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Volumn 22, Issue 3, 2012, Pages 429-438

Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates

Author keywords

ETD MS MS; lectin domain; mucin type O glycosylation; polypeptide GalNAc transferase; unnatural glycopeptide substrate

Indexed keywords

ALPHA LEVO FUCOSE O THREONINE; ALPHA N ACETYL DEXTRO GALACTOSAMINE O THREONINE; BETA N ACETYL DEXTRO GALACTOSAMINE O THREONINE; BETA N ACETYL DEXTRO GLUCOSAMINE O THREONINE; GLYCOPEPTIDE; LECTIN; MUCIN 5AC; N ACETYLGALACTOSAMINE; N ACETYLGALACTOSAMINYLTRANSFERASE 3; N ACETYLGLUCOSAMINE; POLYPEPTIDE; SUGAR; UNCLASSIFIED DRUG;

EID: 84856238781     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr159     Document Type: Article
Times cited : (16)

References (53)
  • 1
    • 0030035111 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel human UDP-N-acetyl-α-D- galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
    • DOI 10.1074/jbc.271.29.17006
    • Bennett EP, Hassan H, Clausen H. 1996. cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3. J Biol Chem. 271:17006-17012. (Pubitemid 26244245)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.29 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 2
    • 0032701175 scopus 로고    scopus 로고
    • A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates
    • DOI 10.1016/S0014-5793(99)01268-5, PII S0014579399012685
    • Bennett EP, Hassan H, Hollingsworth MA, Clausen H. 1999. A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates. FEBS Lett. 460:226-230. (Pubitemid 29495945)
    • (1999) FEBS Letters , vol.460 , Issue.2 , pp. 226-230
    • Bennett, E.P.1    Hassan, H.2    Hollingsworth, M.A.3    Clausen, H.4
  • 3
  • 5
    • 0032760680 scopus 로고    scopus 로고
    • Pathways of O-glycan biosynthesis in cancer cells
    • Brockhausen I. 1999. Pathways of O-glycan biosynthesis in cancer cells. Biochim Biophys Acta. 1473:67-95.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 67-95
    • Brockhausen, I.1
  • 6
    • 69949147510 scopus 로고    scopus 로고
    • Immunotherapy for cancer: Synthetic carbohydrate-based vaccines
    • Buskas T, Thompson P, Boons G-J. 2009. Immunotherapy for cancer: Synthetic carbohydrate-based vaccines. Chem Commun. 36:5335-5349.
    • (2009) Chem Commun , vol.36 , pp. 5335-5349
    • Buskas, T.1    Thompson, P.2    Boons, G.-J.3
  • 8
    • 0029854393 scopus 로고    scopus 로고
    • A family of UDP-GalNAc: Polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation
    • DOI 10.1093/glycob/6.6.635
    • Clausen H, Bennett EP. 1996. A family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases control the initiation of mucin-type O-linked glycosylation. Glycobiology. 6:635-646. (Pubitemid 26386377)
    • (1996) Glycobiology , vol.6 , Issue.6 , pp. 635-646
    • Clausen, H.1    Bennett, E.P.2
  • 9
    • 0001270151 scopus 로고
    • The determination of glycopeptides by liquid chromatography/mass spectrometry with collision-induced dissociation
    • Conboy JJ, Henion JD. 1992. The determination of glycopeptides by liquid chromatography/mass spectrometry with collision-induced dissociation. J Am Soc Mass Spectrom. 3:804-814.
    • (1992) J Am Soc Mass Spectrom , vol.3 , pp. 804-814
    • Conboy, J.J.1    Henion, J.D.2
  • 10
    • 0030583470 scopus 로고    scopus 로고
    • Building blocks for glycopeptide synthesis: Preparation of α-O-fucosylated Fmoc serine and threonine in one step from L-fucose tetraacetate
    • DOI 10.1016/0040-4039(96)01702-9
    • Elofsson M, Roy S, Salvador LA, Kihlberg J. 1996. Building blocks for glycopeptides synthesis: Preparation of α-O-fucosylated Fmoc serine and threonine in one step from L-fucose tetraacetate. Tetrahedron Lett. 37:7645-7648. (Pubitemid 26331462)
    • (1996) Tetrahedron Letters , vol.37 , Issue.42 , pp. 7645-7648
    • Elofsson, M.1    Roy, S.2    Salvador, L.A.3    Kihlberg, J.4
  • 12
    • 33646828699 scopus 로고    scopus 로고
    • Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2
    • DOI 10.1074/jbc.M513590200
    • Fritz TA, Raman J, Tabak LA. 2006. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2. J Biol Chem. 281:8613-8619. (Pubitemid 43847965)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8613-8619
    • Fritz, T.A.1    Raman, J.2    Tabak, L.A.3
  • 14
    • 0035077832 scopus 로고    scopus 로고
    • O-glycosylation of the mucin type
    • DOI 10.1515/BC.2001.022
    • Hanisch F-G. 2001. O-Glycosylation of the mucin type. Biol Chem. 382:143-149. (Pubitemid 32243924)
    • (2001) Biological Chemistry , vol.382 , Issue.2 , pp. 143-149
    • Hanisch, F.-G.1
  • 15
    • 0034780414 scopus 로고    scopus 로고
    • Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides
    • Hanisch F-G, Reis CA, Clausen H, Paulsen H. 2001. Evidence for glycosylation-dependent activities of polypeptide N- acetylgalactosaminyltransferases rGalNAc-T2 and-T4 on mucin glycopeptides. Glycobiology. 11:731-740. (Pubitemid 32976346)
    • (2001) Glycobiology , vol.11 , Issue.9 , pp. 731-740
    • Hanisch, F.-G.1    Reis, C.A.2    Clausen, H.3    Paulsen, H.4
  • 16
    • 84961342241 scopus 로고    scopus 로고
    • Control of mucin-type O-glycosylation: O-glycan occupancy is directed by substrate specificities of polypeptide GalNAc-transferases
    • Ernst B, Hart GW, Sinay P, editors Wiley VCH chapter
    • Hassan H, Bennett EP, Mandel U, Hollingsworth MA, Clausen H. 2000. Control of mucin-type O-glycosylation: O-glycan occupancy is directed by substrate specificities of polypeptide GalNAc-transferases. In: Ernst B, Hart GW, Sinay P, editors. "Carbohydrates in Chemistry and Biology-a Comprehension Handbook", Wiley-VCH chapter. p. 273-292.
    • (2000) Carbohydrates in Chemistry and Biology-A Comprehension Handbook , pp. 273-292
    • Hassan, H.1    Bennett, E.P.2    Mandel, U.3    Hollingsworth, M.A.4    Clausen, H.5
  • 18
    • 43549126011 scopus 로고    scopus 로고
    • Structure and function of the cell surface (tethered) mucins
    • DOI 10.1146/annurev.physiol.70.113006.100659
    • Hattrup CL, Gendler SJ. 2008. Structure and function of the cell surface (tethered) mucins. Annu Rev Physiol. 70:431-457. (Pubitemid 351738187)
    • (2008) Annual Review of Physiology , vol.70 , pp. 431-457
    • Hattrup, C.L.1    Gendler, S.J.2
  • 19
    • 0030035805 scopus 로고    scopus 로고
    • 3 domain: A flexible lectin scaffold
    • Hazes B. 1996. The (QxW)3 domain: A flexible lectin scaffold. Protein Sci. 5:1490-1501. (Pubitemid 26257214)
    • (1996) Protein Science , vol.5 , Issue.8 , pp. 1490-1501
    • Hazes, B.1
  • 20
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • Hollingsworth MA, Swanson BJ. 2004. Mucins in cancer: Protection and control of the cell surface. Nat Rev Cancer. 4:45-60. (Pubitemid 38082153)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.1 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 21
    • 0027586797 scopus 로고
    • Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: Methods for selective detection of glycopeptides in protein digests
    • Huddleston MJ, Bean MF, Carr SA. 1993. Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: Methods for selective detection of glycopeptides in protein digests. Anal Chem. 65:877-884.
    • (1993) Anal Chem , vol.65 , pp. 877-884
    • Huddleston, M.J.1    Bean, M.F.2    Carr, S.A.3
  • 22
    • 0031404510 scopus 로고    scopus 로고
    • Fold recognition and molecular modeling of a lectin-like domain in UDP-GalNAc:Polypeptide N-acetylgalactosaminyltransferases
    • Imberty A, Piller V, Piller F, Breton C. 1997. Fold recognition and molecular modeling of a lectin-like domain in UDP-GalNac:polypeptide N-acetylgalactosaminyltransferases. Protein Eng. 10:1353-1356. (Pubitemid 28116173)
    • (1997) Protein Engineering , vol.10 , Issue.12 , pp. 1353-1356
    • Imberty, A.1    Piller, V.2    Piller, F.3    Breton, C.4
  • 23
    • 70349997971 scopus 로고    scopus 로고
    • A synthetic vaccine consisting of a tumor-associated sialyl-TN-MUC1 tandem-repeat glycopeptide and tetanus toxoid: Induction of a strong and highly selective immune response
    • Kaiser A, Gaidzik N, Westerlind U, Kowalczyk D, Hobel A, Schmitt E, Kunz H. 2009. A synthetic vaccine consisting of a tumor-associated sialyl-TN-MUC1 tandem-repeat glycopeptide and tetanus toxoid: Induction of a strong and highly selective immune response. Angew Chem Int Ed. 48:7551-7555.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 7551-7555
    • Kaiser, A.1    Gaidzik, N.2    Westerlind, U.3    Kowalczyk, D.4    Hobel, A.5    Schmitt, E.6    Kunz, H.7
  • 25
    • 33646795021 scopus 로고    scopus 로고
    • Structural Basis of Carbohydrate Transfer Activity by Human UDP-GalNAc: Polypeptide α-N-Acetylgalactosaminyltransferase (pp-GalNAc-T10)
    • DOI 10.1016/j.jmb.2006.03.061, PII S0022283606004244
    • Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H. 2006. Structural basis of carbohydrate transfer activity by human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J Mol Biol. 359:708-727. (Pubitemid 43767270)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.3 , pp. 708-727
    • Kubota, T.1    Shiba, T.2    Sugioka, S.3    Furukawa, S.4    Sawaki, H.5    Kato, R.6    Wakatsuki, S.7    Narimatsu, H.8
  • 33
    • 61849088987 scopus 로고    scopus 로고
    • Elucidation of O-glycosylation structures of the β-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation
    • Perdivara I, Petrovich R, Allinquant B, Deterding LJ, Tomer KB, Przybylski M. 2009. Elucidation of O-glycosylation structures of the β-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation. J Proteome Res. 8:631-642.
    • (2009) J Proteome Res , vol.8 , pp. 631-642
    • Perdivara, I.1    Petrovich, R.2    Allinquant, B.3    Deterding, L.J.4    Tomer, K.B.5    Przybylski, M.6
  • 34
    • 67749133871 scopus 로고    scopus 로고
    • The glycopeptide preferring polypeptide-GalNAc transferase-10 (ppGalNAc T10), involved in mucin type-O-glycosylation, has a unique GalNAc-O-Ser/Thr binding site in its catalytic domain not found in ppGalNAc T1 or T2
    • Perrine CL, Ganguli A, Wu P, Bertozzi CR, Fritz TA, Raman J, Tabak LA, Gerken TA. 2009. The glycopeptide preferring polypeptide-GalNAc transferase-10 (ppGalNAc T10), involved in mucin type-O-glycosylation, has a unique GalNAc-O-Ser/Thr binding site in its catalytic domain not found in ppGalNAc T1 or T2. J Biol Chem. 284:20387-20397.
    • (2009) J Biol Chem , vol.284 , pp. 20387-20397
    • Perrine, C.L.1    Ganguli, A.2    Wu, P.3    Bertozzi, C.R.4    Fritz, T.A.5    Raman, J.6    Tabak, L.A.7    Gerken, T.A.8
  • 35
    • 15444375314 scopus 로고    scopus 로고
    • •-
    • DOI 10.1021/ac0483872
    • Pitteri SJ, Chrisman PA, Hogan JM, McLuckey SA. 2005. Electron transfer ion/ion reactions in a three-dimensional quadrupole ion trap: Reactions of doubly and triply protonated peptides with SO2 .?. Anal Chem. 77:1831-1839. (Pubitemid 40396281)
    • (2005) Analytical Chemistry , vol.77 , Issue.6 , pp. 1831-1839
    • Pitteri, S.J.1    Chrisman, P.A.2    Hogan, J.M.3    McLuckey, S.A.4
  • 36
    • 3343023761 scopus 로고    scopus 로고
    • Deconvoluting the functions of polypeptide N-α- acetylgalactosaminyltransferase family members by glycopeptide substrate profiling
    • DOI 10.1016/j.chembiol.2004.05.009, PII S1074552104001632
    • Pratt MR, Hang HC, Ten Hagen KG, Rarick J, Gerken TA, Tabak LA, Bertozzi CR. 2004. Deconvoluting the functions of polypeptide N-α- acetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem Biol. 11:1009-1016. (Pubitemid 38991795)
    • (2004) Chemistry and Biology , vol.11 , Issue.7 , pp. 1009-1016
    • Pratt, M.R.1    Hang, H.C.2    Ten Hagen, K.G.3    Rarick, J.4    Gerken, T.A.5    Tabak, L.A.6    Bertozzi, C.R.7
  • 37
    • 53149142512 scopus 로고    scopus 로고
    • The catalytic and lectin domains of UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase function in concert to direct glycosylation site selection
    • Raman J, Fritz TA, Gerken TA, Jamison O, Live D, Mian Liu, Tabak LA. 2008. The catalytic and lectin domains of UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase function in concert to direct glycosylation site selection. J Biol Chem. 283:22942-22951.
    • (2008) J Biol Chem , vol.283 , pp. 22942-22951
    • Raman, J.1    Fritz, T.A.2    Gerken, T.A.3    Jamison, O.4    Live, D.5    Liu, M.6    Tabak, L.A.7
  • 41
    • 0036451590 scopus 로고    scopus 로고
    • O-GalNAc incorporation into a cluster acceptor site of three consecutive threonines: Distinct specificity of GalNAc-transferase isoforms
    • DOI 10.1046/j.1432-1033.2002.03334.x
    • Takeuchi H, Kato K, Hassan H, Clausen H, Irimura T. 2002. O-GalNAc incorporation into a cluster acceptor site of three consecutive threonines. Distinct specificity of GalNAc-transferase isoforms. Eur J Biochem. 269:6173-6183. (Pubitemid 35461830)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.24 , pp. 6173-6183
    • Takeuchi, H.1    Kato, K.2    Hassan, H.3    Clausen, H.4    Irimura, T.5
  • 42
    • 40749160803 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation and its potential use in drug and vaccine development
    • DOI 10.1016/j.bbagen.2007.09.010, PII S0304416507002164
    • Tarp MA, Clausen H. 2008. Mucin-type O-glycosylation and its potential use in drug and vaccine development. Biochim Biophys Acta. 1780:546-563. (Pubitemid 351381249)
    • (2008) Biochimica et Biophysica Acta - General Subjects , vol.1780 , Issue.3 , pp. 546-563
    • Tarp, M.A.1    Clausen, H.2
  • 45
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferase
    • Ten Hagen KG, Fritz TA, Tabak LA. 2003. All in the family: The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Glycobiology. 13:1R-16R.
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 46
    • 0037032994 scopus 로고    scopus 로고
    • The lectin domain of UDP-GALNAC: Polypeptide N- acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites
    • DOI 10.1074/jbc.M207369200
    • Tenno M, Saeki A, Kezdy FJ, Elhammer AP, Kurosaka A. 2002. The lectin domain of UDPGalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites. J Biol Chem. 277:47088-47096. (Pubitemid 36159217)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 47088-47096
    • Tenno, M.1    Saeki, A.2    Kezdy, F.J.3    Elhammer, A.P.4    Kurosaka, A.5
  • 47
    • 0035800114 scopus 로고    scopus 로고
    • Studies of acceptor site specificities for three members of UDP-GalNAc:N-acetylgalactosaminyltransferases by using a synthetic peptide mimicking the tandem repeat of MUC5AC
    • DOI 10.1016/S0008-6215(01)00135-5, PII S0008621501001355
    • Tetaert D, Richet C, Gagnon J, Boersma A, Degand P. 2001. Studies of acceptor site specificities for three members of UDP-GalNAc: N-acetylgalactosaminyltransferases by using a synthetic peptide mimicking the tandem repeat of MUC5AC. Carbohydr Res. 333:165-171. (Pubitemid 32595629)
    • (2001) Carbohydrate Research , vol.333 , Issue.2 , pp. 165-171
    • Tetaert, D.1    Richet, C.2    Gagnon, J.3    Boersma, A.4    Degand, P.5
  • 48
    • 0035395790 scopus 로고    scopus 로고
    • Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides
    • DOI 10.1042/0264-6021:3570313
    • Tetaert D, Ten Hagen KG, Richet C, Boersma A, Gagnon J, Degand P. 2001. Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides. Biochem J. 357:313-320. (Pubitemid 32642932)
    • (2001) Biochemical Journal , vol.357 , Issue.1 , pp. 313-320
    • Tetaert, D.1    Ten Hagen, K.G.2    Richet, C.3    Boersma, A.4    Gagnon, J.5    Degand, P.6
  • 50
    • 33947198189 scopus 로고    scopus 로고
    • The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: Lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O- glycosylation
    • DOI 10.1093/glycob/cwl082
    • Wandall HH, Irazoqui F, Tarp MA, Bennett EP, Mandel U, Takeuchi H, Kato K, Irimura T, Suryanarayanan G, Hollingsworth MA, et al. 2007. The lectin domains of polypeptide GalNAc-transferases exhibit carbohydratebinding specificity for GalNAc: Lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation. Glycobiology. 17:374-387. (Pubitemid 46432009)
    • (2007) Glycobiology , vol.17 , Issue.4 , pp. 374-387
    • Wandall, H.H.1    Irazoqui, F.2    Tarp, M.A.3    Bennett, E.P.4    Mandel, U.5    Takeuchi, H.6    Kato, K.7    Irimura, T.8    Suryanarayanan, G.9    Hollingsworth, M.A.10    Clausen, H.11
  • 51
    • 54749154383 scopus 로고    scopus 로고
    • Synthetic vaccines consisting of tumor-associated MUC1 glycopeptide antigens and a T-cell epitope for the induction of a highly specific humoral immune response
    • Westerlind U, Hobel A, Gaidzik N, Schmitt E, Kunz H. 2008. Synthetic vaccines consisting of tumor-associated MUC1 glycopeptide antigens and a T-cell epitope for the induction of a highly specific humoral immune response. Angew Chem Int Ed. 47:7551-7556.
    • (2008) Angew Chem Int Ed , vol.47 , pp. 7551-7556
    • Westerlind, U.1    Hobel, A.2    Gaidzik, N.3    Schmitt, E.4    Kunz, H.5
  • 53
    • 77954599524 scopus 로고    scopus 로고
    • Unexpected tolerance of glycosylation by UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase revealed by electron capture dissociation mass spectrometry: Carbohydrate as potential protective groups
    • Yoshimura Y, Matsushita T, Fujitani N, Takegawa Y, Fujihira H, Naruchi K, Gao X-D, Manri N, Sakamoto T, Kato K, et al. 2010. Unexpected tolerance of glycosylation by UDP-GalNAc:polypeptide α-N- acetylgalactosaminyltransferase revealed by electron capture dissociation mass spectrometry: Carbohydrate as potential protective groups. Biochemistry. 49:5929-5941.
    • (2010) Biochemistry , vol.49 , pp. 5929-5941
    • Yoshimura, Y.1    Matsushita, T.2    Fujitani, N.3    Takegawa, Y.4    Fujihira, H.5    Naruchi, K.6    Gao, X.-D.7    Manri, N.8    Sakamoto, T.9    Kato, K.10


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