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Volumn 1, Issue 3, 2003, Pages 545-550

Occurrence of O-linked Xyl-GlcNAc and Xyl-Glc disaccharides in trocarin, a factor Xa homolog from snake venom

Author keywords

Blood coagulation; N linked sialylated diantennary oligosaccharides; O linked Xyl GlcNAc; Prothrombin activator glycoprotein

Indexed keywords

BLOOD CLOTTING FACTOR 10A; DISACCHARIDE; N ACETYLGLUCOSAMINE; PROTHROMBIN; SNAKE VENOM; TROCARIN; XYL GLCNAC; XYL-GLCNAC; XYLOSE GLUCOSE; XYLOSE-GLUCOSE;

EID: 0642280706     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1046/j.1538-7836.2003.00090.x     Document Type: Article
Times cited : (14)

References (35)
  • 1
    • 0034903951 scopus 로고    scopus 로고
    • Classification and nomenclature of prothrombin activators isolated from snake venoms
    • Kini RM, Morita T, Rosing J. Classification and nomenclature of prothrombin activators isolated from snake venoms. Thromb Haemost 2001; 86: 710-1.
    • (2001) Thromb Haemost , vol.86 , pp. 710-711
    • Kini, R.M.1    Morita, T.2    Rosing, J.3
  • 2
    • 0033566319 scopus 로고    scopus 로고
    • Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa
    • Joseph JS, Chung MC, Jeyaseelan K, Kini RM. Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa. Blood 1999; 94: 621-31.
    • (1999) Blood , vol.94 , pp. 621-631
    • Joseph, J.S.1    Chung, M.C.2    Jeyaseelan, K.3    Kini, R.M.4
  • 3
    • 0019304405 scopus 로고
    • The structures of the carbohydrate moieties of bovine blood coagulation factor X
    • Mizuochi T, Yamashita K, Fujikawa K, Titani K, Kobata A. The structures of the carbohydrate moieties of bovine blood coagulation factor X. J Biol Chem 1980; 255: 3526-31.
    • (1980) J Biol Chem , vol.255 , pp. 3526-3531
    • Mizuochi, T.1    Yamashita, K.2    Fujikawa, K.3    Titani, K.4    Kobata, A.5
  • 4
    • 0001506214 scopus 로고
    • Activation of bovine X (Stuart factor): conversion of factor Xaa to factor Xaß
    • Fujikawa K, Titani K, Davie EW. Activation of bovine X (Stuart factor): conversion of factor Xaa to factor Xaß. PNAS 1975; 72: 3359-63.
    • (1975) PNAS , vol.72 , pp. 3359-3363
    • Fujikawa, K.1    Titani, K.2    Davie, E.W.3
  • 5
    • 0027426025 scopus 로고
    • Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X The role of the carbohydrate moieties in the activation of factor X
    • Inoue K, Morita T. Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X. Eur J Biochem 1993; 218: 153-63.
    • (1993) Eur J Biochem , vol.218 , pp. 153-163
    • Inoue, K.1    Morita, T.2
  • 6
    • 0025764566 scopus 로고
    • Human plasma and recombinant factor VII Characterization of O-glycosylations at serine residues 52 and 60 and effects of site directed mutagenesis at serine 52 to alanine
    • Bjoern S, Foster DC, Thim L, Wiberg FC, Christensen M, Komiyama Y, Pederson AH, Kisiel W. Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site directed mutagenesis at serine 52 to alanine. J Biol Chem 1991; 266: 11051-7.
    • (1991) J Biol Chem , vol.266 , pp. 11051-11057
    • Bjoern, S.1    Foster, D.C.2    Thim, L.3    Wiberg, F.C.4    Christensen, M.5    Komiyama, Y.6    Pederson, A.H.7    Kisiel, W.8
  • 7
    • 0032522258 scopus 로고    scopus 로고
    • Functional consequences of mutations in Ser-52 and Ser-60 in human blood coagulation factor VII
    • Iino M, Foster DC, Kisiel W. Functional consequences of mutations in Ser-52 and Ser-60 in human blood coagulation factor VII. Arch Biochem Biophys 1998; 352: 182-92.
    • (1998) Arch Biochem Biophys , vol.352 , pp. 182-192
    • Iino, M.1    Foster, D.C.2    Kisiel, W.3
  • 8
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes Evidence for O-linked GlcNAc
    • Torres CR, Hart GW. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 1984; 259: 3308-17.
    • (1984) J Biol Chem , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 9
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • Holt GD, Snow CM, Senior A, Haltiwanger RS, Gerace L, Hart GW. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J Cell Biol 1987; 104: 1157-64.
    • (1987) J Cell Biol , vol.104 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3    Haltiwanger, R.S.4    Gerace, L.5    Hart, G.W.6
  • 10
    • 0034703095 scopus 로고    scopus 로고
    • O-Glycosylation of nuclear and cytosolic proteins Dynamic interplay between O-GlcNAc and O-phosphate
    • Comer FI, Hart GW. O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate. J Biol Chem 2000; 275: 29179-82.
    • (2000) J Biol Chem , vol.275 , pp. 29179-29182
    • Comer, F.I.1    Hart, G.W.2
  • 11
    • 0034854157 scopus 로고    scopus 로고
    • Glycan-dependent signaling: O-linked N-acetylglucosamine
    • Hanover JA. Glycan-dependent signaling: O-linked N-acetylglucosamine. FASEB J 2001; 15: 1865-76.
    • (2001) FASEB J , vol.15 , pp. 1865-1876
    • Hanover, J.A.1
  • 12
    • 0034851055 scopus 로고    scopus 로고
    • Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics
    • Vosseller K, Wells L, Hart GW. Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics. Biochimie 2001; 83: 575-81.
    • (2001) Biochimie , vol.83 , pp. 575-581
    • Vosseller, K.1    Wells, L.2    Hart, G.W.3
  • 13
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
    • Wells L, Vosseller K, Hart GW. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 2001; 291: 2376-8.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 14
    • 0032511103 scopus 로고    scopus 로고
    • Biosynthesis of O-N-acetylglucosamine-linked glycans in Trypanosoma cruzi. Characterization of the novel uridine diphospho-N-acetylglucosamine: polypeptide N-acetylglucosaminyltransferase-catalyzing formation of N-acetylglucosamine alpha1!O-threonine
    • Previato JO, Sola-Penna M, Agrellos OA, Jones C, Oeltmanni T, Travassos LR, Mendonca-Previato L. Biosynthesis of O-N-acetylglucosamine-linked glycans in Trypanosoma cruzi. Characterization of the novel uridine diphospho-N-acetylglucosamine: polypeptide N-acetylglucosaminyltransferase-catalyzing formation of N-acetylglucosamine alpha1!O-threonine. J Biol Chem 1998; 273: 14982-8.
    • (1998) J Biol Chem , vol.273 , pp. 14982-14988
    • Previato, J.O.1    Sola-Penna, M.2    Agrellos, O.A.3    Jones, C.4    Oeltmanni, T.5    Travassos, L.R.6    Mendonca-Previato, L.7
  • 15
    • 0027931371 scopus 로고
    • Isolation and characterization of novel mucin-like glycoproteins from cobra venom
    • Gowda DC, Davidson EA. Isolation and characterization of novel mucin-like glycoproteins from cobra venom. J Biol Chem 1994; 269: 20031-9.
    • (1994) J Biol Chem , vol.269 , pp. 20031-20039
    • Gowda, D.C.1    Davidson, E.A.2
  • 16
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F. Colorimetric method for determination of sugars and related substances. Anal Chem 1956; 28: 350-6.
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 17
    • 9444289552 scopus 로고
    • A new trisaccharide sugar chain linked to a serine residue in the first EGFlike domain of clotting factors VII and IX and protein Z
    • Liu CY, Chien S, eds. New York, NY: Plenum Press
    • Iwanaga S, Nishimura H, Kawabata S, Kisiel W, Hase S, Ikenaka T. A new trisaccharide sugar chain linked to a serine residue in the first EGFlike domain of clotting factors VII and IX and protein Z. In: Liu CY, Chien S, eds. Fibrinogen, Thrombosis, Coagulation, and Fibrinolysis. New York, NY: Plenum Press, 1991: 121-5.
    • (1991) Fibrinogen, Thrombosis, Coagulation, and Fibrinolysis , pp. 121-125
    • Iwanaga, S.1    Nishimura, H.2    Kawabata, S.3    Kisiel, W.4    Hase, S.5    Ikenaka, T.6
  • 19
    • 0024377258 scopus 로고
    • Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein
    • Nishimura H, Kawabata S, Kisiel W, Hase S, Ikenaka T, Shimonishi Y, Iwanaga S. Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein. Z J Biol Chem 1989; 264: 20320-5.
    • (1989) Z J Biol Chem , vol.264 , pp. 20320-20325
    • Nishimura, H.1    Kawabata, S.2    Kisiel, W.3    Hase, S.4    Ikenaka, T.5    Shimonishi, Y.6    Iwanaga, S.7
  • 20
    • 0035146448 scopus 로고    scopus 로고
    • Database analysis of O-glycosylation sites in proteins
    • Thanka Christlet TH, Veluraja K. Database analysis of O-glycosylation sites in proteins. Biophys J 2001; 80: 952-60.
    • (2001) Biophys J , vol.80 , pp. 952-960
    • Thanka Christlet, T.H.1    Veluraja, K.2
  • 21
    • 0023615351 scopus 로고
    • Erythrocytes contain cytoplasmic glycoproteins. O-Linked Glcnac band 4. 1
    • Holt GD, Haltiwanger RS, Torres CR, Hart GW. Erythrocytes contain cytoplasmic glycoproteins. O-Linked Glcnac band 4.1. J Biol Chem 1987; 262: 14847-50.
    • (1987) J Biol Chem , vol.262 , pp. 14847-14850
    • Holt, G.D.1    Haltiwanger, R.S.2    Torres, C.R.3    Hart, G.W.4
  • 22
    • 0023037076 scopus 로고
    • The subcellular distribution of terminal N-acetylglucosamine moieties Localization of a novel protein-saccharide linkage, O-linked GlcNAc
    • Holt GD, Hart GW. The subcellular distribution of terminal N-acetylglucosamine moieties Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J Biol Chem 1986; 261: 8049-57.
    • (1986) J Biol Chem , vol.261 , pp. 8049-8057
    • Holt, G.D.1    Hart, G.W.2
  • 23
    • 0023655430 scopus 로고
    • O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins
    • Hanover JA, Cohen CK, Willingham MC, Park MK. O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. J Biol Chem 1987; 262: 9887-94.
    • (1987) J Biol Chem , vol.262 , pp. 9887-9894
    • Hanover, J.A.1    Cohen, C.K.2    Willingham, M.C.3    Park, M.K.4
  • 24
    • 0023257987 scopus 로고
    • Monoclonal antibodies identify a group of nuclear pore complex glycoproteins
    • Snow CM, Senior A, Gerace L. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J Cell Biol 1987; 104: 1143-56.
    • (1987) J Cell Biol , vol.104 , pp. 1143-1156
    • Snow, C.M.1    Senior, A.2    Gerace, L.3
  • 25
    • 0017084675 scopus 로고
    • Role of g-carboxyglutamic acid. Cation specificity of prothrombin and factor X-phospholipid binding
    • Nelsestuen GL, Broderius M, Martin G. Role of g-carboxyglutamic acid. Cation specificity of prothrombin and factor X-phospholipid binding. J Biol Chem 1976; 251: 6886-93.
    • (1976) J Biol Chem , vol.251 , pp. 6886-6893
    • Nelsestuen, G.L.1    Broderius, M.2    Martin, G.3
  • 26
    • 0017620768 scopus 로고
    • Vitamin K-dependent formation of g-carboxyglutamic acid
    • Stenflo J, Suttie JW. Vitamin K-dependent formation of g-carboxyglutamic acid. Ann Rev Biochem 1977; 46: 157-72.
    • (1977) Ann Rev Biochem , vol.46 , pp. 157-172
    • Stenflo, J.1    Suttie, J.W.2
  • 27
    • 0030056114 scopus 로고    scopus 로고
    • Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX
    • Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B. Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. J Biol Chem 1996; 271: 16227-36.
    • (1996) J Biol Chem , vol.271 , pp. 16227-16236
    • Freedman, S.J.1    Blostein, M.D.2    Baleja, J.D.3    Jacobs, M.4    Furie, B.C.5    Furie, B.6
  • 28
    • 0027537465 scopus 로고
    • Carbohydrate residues modulate the activation of coagulation factor X
    • Sinha U, Wolf DL. Carbohydrate residues modulate the activation of coagulation factor X. J Biol Chem 1993; 268: 3048-51.
    • (1993) J Biol Chem , vol.268 , pp. 3048-3051
    • Sinha, U.1    Wolf, D.L.2
  • 29
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: all of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993; 3: 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 30
    • 0026655996 scopus 로고
    • Structures and functions of the sugar chains of glycoproteins
    • Kobata A. Structures and functions of the sugar chains of glycoproteins. Eur J Biochem 1992; 209: 483-501.
    • (1992) Eur J Biochem , vol.209 , pp. 483-501
    • Kobata, A.1
  • 31
    • 0025369545 scopus 로고
    • Effect of the carbohydrate moiety on the secondary structure of b2-glycoprotein. I. Implications for the biosynthesis and folding of glycoproteins
    • Walsh MT, Watzlawick H, Putnam FW, Schmid K, Brossmer R. Effect of the carbohydrate moiety on the secondary structure of b2-glycoprotein. I. Implications for the biosynthesis and folding of glycoproteins. Biochemistry 1990; 29: 6250-7.
    • (1990) Biochemistry , vol.29 , pp. 6250-6257
    • Walsh, M.T.1    Watzlawick, H.2    Putnam, F.W.3    Schmid, K.4    Brossmer, R.5
  • 32
    • 0021112695 scopus 로고
    • Effect of size and location of the oligosaccharide chain on protease degradation of bovine pancreatic ribonuclease
    • Bernard ER, Sheila AN, Olden K. Effect of size and location of the oligosaccharide chain on protease degradation of bovine pancreatic ribonuclease. J Biol Chem 1983; 258: 12198-202.
    • (1983) J Biol Chem , vol.258 , pp. 12198-12202
    • Bernard, E.R.1    Sheila, A.N.2    Olden, K.3
  • 34
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang C, Eufemi M, Turano C, Giartosio A. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 1996; 35: 7299-307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 35
    • 0025805564 scopus 로고
    • Primary structure of the virus activating protease from chick embryo. Its identity with the blood clotting factor Xa
    • Suzuki H, Harada A, Hayashi Y, Wada K, Asaka J, Gotoh B, Ogasawara T, Nagai Y. Primary structure of the virus activating protease from chick embryo. Its identity with the blood clotting factor Xa. FEBS Lett 1991; 283: 281-5.
    • (1991) FEBS Lett , vol.283 , pp. 281-285
    • Suzuki, H.1    Harada, A.2    Hayashi, Y.3    Wada, K.4    Asaka, J.5    Gotoh, B.6    Ogasawara, T.7    Nagai, Y.8


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