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Fucosyltransferase 1 Mediates Angiogenesis in Rheumatoid Arthritis

dc.contributor.authorIsozaki, Takeoen_US
dc.contributor.authorAmin, Mohammad A.en_US
dc.contributor.authorRuth, Jeffrey H.en_US
dc.contributor.authorCampbell, Phillip L.en_US
dc.contributor.authorTsou, Pei‐suenen_US
dc.contributor.authorHa, Christine M.en_US
dc.contributor.authorStinson, W. Alexen_US
dc.contributor.authorDomino, Steven E.en_US
dc.contributor.authorKoch, Alisa E.en_US
dc.date.accessioned2014-08-06T16:49:34Z
dc.date.availableWITHHELD_13_MONTHSen_US
dc.date.available2014-08-06T16:49:34Z
dc.date.issued2014-08en_US
dc.identifier.citationIsozaki, Takeo; Amin, Mohammad A.; Ruth, Jeffrey H.; Campbell, Phillip L.; Tsou, Pei‐suen ; Ha, Christine M.; Stinson, W. Alex; Domino, Steven E.; Koch, Alisa E. (2014). "Fucosyltransferase 1 Mediates Angiogenesis in Rheumatoid Arthritis." Arthritis & Rheumatology 66(8): 2047-2058.en_US
dc.identifier.issn2326-5191en_US
dc.identifier.issn2326-5205en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/108009
dc.publisherWiley Periodicals, Inc.en_US
dc.titleFucosyltransferase 1 Mediates Angiogenesis in Rheumatoid Arthritisen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelRheumatologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/108009/1/art38648.pdf
dc.identifier.doi10.1002/art.38648en_US
dc.identifier.sourceArthritis & Rheumatologyen_US
dc.identifier.citedreferenceKoch AE, Kunkel SL, Harlow LA, Johnson B, Evanoff HL, Haines GK, et al. Enhanced production of monocyte chemoattractant protein‐1 in rheumatoid arthritis. J Clin Invest 1992; 90: 772 – 9.en_US
dc.identifier.citedreferenceMarotte H, Tsou PS, Rabquer BJ, Pinney AJ, Fedorova T, Lalwani N, et al. Blocking of interferon regulatory factor 1 reduces tumor necrosis factor α–induced interleukin‐18 bioactivity in rheumatoid arthritis synovial fibroblasts by induction of interleukin‐18 binding protein a: role of the nuclear interferon regulatory factor 1–NF‐κB–c‐jun complex. Arthritis Rheum 2011; 63: 3253 – 62.en_US
dc.identifier.citedreferenceRabquer BJ, Pakozdi A, Michel JE, Gujar BS, Haines GK III, Imhof BA, et al. Junctional adhesion molecule C mediates leukocyte adhesion to rheumatoid arthritis synovium. Arthritis Rheum 2008; 58: 3020 – 9.en_US
dc.identifier.citedreferenceVolin MV, Woods JM, Amin MA, Connors MA, Harlow LA, Koch AE. Fractalkine: a novel angiogenic chemokine in rheumatoid arthritis. Am J Pathol 2001; 159: 1521 – 30.en_US
dc.identifier.citedreferencePark CC, Morel JC, Amin MA, Connors MA, Harlow LA, Koch AE. Evidence of IL‐18 as a novel angiogenic mediator. J Immunol 2001; 167: 1644 – 53.en_US
dc.identifier.citedreferenceAmin MA, Volpert OV, Woods JM, Kumar P, Harlow LA, Koch AE. Migration inhibitory factor mediates angiogenesis via mitogen‐activated protein kinase and phosphatidylinositol kinase. Circ Res 2003; 93: 321 – 9.en_US
dc.identifier.citedreferenceMarotte H, Ruth JH, Campbell PL, Koch AE, Ahmed S. Green tea extract inhibits chemokine production, but up‐regulates chemokine receptor expression, in rheumatoid arthritis synovial fibroblasts and rat adjuvant‐induced arthritis. Rheumatology (Oxford) 2010; 49: 467 – 79.en_US
dc.identifier.citedreferenceMacartney JC. Fucose‐containing antigens in normal and neoplastic human gastric mucosa: a comparative study using lectin histochemistry and blood group immunohistochemistry. J Pathol 1987; 152: 23 – 30.en_US
dc.identifier.citedreferenceHachicha M, Rathanaswami P, Schall TJ, McColl SR. Production of monocyte chemotactic protein–1 in human type B synoviocytes: synergistic effect of tumor necrosis factor α and interferon‐γ. Arthritis Rheum 1993; 36: 26 – 34.en_US
dc.identifier.citedreferenceVolin MV, Shah MR, Tokuhira M, Haines GK, Woods JM, Koch AE. RANTES expression and contribution to monocyte chemotaxis in arthritis. Clin Immunol Immunopathol 1998; 89: 44 – 53.en_US
dc.identifier.citedreferenceApweiler R, Hermjakob H, Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS‐PROT database. Biochim Biophys Acta 1999; 1473: 4 – 8.en_US
dc.identifier.citedreferenceHakomori S. Aberrant glycosylation in tumors and tumor‐associated carbohydrate antigens. Adv Cancer Res 1989; 52: 257 – 331.en_US
dc.identifier.citedreferenceNakagawa T, Uozumi N, Nakano M, Mizuno‐Horikawa Y, Okuyama N, Taguchi T, et al. Fucosylation of N‐glycans regulates the secretion of hepatic glycoproteins into bile ducts. J Biol Chem 2006; 281: 29797 – 806.en_US
dc.identifier.citedreferencePrzybysz M, Maszczak D, Borysewicz K, Szechinski J, Katnik‐Prastowska I. Relative sialylation and fucosylation of synovial and plasma fibronectins in relation to the progression and activity of rheumatoid arthritis. Glycoconj J 2007; 24: 543 – 50.en_US
dc.identifier.citedreferenceFerens‐Sieczkowska M, Kossowska B, Gancarz R, Dudzik D, Knas M, Popko J, et al. Fucosylation in synovial fluid as a novel clinical marker for differentiating joint diseases: a preliminary study. Clin Exp Rheumatol 2007; 25: 92 – 5.en_US
dc.identifier.citedreferenceSalcedo R, Ponce ML, Young HA, Wasserman K, Ward JM, Kleinman HK, et al. Human endothelial cells express CCR2 and respond to MCP‐1: direct role of MCP‐1 in angiogenesis and tumor progression. Blood 2000; 96: 34 – 40.en_US
dc.identifier.citedreferenceIsozaki T, Ruth JH, Amin MA, Campbell PL, Tsou PS, Ha CM, et al. Fucosyltransferase 1 mediates angiogenesis, cell adhesion and rheumatoid arthritis synovial tissue fibroblast proliferation. Arthritis Res Ther 2014; 16: R28.en_US
dc.identifier.citedreferenceProost P, Struyf S, Couvreur M, Lenaerts JP, Conings R, Menten P, et al. Posttranslational modifications affect the activity of the human monocyte chemotactic proteins MCP‐1 and MCP‐2: identification of MCP‐2(6‐76) as a natural chemokine inhibitor. J Immunol 1998; 160: 4034 – 41.en_US
dc.identifier.citedreferenceCarlyon JA, Akkoyunlu M, Xia L, Yago T, Wang T, Cummings RD, et al. Murine neutrophils require α1,3‐fucosylation but not PSGL‐1 for productive infection with Anaplasma phagocytophilum. Blood 2003; 102: 3387 – 95.en_US
dc.identifier.citedreferenceMathieu S, Gerolami R, Luis J, Carmona S, Kol O, Crescence L, et al. Introducing α(1,2)‐linked fucose into hepatocarcinoma cells inhibits vasculogenesis and tumor growth. Int J Cancer 2007; 121: 1680 – 9.en_US
dc.identifier.citedreferencePalumberi D, Aldi S, Ermini L, Ziche M, Finetti F, Donnini S, et al. RNA‐mediated gene silencing of FUT1 and FUT2 influences expression and activities of bovine and human fucosylated nucleolin and inhibits cell adhesion and proliferation. J Cell Biochem 2010; 111: 229 – 38.en_US
dc.identifier.citedreferenceTsou PS, Ruth JH, Campbell PL, Isozaki T, Lee S, Marotte H, et al. A novel role for inducible Fut2 in angiogenesis. Angiogenesis 2013; 16: 195 – 205.en_US
dc.identifier.citedreferenceMoremen KW, Tiemeyer M, Nairn AV. Vertebrate protein glycosylation: diversity, synthesis and function. Nat Rev Mol Cell Biol 2012; 13: 448 – 62.en_US
dc.identifier.citedreferenceMoelants EA, Mortier A, Grauwen K, Ronsse I, Van Damme J, Proost P. Citrullination of TNF‐α by peptidylarginine deiminases reduces its capacity to stimulate the production of inflammatory chemokines. Cytokine 2013; 61: 161 – 7.en_US
dc.identifier.citedreferenceHart GW. Glycosylation. Curr Opin Cell Biol 1992; 4: 1017 – 23.en_US
dc.identifier.citedreferenceKannagi R, Izawa M, Koike T, Miyazaki K, Kimura N. Carbohydrate‐mediated cell adhesion in cancer metastasis and angiogenesis. Cancer Sci 2004; 95: 377 – 84.en_US
dc.identifier.citedreferenceMiyoshi E, Moriwaki K, Nakagawa T. Biological function of fucosylation in cancer biology. J Biochem 2008; 143: 725 – 9.en_US
dc.identifier.citedreferenceFukushima K, Satoh T, Baba S, Yamashita K. α1,2‐Fucosylated and β‐N‐acetylgalactosaminylated prostate‐specific antigen as an efficient marker of prostatic cancer. Glycobiology 2010; 20: 452 – 60.en_US
dc.identifier.citedreferenceYoshida M, Takimoto R, Murase K, Sato Y, Hirakawa M, Tamura F, et al. Targeting anticancer drug delivery to pancreatic cancer cells using a fucose‐bound nanoparticle approach. PLoS One 2012; 7: e39545.en_US
dc.identifier.citedreferenceKelly RJ, Rouquier S, Giorgi D, Lennon GG, Lowe JB. Sequence and expression of a candidate for the human Secretor blood group α(1,2)fucosyltransferase gene (FUT2): homozygosity for an enzyme‐inactivating nonsense mutation commonly correlates with the non‐secretor phenotype. J Biol Chem 1995; 270: 4640 – 9.en_US
dc.identifier.citedreferenceLarsen RD, Ernst LK, Nair RP, Lowe JB. Molecular cloning, sequence, and expression of a human GDP‐L‐fucose:β‐D‐galactoside 2‐α‐L‐fucosyltransferase cDNA that can form the H blood group antigen. Proc Natl Acad Sci U S A 1990; 87: 6674 – 8.en_US
dc.identifier.citedreferenceKoch AE, Halloran MM, Haskell CJ, Shah MR, Polverini PJ. Angiogenesis mediated by soluble forms of E‐selectin and vascular cell adhesion molecule‐1. Nature 1995; 376: 517 – 9.en_US
dc.identifier.citedreferenceHalloran MM, Carley WW, Polverini PJ, Haskell CJ, Phan S, Anderson BJ, et al. Ley/H: an endothelial‐selective, cytokine‐inducible, angiogenic mediator. J Immunol 2000; 164: 4868 – 77.en_US
dc.identifier.citedreferenceZhu K, Amin MA, Kim MJ, Katschke KJ Jr, Park CC, Koch AE. A novel function for a glucose analog of blood group H antigen as a mediator of leukocyte‐endothelial adhesion via intracellular adhesion molecule 1. J Biol Chem 2003; 278: 21869 – 77.en_US
dc.identifier.citedreferenceKoch AE, Kunkel SL, Burrows JC, Evanoff HL, Haines GK, Pope RM, et al. Synovial tissue macrophage as a source of the chemotactic cytokine IL‐8. J Immunol 1991; 147: 2187 – 95.en_US
dc.identifier.citedreferenceRitchlin C. Fibroblast biology: effector signals released by the synovial fibroblast in arthritis. Arthritis Res 2000; 2: 356 – 60.en_US
dc.identifier.citedreferenceWeinblatt ME, Keystone EC, Furst DE, Moreland LW, Weisman MH, Birbara CA, et al. Adalimumab, a fully human anti–tumor necrosis factor α monoclonal antibody, for the treatment of rheumatoid arthritis in patients taking concomitant methotrexate: the ARMADA trial. Arthritis Rheum 2003; 48: 35 – 45.en_US
dc.identifier.citedreferenceMori K, Iida S, Yamane‐Ohnuki N, Kanda Y, Kuni‐Kamochi R, Nakano R, et al. Non‐fucosylated therapeutic antibodies: the next generation of therapeutic antibodies. Cytotechnology 2007; 55: 109 – 14.en_US
dc.identifier.citedreferenceFolkman J, Shing Y. Angiogenesis. J Biol Chem 1992; 267: 10931 – 4.en_US
dc.identifier.citedreferenceCarmeliet P. Angiogenesis in life, disease and medicine. Nature 2005; 438: 932 – 6.en_US
dc.identifier.citedreferenceDomino SE, Zhang L, Gillespie PJ, Saunders TL, Lowe JB. Deficiency of reproductive tract α(1,2)fucosylated glycans and normal fertility in mice with targeted deletions of the FUT1 or FUT2 α(1,2)fucosyltransferase locus. Mol Cell Biol 2001; 21: 8336 – 45.en_US
dc.identifier.citedreferenceDomino SE, Zhang L, Lowe JB. Molecular cloning, genomic mapping, and expression of two Secretor blood group α(1,2)fucosyltransferase genes differentially regulated in mouse uterine epithelium and gastrointestinal tract. J Biol Chem 2001; 276: 23748 – 56.en_US
dc.identifier.citedreferenceIwamori M, Domino SE. Tissue‐specific loss of fucosylated glycolipids in mice with targeted deletion of α(1,2)fucosyltransferase genes. Biochem J 2004; 380: 75 – 81.en_US
dc.identifier.citedreferenceMarelli‐Berg FM, Peek E, Lidington EA, Stauss HJ, Lechler RI. Isolation of endothelial cells from murine tissue. J Immunol Methods 2000; 244: 205 – 15.en_US
dc.identifier.citedreferenceRuth JH, Volin MV, Haines GK III, Woodruff DC, Katschke KJ Jr, Woods JM, et al. Fractalkine, a novel chemokine in rheumatoid arthritis and in rat adjuvant‐induced arthritis. Arthritis Rheum 2001; 44: 1568 – 81.en_US
dc.identifier.citedreferenceIsozaki T, Rabquer BJ, Ruth JH, Haines GK III, Koch AE. ADAM‐10 is overexpressed in rheumatoid arthritis synovial tissue and mediates angiogenesis. Arthritis Rheum 2013; 65: 98 – 108.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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