메뉴 건너뛰기




Volumn 102, Issue 6, 2009, Pages 1183-1193

Anticoagulant activity of a sulfated galactan: Serpin-independent effect and specific interaction with factor Xa

Author keywords

Antithrombotic drug; Heparin; Heparin binding exosite; Prothrombinase complex; Sulfated galactan; Tenase complex

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 10A; GALACTAN; HEPARIN; SERINE PROTEINASE INHIBITOR; THROMBIN;

EID: 72949100767     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH09-04-0273     Document Type: Article
Times cited : (33)

References (34)
  • 1
    • 0033821407 scopus 로고    scopus 로고
    • Heparins in the new millennium: Will unfractionated heparin survive?
    • Fareed J, Hoppensteadt DA. Heparins in the new millennium: Will unfractionated heparin survive? Semin Thromb Haemost 2000; 26: 87-88.
    • (2000) Semin Thromb Haemost , vol.26 , pp. 87-88
    • Fareed, J.1    Hoppensteadt, D.A.2
  • 2
    • 0024216243 scopus 로고
    • The mode of action of heparin in plasma.Thromb
    • Béguin S, Lindhout T, Hemker HC. The mode of action of heparin in plasma.Thromb Haemost 1988; 60: 457-462.
    • (1988) Haemost , vol.60 , pp. 457-462
    • Béguin, S.1    Lindhout, T.2    Hemker, H.C.3
  • 3
    • 58049216683 scopus 로고    scopus 로고
    • Outbreak of adverse reactions associated with contaminated heparin
    • Blossom DB et al. Outbreak of adverse reactions associated with contaminated heparin. N Engl J Med 2008; 359: 2674-2684.
    • (2008) N Engl J Med , vol.359 , pp. 2674-2684
    • Blossom, D.B.1
  • 5
    • 0034703076 scopus 로고    scopus 로고
    • Structure and anticoagulant activity of sulfated galactans - Isolation of a unique sulfated galactan from the red algae Botryocladia occidentalis and comparison of its anticoagulant action with that of sulfated galactans from invertebrates
    • Farias WRL, Valente AP, Pereira MS, et al. Structure and anticoagulant activity of sulfated galactans - Isolation of a unique sulfated galactan from the red algae Botryocladia occidentalis and comparison of its anticoagulant action with that of sulfated galactans from invertebrates. J Biol Chem 2000; 275: 29299-29307.
    • (2000) J Biol Chem , vol.275 , pp. 29299-29307
    • Farias, W.R.L.1    Valente, A.P.2    Pereira, M.S.3
  • 6
    • 0033583063 scopus 로고    scopus 로고
    • Structure and anticoagulant activity of sulfated fucans - Comparison between the regular, repetitive, and linear fucans from echinoderms with the more heterogeneous and branched polymers from brown algae
    • Pereira MS, Mulloy B, Mourão PAS. Structure and anticoagulant activity of sulfated fucans - Comparison between the regular, repetitive, and linear fucans from echinoderms with the more heterogeneous and branched polymers from brown algae. J Biol Chem 1999; 274: 7656-7667.
    • (1999) J Biol Chem , vol.274 , pp. 7656-7667
    • Pereira, M.S.1    Mulloy, B.2    Mourão, P.A.S.3
  • 7
    • 0036799656 scopus 로고    scopus 로고
    • Is there a correlation between structure and anticoagulant action of sulfated galactans and sulfated fucans?
    • Pereira MS, Melo FR, Mourão PAS. Is there a correlation between structure and anticoagulant action of sulfated galactans and sulfated fucans? Glycobiology 2002; 12: 573-580.
    • (2002) Glycobiology , vol.12 , pp. 573-580
    • Pereira, M.S.1    Melo, F.R.2    Mourão, P.A.S.3
  • 8
    • 0037137264 scopus 로고    scopus 로고
    • A 2-sulfated, 3-linked alpha-L- galactan is an anticoagulant polysaccharide
    • Pereira MS, Vilela-Silva ACES, Valente AP, et al. A 2-sulfated, 3-linked alpha-L- galactan is an anticoagulant polysaccharide. Carbohydr Res 2002; 337: 2231-2238.
    • (2002) Carbohydr Res , vol.337 , pp. 2231-2238
    • Pereira, M.S.1    Vilela-Silva, A.C.E.S.2    Valente, A.P.3
  • 9
    • 2442682767 scopus 로고    scopus 로고
    • Antithrombin-mediated anticoagulant activity of sulfated polysaccharides - different mechanisms for heparin and sulfated galactans
    • Melo FR, Pereira MS, Foguel D, et al. Antithrombin-mediated anticoagulant activity of sulfated polysaccharides - different mechanisms for heparin and sulfated galactans, J Biol Chem 2004; 279: 20824-20835.
    • (2004) J Biol Chem , vol.279 , pp. 20824-20835
    • Melo, F.R.1    Pereira, M.S.2    Foguel, D.3
  • 10
    • 33847030646 scopus 로고    scopus 로고
    • Profiling the sulfation specificities of glycosaminoglycans interactions with growth factor and chemotactic proteins using microarrays
    • Shipp EL, Hsieh-Wilson LC. Profiling the sulfation specificities of glycosaminoglycans interactions with growth factor and chemotactic proteins using microarrays. Chem Biol 2007; 14: 195-208.
    • (2007) Chem Biol , vol.14 , pp. 195-208
    • Shipp, E.L.1    Hsieh-Wilson, L.C.2
  • 11
    • 33747618728 scopus 로고    scopus 로고
    • Sulfation patterns of glycosaminoglycans encode molecular recognition and activity
    • Gama CI, Tully SE, Sotogaku N, et al. Sulfation patterns of glycosaminoglycans encode molecular recognition and activity. Nat Chem Biol 2006; 2: 467-473.
    • (2006) Nat Chem Biol , vol.2 , pp. 467-473
    • Gama, C.I.1    Tully, S.E.2    Sotogaku, N.3
  • 12
    • 0035657212 scopus 로고    scopus 로고
    • Dual effects of sulfated D-galactans from the red algae Botryocladia occidentalis preventing thrombosis and inducing platelet aggregation
    • Farias WRL, Nazareth RA, Mourão PAS. Dual effects of sulfated D-galactans from the red algae Botryocladia occidentalis preventing thrombosis and inducing platelet aggregation. Thromb Haemostasis 2001; 86: 1540-1546.
    • (2001) Thromb Haemostasis , vol.86 , pp. 1540-1546
    • Farias, W.R.L.1    Nazareth, R.A.2    Mourão, P.A.S.3
  • 13
    • 47049103979 scopus 로고    scopus 로고
    • Sulfated galactan is a catalyst of antithrombin-mediated inactivation of a-thrombin
    • Melo FR, Pereira MS, Monteiro RQ, et al. Sulfated galactan is a catalyst of antithrombin-mediated inactivation of a-thrombin. Biochim Biophys Acta 2008; 1780: 1047-1053.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 1047-1053
    • Melo, F.R.1    Pereira, M.S.2    Monteiro, R.Q.3
  • 14
    • 0026775129 scopus 로고
    • Effects of gamma-carboxyglutamic acid and epidermal growth factor-likemodules of factor IX on factor X activation. Studies using proteolytic fragments of bovine factor IX
    • Astermark J, Hogg PJ, Bjork I, et al. Effects of gamma-carboxyglutamic acid and epidermal growth factor-likemodules of factor IX on factor X activation. Studies using proteolytic fragments of bovine factor IX. J Biol Chem 1992; 267: 3249-3256.
    • (1992) J Biol Chem , vol.267 , pp. 3249-3256
    • Astermark, J.1    Hogg, P.J.2    Bjork, I.3
  • 15
    • 0026317507 scopus 로고
    • A novel one-step purification of human alpha-thrombin after direct activation of crude prothrombin enriched from plasma
    • Ngai PK, Chang JY. A novel one-step purification of human alpha-thrombin after direct activation of crude prothrombin enriched from plasma. Biochem J 1991; 280: 805-806.
    • (1991) Biochem J , vol.280 , pp. 805-806
    • Ngai, P.K.1    Chang, J.Y.2
  • 16
    • 0034602993 scopus 로고    scopus 로고
    • Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding
    • Rezaie, AR. Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding. J Biol Chem 2000; 275: 3320-3327.
    • (2000) J Biol Chem , vol.275 , pp. 3320-3327
    • Rezaie, A.R.1
  • 17
    • 33746744345 scopus 로고    scopus 로고
    • Antithrombotic properties of Ixolaris, a factor VIIa/tissue factor complex inhibitor
    • Nazareth RA, Tomaz LS, Ortiz-Costa S, et al. Antithrombotic properties of Ixolaris, a factor VIIa/tissue factor complex inhibitor. Thromb Haemost 2006; 96: 7-13.
    • (2006) Thromb Haemost , vol.96 , pp. 7-13
    • Nazareth, R.A.1    Tomaz, L.S.2    Ortiz-Costa, S.3
  • 18
    • 37549032692 scopus 로고    scopus 로고
    • Ixolaris binding to factor X reveals a precursor state of factor Xa heparin-binding exosite
    • Monteiro RQ, Rezaie AR, Bae JS, et al. Ixolaris binding to factor X reveals a precursor state of factor Xa heparin-binding exosite. Protein Sci 2008; 17: 146-153.
    • (2008) Protein Sci , vol.17 , pp. 146-153
    • Monteiro, R.Q.1    Rezaie, A.R.2    Bae, J.S.3
  • 19
    • 0036166459 scopus 로고    scopus 로고
    • Monteiro RQ, Zingali RB. Bothrojaracin, a proexosite I ligand, inhibits factor Va-accelerated prothrombin activation. Thromb Haemost 2002; 87: 288-293.
    • Monteiro RQ, Zingali RB. Bothrojaracin, a proexosite I ligand, inhibits factor Va-accelerated prothrombin activation. Thromb Haemost 2002; 87: 288-293.
  • 20
    • 0028072085 scopus 로고
    • Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator
    • Barrow RT, Parker ET, Krishnaswamy S, et al. Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator. J Biol Chem 1994; 269: 26796-26800.
    • (1994) J Biol Chem , vol.269 , pp. 26796-26800
    • Barrow, R.T.1    Parker, E.T.2    Krishnaswamy, S.3
  • 21
    • 0026063331 scopus 로고
    • Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors
    • Stenflo J. Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. Blood 1991; 78: 1637-1651.
    • (1991) Blood , vol.78 , pp. 1637-1651
    • Stenflo, J.1
  • 22
    • 0034447287 scopus 로고    scopus 로고
    • Heparin-binding exosite of factor Xa
    • Rezaie AR. Heparin-binding exosite of factor Xa. Trends Cardiovasc Med 2000; 10: 333-338.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 333-338
    • Rezaie, A.R.1
  • 23
    • 0028332939 scopus 로고
    • Molecular mapping of the heparin-binding exosite of thrombin
    • Sheehan, JP, Sadler, JE. Molecular mapping of the heparin-binding exosite of thrombin. Proc Natl Acad Sci (USA) 1994; 91: 5518-5522.
    • (1994) Proc Natl Acad Sci (USA) , vol.91 , pp. 5518-5522
    • Sheehan, J.P.1    Sadler, J.E.2
  • 24
    • 0032479424 scopus 로고    scopus 로고
    • Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa
    • Rezaie AR. Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa. J Biol Chem 1998; 273: 16824-16827.
    • (1998) J Biol Chem , vol.273 , pp. 16824-16827
    • Rezaie, A.R.1
  • 25
    • 18844445708 scopus 로고    scopus 로고
    • Ixolaris: A Factor Xa heparin-binding exosite inhibitor
    • Monteiro RQ, Rezaie AR, Ribeiro JMC, et al. Ixolaris: a Factor Xa heparin-binding exosite inhibitor. Biochem J 2005; 387: 871-877.
    • (2005) Biochem J , vol.387 , pp. 871-877
    • Monteiro, R.Q.1    Rezaie, A.R.2    Ribeiro, J.M.C.3
  • 26
    • 0022920122 scopus 로고
    • Respective role of antithrombin III and heparin cofactor II in the in vitro anticoagulant effect of heparin and of various sulfated polysaccharides
    • Sie P, Ofosu F, Fernandez F, et al. Respective role of antithrombin III and heparin cofactor II in the in vitro anticoagulant effect of heparin and of various sulfated polysaccharides. Br J Haematol 1986; 64: 707.
    • (1986) Br J Haematol , vol.64 , pp. 707
    • Sie, P.1    Ofosu, F.2    Fernandez, F.3
  • 27
    • 51349116958 scopus 로고    scopus 로고
    • Serpin-independent anticoagulant activity of a fucosylated chondroitin sulfate
    • Glauser BF, Pereira MS, Monteiro RQ, et al. Serpin-independent anticoagulant activity of a fucosylated chondroitin sulfate. Thromb Haemost 2008; 100: 420-428.
    • (2008) Thromb Haemost , vol.100 , pp. 420-428
    • Glauser, B.F.1    Pereira, M.S.2    Monteiro, R.Q.3
  • 28
    • 0028921935 scopus 로고
    • Depolymerized holothurian glycosaminoglycan with novel anticoagulant actions: Antithrombin III- and heparin cofactor II-independent inhibition of factor X activation by factor IXa-factor VIIIa complex and heparin cofactor II-dependent inhibition of thrombin
    • Nagase H, Enjyoji K, Minamiguchi K, et al. Depolymerized holothurian glycosaminoglycan with novel anticoagulant actions: antithrombin III- and heparin cofactor II-independent inhibition of factor X activation by factor IXa-factor VIIIa complex and heparin cofactor II-dependent inhibition of thrombin. Blood 1995; 85: 1527-1534.
    • (1995) Blood , vol.85 , pp. 1527-1534
    • Nagase, H.1    Enjyoji, K.2    Minamiguchi, K.3
  • 29
    • 44849115945 scopus 로고    scopus 로고
    • Contaminated heparin associated with adverse clinical events and activation of the contact system
    • Kishimoto TK, Viswanathan K, Ganguly T, et al. Contaminated heparin associated with adverse clinical events and activation of the contact system. N Engl J Med 2008; 358: 2457-2467.
    • (2008) N Engl J Med , vol.358 , pp. 2457-2467
    • Kishimoto, T.K.1    Viswanathan, K.2    Ganguly, T.3
  • 30
    • 72949092518 scopus 로고    scopus 로고
    • Holmer E. In: Heparin. Chemical and Biological Properties, Clinical Applications. 1989; pp. 575-595.
    • Holmer E. In: Heparin. Chemical and Biological Properties, Clinical Applications. 1989; pp. 575-595.
  • 31
    • 0026761832 scopus 로고
    • Low molecular weight heparin in prevention of perioperative thrombosis
    • Leizorovicz A, Haugh MC, Chapuis FR, et al. Low molecular weight heparin in prevention of perioperative thrombosis. Br Med J 1992; 305: 913-920.
    • (1992) Br Med J , vol.305 , pp. 913-920
    • Leizorovicz, A.1    Haugh, M.C.2    Chapuis, F.R.3
  • 32
    • 0026718529 scopus 로고
    • Low-molecular-weight heparin versus standard heparin in general and orthopaedic surgery: A meta-analysis
    • Nurmohamed MT, Rosendaal FR, Büller HR, et al. Low-molecular-weight heparin versus standard heparin in general and orthopaedic surgery: a meta-analysis. Lancet 1992; 340: 152-156.
    • (1992) Lancet , vol.340 , pp. 152-156
    • Nurmohamed, M.T.1    Rosendaal, F.R.2    Büller, H.R.3
  • 33
    • 0035971113 scopus 로고    scopus 로고
    • Hypersulfated low molecular weight heparin with reduced affinity for antithrombin acts as an anticoagulant by inhibiting intrinsic tenase and prothrombinase
    • Anderson JA, Fredenburgh JC, Stafford AR, et al. Hypersulfated low molecular weight heparin with reduced affinity for antithrombin acts as an anticoagulant by inhibiting intrinsic tenase and prothrombinase. J Biol Chem 2001; 276: 9755-9761.
    • (2001) J Biol Chem , vol.276 , pp. 9755-9761
    • Anderson, J.A.1    Fredenburgh, J.C.2    Stafford, A.R.3
  • 34
    • 42249112662 scopus 로고    scopus 로고
    • An algal sulfated galactan has an unusual dual effect on venous thrombosis due to activation of factor XII and inhibition of the coagulation proteases
    • Melo FR, Mourão PAS. An algal sulfated galactan has an unusual dual effect on venous thrombosis due to activation of factor XII and inhibition of the coagulation proteases. Thromb Haemost 2008; 99: 531-538.
    • (2008) Thromb Haemost , vol.99 , pp. 531-538
    • Melo, F.R.1    Mourão, P.A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.