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Volumn 23, Issue 7, 2013, Pages 865-876

Glycosaminoglycans in the blood of hereditary multiple exostoses patients: Half reduction of heparan sulfate to chondroitin sulfate ratio and the possible diagnostic application

Author keywords

chondroitin sulfate; chondroitinase; heparan sulfate; heparinase; hereditary multiple exostoses

Indexed keywords

ALCOHOL; CHONDROITIN SULFATE; DISACCHARIDE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; N ACETYLGALACTOSAMINE 4 SULFATASE;

EID: 84881104181     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwt024     Document Type: Article
Times cited : (38)

References (61)
  • 1
    • 0025021282 scopus 로고
    • Rapid purification of human DNA from whole blood for potential application in clinical chemistry laboratories
    • Adell K, Ogbonna G. 1990. Rapid purification of human DNA from whole blood for potential application in clinical chemistry laboratories. Clin Chem. 36/2:261-264.
    • (1990) Clin Chem. , vol.36 , Issue.2 , pp. 261-264
    • Adell, K.1    Ogbonna, G.2
  • 4
    • 0004038637 scopus 로고
    • Oxford: Oxford University Press
    • Lewin B. 1994. Genes V. Oxford: Oxford University Press. p. 59-79.
    • (1994) Genes V. , pp. 59-79
    • Lewin, B.1
  • 7
    • 84858293542 scopus 로고    scopus 로고
    • Hereditary protein C deficiency and thrombosis risk: Genotype and phenotype relation in a large Italian family
    • Cafolla A, D'Andrea G, Baldacci E, Margaglione M, Mazzucconi MG, Foa R. 2012. Hereditary protein C deficiency and thrombosis risk: Genotype and phenotype relation in a large Italian family. Eur J Haematol. 88:336-339.
    • (2012) Eur J Haematol. , vol.88 , pp. 336-339
    • Cafolla, A.1    D'andrea, G.2    Baldacci, E.3    Margaglione, M.4    Mazzucconi, M.G.5    Foa, R.6
  • 8
    • 0026572171 scopus 로고
    • Characteristics of the interactions between acid glycosaminoglycans and proteins in normal human plasma as revealed by the behavior of the protein-polysaccharide complexes in ultrafiltration and chromatographic procedures
    • Calatroni A, Vinci R, Ferlazzo AM. 1992. Characteristics of the interactions between acid glycosaminoglycans and proteins in normal human plasma as revealed by the behavior of the protein-polysaccharide complexes in ultrafiltration and chromatographic procedures. Clin Chim Acta. 206:167-180.
    • (1992) Clin Chim Acta. , vol.206 , pp. 167-180
    • Calatroni, A.1    Vinci, R.2    Ferlazzo, A.M.3
  • 9
    • 33845502506 scopus 로고    scopus 로고
    • High glucose alters proteoglycan expression and the glycosaminoglycan composition in placentas of women with gestational diabetes mellitus and in cultured trophoblasts
    • Chen CP, Chang SC, Yang WCV. 2007. High glucose alters proteoglycan expression and the glycosaminoglycan composition in placentas of women with gestational diabetes mellitus and in cultured trophoblasts. Placenta. 28:97-106.
    • (2007) Placenta. , vol.28 , pp. 97-106
    • Chen, C.P.1    Chang, S.C.2    Yang, W.C.V.3
  • 10
    • 0014747864 scopus 로고
    • Multiple exostoses of bone with fatal spinal cord compression; A report of a case and brief review of the literature
    • Chiurco AA. 1970. Multiple exostoses of bone with fatal spinal cord compression; a report of a case and brief review of the literature. Neurology. 20:275-278.
    • (1970) Neurology. , vol.20 , pp. 275-278
    • Chiurco, A.A.1
  • 11
    • 0242286531 scopus 로고    scopus 로고
    • Antibodies that inhibit plasmodium falciparum adhesion to chondroitin sulfate A are associated with increased birth weight and the gestational age of newborns
    • Duffy PE, Fried M. 2003. Antibodies that inhibit plasmodium falciparum adhesion to chondroitin sulfate A are associated with increased birth weight and the gestational age of newborns. Infect Immun. 71:6620-6623.
    • (2003) Infect Immun. , vol.71 , pp. 6620-6623
    • Duffy, P.E.1    Fried, M.2
  • 12
    • 77953684080 scopus 로고    scopus 로고
    • Proteoglycans and sulfated glycosaminoglycans
    • In: Varki A, Cummings R, et al. editors. New York, NY: Cold Spring Harbor Laboratory Press
    • Esko JD, Kimata K, Lindahl U. 2009. Proteoglycans and sulfated glycosaminoglycans. In: Varki A, Cummings R, et al. editors. Essentials of Glycobiology. New York, NY: Cold Spring Harbor Laboratory Press. p. 229-248.
    • (2009) Essentials of Glycobiology , pp. 229-248
    • Esko, J.D.1    Kimata, K.2    Lindahl, U.3
  • 13
    • 0030272433 scopus 로고    scopus 로고
    • Influence of core protein sequence on glycosaminoglycan assembly
    • Esko JD, Zhang L. 1996. Influence of core protein sequence on glycosaminoglycan assembly. Curr Opin Struct Biol. 6:663-670.
    • (1996) Curr Opin Struct Biol. , vol.6 , pp. 663-670
    • Esko, J.D.1    Zhang, L.2
  • 14
    • 65149092670 scopus 로고    scopus 로고
    • Structural insights into chondroitin sulfate A binding duffy-binding-like domains from plasmodium falciparum: Implications for intervention strategies against placental malaria
    • Gill J, Chitnis CE, Sharma A. 2009. Structural insights into chondroitin sulfate A binding duffy-binding-like domains from plasmodium falciparum: Implications for intervention strategies against placental malaria. Malar J. 8:1-10.
    • (2009) Malar J. , vol.8 , pp. 1-10
    • Gill, J.1    Chitnis, C.E.2    Sharma, A.3
  • 16
    • 0037105009 scopus 로고    scopus 로고
    • Reevaluation of a genetic model for the development of exostosis in hereditary multiple exostosis
    • Hall CR, Cole WG, Haynes R, Hecht JT. 2002. Reevaluation of a genetic model for the development of exostosis in hereditary multiple exostosis. Am J Med Genet. 112:1-5.
    • (2002) Am J Med Genet. , vol.112 , pp. 1-5
    • Hall, C.R.1    Cole, W.G.2    Haynes, R.3    Hecht, J.T.4
  • 17
    • 0018131781 scopus 로고
    • Low-sulfated chondroitin sulfate in human blood and urine
    • Hata RI, Ohkawa SI, Nagai Y. 1978. Low-sulfated chondroitin sulfate in human blood and urine. Biochem Biophys Acta. 543:156-166.
    • (1978) Biochem Biophys Acta. , vol.543 , pp. 156-166
    • Hata, R.I.1    Ohkawa, S.I.2    Nagai, Y.3
  • 20
    • 51349112071 scopus 로고    scopus 로고
    • The structure of a chondroitin sulfate binding domain important in placental malaria
    • Higgins MK. 2008. The structure of a chondroitin sulfate binding domain important in placental malaria. J Biol Chem. 283:21842-21846.
    • (2008) J Biol Chem. , vol.283 , pp. 21842-21846
    • Higgins, M.K.1
  • 21
    • 0028927919 scopus 로고
    • Determination of chondroitin sulfates in human whole blood, plasma and blood cells by highperformance liquid chromatography
    • Huang Y, Toyoda H, Toida T, Imanari T. 1995. Determination of chondroitin sulfates in human whole blood, plasma and blood cells by highperformance liquid chromatography. Biomed Chromatogr. 9:102-105.
    • (1995) Biomed Chromatogr. , vol.9 , pp. 102-105
    • Huang, Y.1    Toyoda, H.2    Toida, T.3    Imanari, T.4
  • 24
    • 26844481045 scopus 로고    scopus 로고
    • Alteration of glycosaminoglycan metabolism in the development of diabetic complications in relation to metabolic control
    • Komosinska-Vassev K, Olczyk K, Kozma EM, Olczyk P, Wisowski G, Winsz-Szczotka K. 2005. Alteration of glycosaminoglycan metabolism in the development of diabetic complications in relation to metabolic control. Clin Chem Lab Med. 43:924-929.
    • (2005) Clin Chem Lab Med. , vol.43 , pp. 924-929
    • Komosinska-Vassev, K.1    Olczyk, K.2    Kozma, E.M.3    Olczyk, P.4    Wisowski, G.5    Winsz-Szczotka, K.6
  • 25
    • 57749107717 scopus 로고    scopus 로고
    • Evolutionary differences in glycosaminoglycan fine structure detected by quantitative glycan reductive isotope labeling
    • Lawrence R, Olson SK, Steele RE, Wang L, Warrior R, Cummings RD, Esko JD. 2008. Evolutionary differences in glycosaminoglycan fine structure detected by quantitative glycan reductive isotope labeling. J Biol Chem. 283:33674-33684.
    • (2008) J Biol Chem. , vol.283 , pp. 33674-33684
    • Lawrence, R.1    Olson, S.K.2    Steele, R.E.3    Wang, L.4    Warrior, R.5    Cummings, R.D.6    Esko, J.D.7
  • 26
    • 0030829353 scopus 로고    scopus 로고
    • Incomplete penetrance and expressivity skewing in hereditary multiple exostoses
    • Legeai-Mallet L, Munnich A, Maroteaux P, Le Merrer M. 1997. Incomplete penetrance and expressivity skewing in hereditary multiple exostoses. Clin Genet. 52:12-16.
    • (1997) Clin Genet. , vol.52 , pp. 12-16
    • Legeai-Mallet, L.1    Munnich, A.2    Maroteaux, P.3    Le Merrer, M.4
  • 28
    • 0034663225 scopus 로고    scopus 로고
    • Disruption of gastrulation and heparan sulfate biosynthesis in EXT1-deficient mice
    • Lin X, Wei G, Shi Z, Dryer L, Esko JD, Wells DE, Matzuk MM. 2000. Disruption of gastrulation and heparan sulfate biosynthesis in EXT1-deficient mice. Dev Biol. 224:299-311.
    • (2000) Dev Biol. , vol.224 , pp. 299-311
    • Lin, X.1    Wei, G.2    Shi, Z.3    Dryer, L.4    Esko, J.D.5    Wells, D.E.6    Matzuk, M.M.7
  • 29
    • 0032500662 scopus 로고    scopus 로고
    • The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate
    • Lind T, Tufaro F, McCormick C, Lindahl U, Lidholt K. 1998. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J Biol Chem. 273:26265-26268.
    • (1998) J Biol Chem. , vol.273 , pp. 26265-26268
    • Lind, T.1    Tufaro, F.2    McCormick, C.3    Lindahl, U.4    Lidholt, K.5
  • 30
    • 78649443793 scopus 로고    scopus 로고
    • Glycosaminoglycans in human and bovine serum: Detection of twenty-four heparan sulfate and chondroitin sulfate motifs including a novel sialic acidmodified chondroitin sulfate linkage hexasaccharide
    • Lu H, Mcdowell LM, Studelska DR, Zhang L. 2010. Glycosaminoglycans in human and bovine serum: Detection of twenty-four heparan sulfate and chondroitin sulfate motifs including a novel sialic acidmodified chondroitin sulfate linkage hexasaccharide. Glycobiol Insights. 2:13-28.
    • (2010) Glycobiol Insights. , vol.2 , pp. 13-28
    • Lu, H.1    McDowell, L.M.2    Studelska, D.R.3    Zhang, L.4
  • 32
    • 77954627828 scopus 로고    scopus 로고
    • A mouse model of chondrocyte specific somatic mutation reveals a role for Ext1 loss of heterozygosity in multiple hereditary exostoses
    • Matsumoto K, Irie F, Mackem S, Yamaguchi Y. 2010. A mouse model of chondrocyte specific somatic mutation reveals a role for Ext1 loss of heterozygosity in multiple hereditary exostoses. Proc Natl Acad Sci USA. 107:10932-10937.
    • (2010) Proc Natl Acad Sci USA. , vol.107 , pp. 10932-10937
    • Matsumoto, K.1    Irie, F.2    Mackem, S.3    Yamaguchi, Y.4
  • 33
    • 0034681139 scopus 로고    scopus 로고
    • The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate
    • McCormick C, Duncan G, Goutsos KT, Tufaro F. 2000. The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci USA. 97:668-673.
    • (2000) Proc Natl Acad Sci USA. , vol.97 , pp. 668-673
    • McCormick, C.1    Duncan, G.2    Goutsos, K.T.3    Tufaro, F.4
  • 35
    • 79551515947 scopus 로고    scopus 로고
    • Structural analysis of glycans
    • In: Varki A, Cummings R, et al. editors. New York, NY: Cold Spring Harbor Laboratory Press
    • Mulloy B, Hart GW, Stanley P. 2009. Structural analysis of glycans. In: Varki A, Cummings R, et al. editors. Essentials of Glycobiology. New York, NY: Cold Spring Harbor Laboratory Press. p. 661-678.
    • (2009) Essentials of Glycobiology , pp. 661-678
    • Mulloy, B.1    Hart, G.W.2    Stanley, P.3
  • 36
    • 0016202095 scopus 로고
    • Acidic glycosaminoglycans in human platelets and leukocytes: The isolation and enzymatic characterization of chondroitin 4-sulfate
    • Murata K. 1974. Acidic glycosaminoglycans in human platelets and leukocytes: The isolation and enzymatic characterization of chondroitin 4-sulfate. Clin Chim Acta. 57:115-124.
    • (1974) Clin Chim Acta. , vol.57 , pp. 115-124
    • Murata, K.1
  • 38
    • 0032524636 scopus 로고    scopus 로고
    • Glycosaminoglycan sulfation in human osteoarthritis. Disease-related alterations at the nonreducing termini of chondroitin and dermatan sulfate
    • Plaas AHK, West LA, Wong-Palms S, Nelson FRT. 1998. Glycosaminoglycan sulfation in human osteoarthritis. Disease-related alterations at the nonreducing termini of chondroitin and dermatan sulfate. J Biol Chem. 273:12642-12649.
    • (1998) J Biol Chem. , vol.273 , pp. 12642-12649
    • Plaas, A.H.K.1    West, L.A.2    Wong-Palms, S.3    Nelson, F.R.T.4
  • 39
    • 0038745922 scopus 로고    scopus 로고
    • A new heterozygous mutation (L338N) in the human Gsα (GNAS1) gene as a cause for congenital hypothyroidism in Albright's hereditary osteodystrophy
    • Pohlenz J, Ahrens W, Hiort O. 2003. A new heterozygous mutation (L338N) in the human Gsα (GNAS1) gene as a cause for congenital hypothyroidism in Albright's hereditary osteodystrophy. Eur J Endocrinol. 148:463-468.
    • (2003) Eur J Endocrinol. , vol.148 , pp. 463-468
    • Pohlenz, J.1    Ahrens, W.2    Hiort, O.3
  • 41
    • 33845706310 scopus 로고    scopus 로고
    • Analysis of plasma proteins that bind to glycosaminoglycans
    • Saito A, Munakata H. 2007. Analysis of plasma proteins that bind to glycosaminoglycans. Biochem Biophys Acta. 1770:241-246.
    • (2007) Biochem Biophys Acta. , vol.1770 , pp. 241-246
    • Saito, A.1    Munakata, H.2
  • 45
    • 0001524698 scopus 로고
    • Hereditary multiple exostosis
    • Solomon L. 1964. Hereditary multiple exostosis. Am J Hum Genet. 16:351-363.
    • (1964) Am J Hum Genet. , vol.16 , pp. 351-363
    • Solomon, L.1
  • 47
    • 28844450108 scopus 로고    scopus 로고
    • Mice deficient in Ext2 lack heparan sulfate and develop exostoses
    • Stickens D, Zak BM, Rougier N, Esko JD, Werb Z. 2005. Mice deficient in Ext2 lack heparan sulfate and develop exostoses. Development. 132:5055-5068.
    • (2005) Development. , vol.132 , pp. 5055-5068
    • Stickens, D.1    Zak, B.M.2    Rougier, N.3    Esko, J.D.4    Werb, Z.5
  • 48
    • 0034723308 scopus 로고    scopus 로고
    • Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects Heparan Sulfate in Vivo
    • Toyoda H, Kinoshita-Toyoda A, Selleck SB. 2000. Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects Heparan Sulfate in Vivo. J Biol Chem. 275:2269-2275.
    • (2000) J Biol Chem. , vol.275 , pp. 2269-2275
    • Toyoda, H.1    Kinoshita-Toyoda, A.2    Selleck, S.B.3
  • 50
    • 67650320143 scopus 로고    scopus 로고
    • Cellular organization of glycosylation
    • In: Varki A, Cummings R, et al. editors. New York, NY: Cold Spring Harbor Laboratory Press. p. 37-46
    • Varki A, Esko JD, Colley KJ. 2009. Cellular organization of glycosylation. In: Varki A, Cummings R, et al. editors. Essentials of Glycobiology. New York, NY: Cold Spring Harbor Laboratory Press. p. 37-46.
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Esko, J.D.2    Colley, K.J.3
  • 53
    • 0034623224 scopus 로고    scopus 로고
    • Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants
    • Wei G, Bai X, Gabb MMG, Bame KJ, Koshy TI, Spear PG, Esko JD. 2000. Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants. J Biol Chem. 275:27733-27740.
    • (2000) J Biol Chem. , vol.275 , pp. 27733-27740
    • Wei, G.1    Bai, X.2    Gabb, M.M.G.3    Bame, K.J.4    Koshy, T.I.5    Spear, P.G.6    Esko, J.D.7
  • 54
    • 79956161618 scopus 로고    scopus 로고
    • A comprehensive compositional analysis of heparin/heparan sulfate-derived disaccharides from human serum
    • Wei W, Ninonuevo MR, Sharma A, Danan-Leon LM, Leary JA. 2011. A comprehensive compositional analysis of heparin/heparan sulfate-derived disaccharides from human serum. Anal Chem. 83:3703-3708.
    • (2011) Anal Chem. , vol.83 , pp. 3703-3708
    • Wei, W.1    Ninonuevo, M.R.2    Sharma, A.3    Danan-Leon, L.M.4    Leary, J.A.5
  • 56
    • 0034053120 scopus 로고    scopus 로고
    • Molecular basis of multiple exostoses: Mutations in the EXT1 and EXT2 genes
    • Wuyts W, Hul WV. 2000. Molecular basis of multiple exostoses: Mutations in the EXT1 and EXT2 genes. Hum Mutat. 15:220-227.
    • (2000) Hum Mutat. , vol.15 , pp. 220-227
    • Wuyts, W.1    Hul, W.V.2
  • 58
    • 0037137494 scopus 로고    scopus 로고
    • Hereditary multiple exostoses and heparan sulfate polymerization
    • Zak BM, Crawford BE, Esko JD. 2002. Hereditary multiple exostoses and heparan sulfate polymerization. Biochim Biophys Acta. 1573:346-355.
    • (2002) Biochim Biophys Acta. , vol.1573 , pp. 346-355
    • Zak, B.M.1    Crawford, B.E.2    Esko, J.D.3
  • 59
    • 79954574438 scopus 로고    scopus 로고
    • Compound heterozygous loss of Ext1 and Ext2 is sufficient for formation of multiple exostoses in mouse ribs and long bones
    • Zak BM, Schuksz M, Koyama E, Mundy C, Wells DE, Yamaguchi Y, Pacifici M, Esko JD. 2011. Compound heterozygous loss of Ext1 and Ext2 is sufficient for formation of multiple exostoses in mouse ribs and long bones. Bone. 48:979-987.
    • (2011) Bone. , vol.48 , pp. 979-987
    • Zak, B.M.1    Schuksz, M.2    Koyama, E.3    Mundy, C.4    Wells, D.E.5    Yamaguchi, Y.6    Pacifici, M.7    Esko, J.D.8
  • 60
    • 4644353637 scopus 로고    scopus 로고
    • Inter-alpha-trypsin inhibitor, a covalent protein-glycosaminoglycan- protein complex
    • Zhuo L, Hascall VC, Kimata K. 2004. Inter-alpha-trypsin inhibitor, a covalent protein-glycosaminoglycan-protein complex. J Biol Chem. 279:38079-38082.
    • (2004) J Biol Chem. , vol.279 , pp. 38079-38082
    • Zhuo, L.1    Hascall, V.C.2    Kimata, K.3
  • 61
    • 0141764668 scopus 로고    scopus 로고
    • A physiological function of serum proteoglycan bikunin: The chondroitin sulfate moiety plays a central role
    • Zhuo L, Salustri A, Kimata K. 2003. A physiological function of serum proteoglycan bikunin: The chondroitin sulfate moiety plays a central role. Glycoconj J. 19:241-247.
    • (2003) Glycoconj J. , vol.19 , pp. 241-247
    • Zhuo, L.1    Salustri, A.2    Kimata, K.3


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