat B, Davies GJ, Withers SG (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu Rev Biochem 77:521–555
Molinari M (2007) N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3(6):313–320
Pang TL, Wu CJ, Chen PA, Weng YL, Chen MY (2007) Dictyostelium gnt15 encodes a protein with similarity to LARGE and plays an essential role in development. Biochem Biophys Res Commun 360(1):83–89
Peyrard M, Seroussi E, Sandberg-Nordqvist AC, Xie YG, Han FY, Fransson I, Collins J, Dunham I, Kost-Alimova M, Imreh S, Dumanski JP (1999) The human LARGE gene from 22q12.3-q13.1 is a new, distinct member of the glycosyltransferase gene family. Proc Natl Acad Sci USA 96(2):598–603
Przybylo M, Pochec E, Link-Lenczowski P, Litynska A (2008) Beta1-6 branching of cell surface glycoproteins may contribute to uveal melanoma progression by up-regulating cell motility. Mol Vis 14:625–636
Ruddock LW, Molinari M (2006) N-glycan processing in ER quality control. J Cell Sci 119(Pt 21):4373–4380
Sasaki K, Kurata-Miura K, Ujita M, Angata K, Nakagawa S, Sekine S, Nishi T, Fukuda M (1997) Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis. Proc Natl Acad Sci USA 94(26):14294–14299
Acknowledgments
The work was supported by the grant to K.Y. Hwa from the National Science Council, Taiwan (97-2320-B-027-001) and from the National Taipei University of Technology (NTUT100-140-01). The authors declare that there is no conflict of interest.
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Hwa, KY., Lin, W.M. & Li, CP. LGTBase: LARGE-like GlcNAc Transferase Database. Soft Comput 16, 393–401 (2012). https://doi.org/10.1007/s00500-011-0723-2
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DOI: https://doi.org/10.1007/s00500-011-0723-2