메뉴 건너뛰기




Volumn 365, Issue 1, 2007, Pages 62-73

MS analysis of chondroitin polymerization: Effects of Mn2+ ions on the stability of UDP-sugars and chondroitin synthesis

Author keywords

Chondroitin; Glycosaminoglycan; MALDI TOF MS; Manganese ion; Polymerase; UDP GlcA

Indexed keywords

ESCHERICHIA COLI; GLUCOSE; INDUCTIVELY COUPLED PLASMA; IONS; MASS SPECTROMETRY;

EID: 34247236277     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.02.023     Document Type: Article
Times cited : (18)

References (37)
  • 1
    • 0002549947 scopus 로고    scopus 로고
    • Structure and biosynthesis of chondroitin sulfate and hyaluronan
    • Iozzo R. (Ed), Marcel Dekker, New York
    • Calabro A., Midura R., Hascall V., Plaas A., Goodstone N., and Roden L. Structure and biosynthesis of chondroitin sulfate and hyaluronan. In: Iozzo R. (Ed). Proteoglycans (2000), Marcel Dekker, New York 5-26
    • (2000) Proteoglycans , pp. 5-26
    • Calabro, A.1    Midura, R.2    Hascall, V.3    Plaas, A.4    Goodstone, N.5    Roden, L.6
  • 2
    • 0036818369 scopus 로고    scopus 로고
    • Biosynthesis of chondroitin/dermatan sulfate
    • Silbert J.E., and Sugumaran G. Biosynthesis of chondroitin/dermatan sulfate. IUBMB Life 54 (2002) 177-186
    • (2002) IUBMB Life , vol.54 , pp. 177-186
    • Silbert, J.E.1    Sugumaran, G.2
  • 3
    • 0034698161 scopus 로고    scopus 로고
    • Structural analysis of glycosaminoglycans in animals bearing mutations in sugarless, sulfateless, and tout-velu: Drosophila homologues of vertebrate genes encoding glycosaminoglycan biosynthetic enzymes
    • Toyoda H., Kinoshita-Toyoda A., Fox B., and Selleck S.B. Structural analysis of glycosaminoglycans in animals bearing mutations in sugarless, sulfateless, and tout-velu: Drosophila homologues of vertebrate genes encoding glycosaminoglycan biosynthetic enzymes. J. Biol. Chem. 275 (2000) 21856-21861
    • (2000) J. Biol. Chem. , vol.275 , pp. 21856-21861
    • Toyoda, H.1    Kinoshita-Toyoda, A.2    Fox, B.3    Selleck, S.B.4
  • 4
    • 0034602170 scopus 로고    scopus 로고
    • Purification and characterization of N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase from the squid cartilage
    • Ito Y., and Habuchi O. Purification and characterization of N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase from the squid cartilage. J. Biol. Chem. 275 (2000) 34728-34736
    • (2000) J. Biol. Chem. , vol.275 , pp. 34728-34736
    • Ito, Y.1    Habuchi, O.2
  • 6
    • 11144220862 scopus 로고    scopus 로고
    • Nematode chondroitin polymerizing factor showing cell-/organ-specific expression is indispensable for chondroitin synthesis and embryonic cell division
    • Izumikawa T., Kitagawa H., Mizuguchi S., Nomura K.H., Nomura K., Tamura J., Gengyo-Ando K., Mitani S., and Sugahara K. Nematode chondroitin polymerizing factor showing cell-/organ-specific expression is indispensable for chondroitin synthesis and embryonic cell division. J. Biol. Chem. 279 (2004) 53755-53761
    • (2004) J. Biol. Chem. , vol.279 , pp. 53755-53761
    • Izumikawa, T.1    Kitagawa, H.2    Mizuguchi, S.3    Nomura, K.H.4    Nomura, K.5    Tamura, J.6    Gengyo-Ando, K.7    Mitani, S.8    Sugahara, K.9
  • 7
    • 0027264507 scopus 로고
    • Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction
    • Sugiura N., Sakurai K., Hori Y., Karasawa K., Suzuki S., and Kimata K. Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction. J. Biol. Chem. 268 (1993) 15779-15787
    • (1993) J. Biol. Chem. , vol.268 , pp. 15779-15787
    • Sugiura, N.1    Sakurai, K.2    Hori, Y.3    Karasawa, K.4    Suzuki, S.5    Kimata, K.6
  • 8
    • 0035957924 scopus 로고    scopus 로고
    • Transcriptional cross-talk between Smad, ERK1/2, and p38 mitogen-activated protein kinase pathways regulates transforming growth factor-β-induced aggrecan gene expression in chondrogenic ATDC5 cells
    • Watanabe H., de Caestecker M.P., and Yamada Y. Transcriptional cross-talk between Smad, ERK1/2, and p38 mitogen-activated protein kinase pathways regulates transforming growth factor-β-induced aggrecan gene expression in chondrogenic ATDC5 cells. J. Biol. Chem. 276 (2001) 14466-14473
    • (2001) J. Biol. Chem. , vol.276 , pp. 14466-14473
    • Watanabe, H.1    de Caestecker, M.P.2    Yamada, Y.3
  • 9
    • 0037151058 scopus 로고    scopus 로고
    • The structural motif in chondroitin sulfate for adhesion of Plasmodium falciparum-infected erythrocytes comprises disaccharide units of 4-O-sulfated and non-sulfated N-acetylgalactosamine linked to glucuronic acid
    • Chai W., Beeson J.G., and Lawson A.M. The structural motif in chondroitin sulfate for adhesion of Plasmodium falciparum-infected erythrocytes comprises disaccharide units of 4-O-sulfated and non-sulfated N-acetylgalactosamine linked to glucuronic acid. J. Biol. Chem. 277 (2002) 22438-22446
    • (2002) J. Biol. Chem. , vol.277 , pp. 22438-22446
    • Chai, W.1    Beeson, J.G.2    Lawson, A.M.3
  • 10
    • 0041815999 scopus 로고    scopus 로고
    • Heterogeneity of the chondroitin sulfate portion of phosphacan/6B4 proteoglycan regulates its binding affinity for pleiotrophin/heparin binding growth-associated molecule
    • Maeda N., He J., Yajima Y., Mikami T., Sugahara K., and Yabe T. Heterogeneity of the chondroitin sulfate portion of phosphacan/6B4 proteoglycan regulates its binding affinity for pleiotrophin/heparin binding growth-associated molecule. J. Biol. Chem. 278 (2003) 35805-35811
    • (2003) J. Biol. Chem. , vol.278 , pp. 35805-35811
    • Maeda, N.1    He, J.2    Yajima, Y.3    Mikami, T.4    Sugahara, K.5    Yabe, T.6
  • 11
    • 0035914310 scopus 로고    scopus 로고
    • Molecular cloning and expression of a human chondroitin synthase
    • Kitagawa H., Uyama T., and Sugahara K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721-38726
    • (2001) J. Biol. Chem. , vol.276 , pp. 38721-38726
    • Kitagawa, H.1    Uyama, T.2    Sugahara, K.3
  • 12
    • 0043031425 scopus 로고    scopus 로고
    • Chondroitin sulfate synthase-2: Molecular cloning and characterization of a novel human glycosyltransferase homologous to chondroitin sulfate glucuronyltransferase, which has dual enzymatic activities
    • Yada T., Gotoh M., Sato T., Shionyu M., Go M., Kaseyama H., Iwasaki H., Kikuchi N., Kwon Y.D., Togayachi A., Kudo T., Watanabe H., Narimatsu H., and Kimata K. Chondroitin sulfate synthase-2: Molecular cloning and characterization of a novel human glycosyltransferase homologous to chondroitin sulfate glucuronyltransferase, which has dual enzymatic activities. J. Biol. Chem. 278 (2003) 30235-30247
    • (2003) J. Biol. Chem. , vol.278 , pp. 30235-30247
    • Yada, T.1    Gotoh, M.2    Sato, T.3    Shionyu, M.4    Go, M.5    Kaseyama, H.6    Iwasaki, H.7    Kikuchi, N.8    Kwon, Y.D.9    Togayachi, A.10    Kudo, T.11    Watanabe, H.12    Narimatsu, H.13    Kimata, K.14
  • 14
    • 0034611771 scopus 로고    scopus 로고
    • Diversity and functions of glycosaminoglycan sulfotransferases
    • Habuchi O. Diversity and functions of glycosaminoglycan sulfotransferases. Biochim. Biophys. Acta 1474 (2000) 115-127
    • (2000) Biochim. Biophys. Acta , vol.1474 , pp. 115-127
    • Habuchi, O.1
  • 15
    • 0031016684 scopus 로고    scopus 로고
    • Biosynthesis of the Escherichia coli K4 capsule polysaccharide: A parallel system for studies of glycosyltransferases in chondroitin formation
    • Lidholt K., and Fjelstad M. Biosynthesis of the Escherichia coli K4 capsule polysaccharide: A parallel system for studies of glycosyltransferases in chondroitin formation. J. Biol. Chem. 272 (1997) 2682-2687
    • (1997) J. Biol. Chem. , vol.272 , pp. 2682-2687
    • Lidholt, K.1    Fjelstad, M.2
  • 16
    • 0023815409 scopus 로고
    • Structure and serological characteristics of the capsular K4 antigen of Escherichia coli O5:K4:H4, a fructose-containing polysaccharide with a chondroitin backbone
    • Rodriguez M.-L., Jann B., and Jann K. Structure and serological characteristics of the capsular K4 antigen of Escherichia coli O5:K4:H4, a fructose-containing polysaccharide with a chondroitin backbone. Eur. J. Biochem. 177 (1988) 117-124
    • (1988) Eur. J. Biochem. , vol.177 , pp. 117-124
    • Rodriguez, M.-L.1    Jann, B.2    Jann, K.3
  • 17
    • 0033022996 scopus 로고    scopus 로고
    • Structure, assembly, and regulation of expression of capsules in Escherichia coli
    • Whitfield C., and Roberts I.S. Structure, assembly, and regulation of expression of capsules in Escherichia coli. Mol. Microbiol. 31 (1999) 1307-1319
    • (1999) Mol. Microbiol. , vol.31 , pp. 1307-1319
    • Whitfield, C.1    Roberts, I.S.2
  • 18
    • 0025152679 scopus 로고
    • Structure and biosynthesis of the capsular antigens of Escherichia coli
    • Jann B., and Jann K. Structure and biosynthesis of the capsular antigens of Escherichia coli. Curr. Top. Microbiol. Immunol. 150 (1990) 19-42
    • (1990) Curr. Top. Microbiol. Immunol. , vol.150 , pp. 19-42
    • Jann, B.1    Jann, K.2
  • 19
    • 0037077210 scopus 로고    scopus 로고
    • Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4
    • Ninomiya T., Sugiura N., Tawada A., Sugimoto K., Watanabe H., and Kimata K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567-21575
    • (2002) J. Biol. Chem. , vol.277 , pp. 21567-21575
    • Ninomiya, T.1    Sugiura, N.2    Tawada, A.3    Sugimoto, K.4    Watanabe, H.5    Kimata, K.6
  • 20
    • 0242351116 scopus 로고    scopus 로고
    • Analysis of the two active sites of the hyaluronan synthase and the chondroitin synthase of Pasteurella multocida
    • Jing W., and DeAngelis P.L. Analysis of the two active sites of the hyaluronan synthase and the chondroitin synthase of Pasteurella multocida. Glycobiology 13 (2003) 661-671
    • (2003) Glycobiology , vol.13 , pp. 661-671
    • Jing, W.1    DeAngelis, P.L.2
  • 21
    • 0036628807 scopus 로고    scopus 로고
    • Studies on the metal binding sites in the catalytic domain of β1,4-galactosyltransferase
    • Boeggeman E., and Qasba P.K. Studies on the metal binding sites in the catalytic domain of β1,4-galactosyltransferase. Glycobiology 12 (2002) 395-407
    • (2002) Glycobiology , vol.12 , pp. 395-407
    • Boeggeman, E.1    Qasba, P.K.2
  • 22
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • Hillenkamp F., Karas M., Beavis R.C., and Chait B.T. Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal. Chem. 63 (1991) 1193A-1203A
    • (1991) Anal. Chem. , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 23
    • 0029841119 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization mass-spectrometry of proteins
    • Beavis R.C., and Chait B.T. Matrix-assisted laser desorption ionization mass-spectrometry of proteins. Methods Enzymol. 270 (1996) 519-551
    • (1996) Methods Enzymol. , vol.270 , pp. 519-551
    • Beavis, R.C.1    Chait, B.T.2
  • 24
    • 0028143502 scopus 로고
    • Oligosaccharides from human milk as revealed by matrix-assisted laser desorption/ionization mass spectrometry
    • Stahl B., Thurl S., Zeng J., Karas M., Hillenkamp F., Steup M., and Sawatzki G. Oligosaccharides from human milk as revealed by matrix-assisted laser desorption/ionization mass spectrometry. Anal. Biochem. 223 (1994) 218-226
    • (1994) Anal. Biochem. , vol.223 , pp. 218-226
    • Stahl, B.1    Thurl, S.2    Zeng, J.3    Karas, M.4    Hillenkamp, F.5    Steup, M.6    Sawatzki, G.7
  • 25
    • 0037184256 scopus 로고    scopus 로고
    • Matrix-assisted ultraviolet laser-desorption ionization and electrospray-ionization time-of-flight mass spectrometry of sulfated neocarrabiose oligosaccharides
    • Fukuyama Y., Ciancia M., Nonami H., Cerezo A.S., Erra-Balsells R., and Matulewicz M.C. Matrix-assisted ultraviolet laser-desorption ionization and electrospray-ionization time-of-flight mass spectrometry of sulfated neocarrabiose oligosaccharides. Carbohydr. Res. 337 (2002) 1553-1562
    • (2002) Carbohydr. Res. , vol.337 , pp. 1553-1562
    • Fukuyama, Y.1    Ciancia, M.2    Nonami, H.3    Cerezo, A.S.4    Erra-Balsells, R.5    Matulewicz, M.C.6
  • 27
    • 0033199325 scopus 로고    scopus 로고
    • Analysis of high-molecular-weight oligosaccharides from human milk by liquid chromatography and MALDI-MS
    • Finke B., Stahl B., Pfenninger A., Karas M., Daniel H., and Sawatzki G. Analysis of high-molecular-weight oligosaccharides from human milk by liquid chromatography and MALDI-MS. Anal. Chem. 71 (1999) 3755-3762
    • (1999) Anal. Chem. , vol.71 , pp. 3755-3762
    • Finke, B.1    Stahl, B.2    Pfenninger, A.3    Karas, M.4    Daniel, H.5    Sawatzki, G.6
  • 28
    • 0032788787 scopus 로고    scopus 로고
    • Molecular weight determination of hyaluronic acid by gel filtration chromatography coupled to matrix-assisted laser desorption ionization mass spectrometry
    • Yeung B., and Marecak D. Molecular weight determination of hyaluronic acid by gel filtration chromatography coupled to matrix-assisted laser desorption ionization mass spectrometry. J. Chromatogr. A 852 (1999) 573-581
    • (1999) J. Chromatogr. A , vol.852 , pp. 573-581
    • Yeung, B.1    Marecak, D.2
  • 30
    • 0035714137 scopus 로고    scopus 로고
    • Novel methods for the preparation and characterization of hyaluronan oligosaccharides of defined length
    • Mahoney D.J., Aplin R.T., Calabro A., Hascall V.C., and Day A.J. Novel methods for the preparation and characterization of hyaluronan oligosaccharides of defined length. Glycobiology 11 (2001) 1025-1033
    • (2001) Glycobiology , vol.11 , pp. 1025-1033
    • Mahoney, D.J.1    Aplin, R.T.2    Calabro, A.3    Hascall, V.C.4    Day, A.J.5
  • 31
    • 0032829352 scopus 로고    scopus 로고
    • Cartilage degradation by hyaluronate lyase and chondroitin ABC lyase: A MALDI-TOF mass spectrometric study
    • Schiller J., Arnhold J., Benard S., Reichl S., and Arnold K. Cartilage degradation by hyaluronate lyase and chondroitin ABC lyase: A MALDI-TOF mass spectrometric study. Carbohydr. Res. 318 (1999) 116-122
    • (1999) Carbohydr. Res. , vol.318 , pp. 116-122
    • Schiller, J.1    Arnhold, J.2    Benard, S.3    Reichl, S.4    Arnold, K.5
  • 32
    • 0029068089 scopus 로고
    • Utility of non-covalent complexes in the matrix-assisted laser desorption ionization mass spectrometry of heparin-derived oligosaccharides
    • Juhasz P., and Biemann K. Utility of non-covalent complexes in the matrix-assisted laser desorption ionization mass spectrometry of heparin-derived oligosaccharides. Carbohydr. Res. 270 (1995) 131-147
    • (1995) Carbohydr. Res. , vol.270 , pp. 131-147
    • Juhasz, P.1    Biemann, K.2
  • 35
  • 36
    • 33646849921 scopus 로고    scopus 로고
    • Critical elements of oligosaccharide acceptor substrates for the Pasteurella multocida hyaluronan synthase
    • Williams K.J., Halkes K.M., Kamerling J.P., and DeAngelis P.L. Critical elements of oligosaccharide acceptor substrates for the Pasteurella multocida hyaluronan synthase. J. Biol. Chem. 281 (2006) 5391-5397
    • (2006) J. Biol. Chem. , vol.281 , pp. 5391-5397
    • Williams, K.J.1    Halkes, K.M.2    Kamerling, J.P.3    DeAngelis, P.L.4
  • 37
    • 0033839262 scopus 로고    scopus 로고
    • Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: Two active sites exist in one polypeptide
    • Jing W., and DeAngelis P.L. Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: Two active sites exist in one polypeptide. Glycobiology 10 (2000) 883-889
    • (2000) Glycobiology , vol.10 , pp. 883-889
    • Jing, W.1    DeAngelis, P.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.