메뉴 건너뛰기




Volumn 339, Issue 3, 2006, Pages 964-970

Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation

Author keywords

Collagen; Disintegrin like domain; Fibrinogen; Hemorrhagic metalloprotease; Platelet aggregation; Snake venom

Indexed keywords

SNAKE VENOM;

EID: 28844437147     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.11.083     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 0029055393 scopus 로고
    • Snake venom metalloendopepidase: Reprolysins
    • J.B. Bjarnason, and J.W. Fox Snake venom metalloendopepidase: reprolysins Methods Enzymol. 248 1995 345 368
    • (1995) Methods Enzymol. , vol.248 , pp. 345-368
    • Bjarnason, J.B.1    Fox, J.W.2
  • 2
    • 0028337108 scopus 로고
    • CDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins
    • L.A. Hite, L.G. Jia, J.B. Bjarnason, and J.W. Fox cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins Arch. Biochem. Biophys. 308 1994 182 191
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 3
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • T. Matsui, Y. Fujimura, and K. Titani Snake venom proteases affecting hemostasis and thrombosis Biochim. Biophys. Acta 1477 2000 146 156
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 4
    • 0027193420 scopus 로고
    • Primary structure of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhgic metalloproteinase and new fluorogenic peptide substrates for these enzymes
    • H. Takeya, S. Nishida, N. Nishino, Y. Makinose, T. Omori-Satoh, H. Nikai, H. Sugihara, and S. Iwanaga Primary structure of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhgic metalloproteinase and new fluorogenic peptide substrates for these enzymes J. Biochem. 113 1993 473 483
    • (1993) J. Biochem. , vol.113 , pp. 473-483
    • Takeya, H.1    Nishida, S.2    Nishino, N.3    Makinose, Y.4    Omori-Satoh, T.5    Nikai, H.6    Sugihara, H.7    Iwanaga, S.8
  • 5
    • 0028246347 scopus 로고
    • Inventory of haemorrhagic factors from snake venoms. Registry of Exogenous Hemostatic Factors. Scientific and Standardisation Committee of the International Society on Thrombosis and Haemostasis
    • N. Marsh Inventory of haemorrhagic factors from snake venoms. Registry of Exogenous Hemostatic Factors. Scientific and Standardisation Committee of the International Society on Thrombosis and Haemostasis Thromb. Haemost. 71 1994 793 797
    • (1994) Thromb. Haemost. , vol.71 , pp. 793-797
    • Marsh, N.1
  • 6
    • 0028150753 scopus 로고
    • Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors
    • S. Niewiarowski, M.A. McLane, M. Kloczewiak, and G.J. Stewart Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors Semin. Hematol. 31 1994 289 300
    • (1994) Semin. Hematol. , vol.31 , pp. 289-300
    • Niewiarowski, S.1    McLane, M.A.2    Kloczewiak, M.3    Stewart, G.J.4
  • 7
  • 8
    • 19544372787 scopus 로고    scopus 로고
    • Jararhagin and its multiple effects on hemostasis
    • G.D. Laing, and A.M. Moura-da-Silva Jararhagin and its multiple effects on hemostasis Toxicon 34 2005 987 996
    • (2005) Toxicon , vol.34 , pp. 987-996
    • Laing, G.D.1    Moura-Da-Silva, A.M.2
  • 9
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage
    • J.M. Gutierrez, A. Rucavado, T. Escalante, and C. Diaz Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage Toxicon 45 2005 997 1011
    • (2005) Toxicon , vol.45 , pp. 997-1011
    • Gutierrez, J.M.1    Rucavado, A.2    Escalante, T.3    Diaz, C.4
  • 10
    • 0347993780 scopus 로고    scopus 로고
    • A novel metalloprotease from Gloydius halys venom induces endothelial cell apoptosis by its protease and disintegrin-like domains
    • W.K. You, H.J. Seo, K.H. Chung, and D.S. Kim A novel metalloprotease from Gloydius halys venom induces endothelial cell apoptosis by its protease and disintegrin-like domains J. Biochem. 134 2003 739 749
    • (2003) J. Biochem. , vol.134 , pp. 739-749
    • You, W.K.1    Seo, H.J.2    Chung, K.H.3    Kim, D.S.4
  • 11
    • 0032916298 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a cDNA encoding snake venom metalloprotease
    • O.H. Jeon, and D.S. Kim Cloning, expression, and characterization of a cDNA encoding snake venom metalloprotease Biochem. Mol. Biol. Int. 47 1999 417 425
    • (1999) Biochem. Mol. Biol. Int. , vol.47 , pp. 417-425
    • Jeon, O.H.1    Kim, D.S.2
  • 12
    • 0033565573 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a snake venom metalloprotease
    • O.H. Jeon, and D.S. Kim Molecular cloning and functional characterization of a snake venom metalloprotease Eur. J. Biochem. 263 1999 526 533
    • (1999) Eur. J. Biochem. , vol.263 , pp. 526-533
    • Jeon, O.H.1    Kim, D.S.2
  • 13
    • 0041829403 scopus 로고    scopus 로고
    • A novel disintegrin-like domain of a high molecular weight metalloprotease inhibits platelet aggregation
    • W.K. You, Y.J. Jang, K.H. Chung, and D.S. Kim A novel disintegrin-like domain of a high molecular weight metalloprotease inhibits platelet aggregation Biochem. Biophys. Res. Commun. 309 2003 637 642
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 637-642
    • You, W.K.1    Jang, Y.J.2    Chung, K.H.3    Kim, D.S.4
  • 15
    • 0021734026 scopus 로고
    • Effect of calcium on proteolytic activity and conformation of hemorrhagic toxin I from five pace snake (Agkistrodon acutus) venom
    • J. Zhang, Z. Chen, Y. He, and X. Xu Effect of calcium on proteolytic activity and conformation of hemorrhagic toxin I from five pace snake (Agkistrodon acutus) venom Toxicon 22 1984 931 935
    • (1984) Toxicon , vol.22 , pp. 931-935
    • Zhang, J.1    Chen, Z.2    He, Y.3    Xu, X.4
  • 16
    • 0026099011 scopus 로고
    • Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex
    • T.F. Huang, J.R. Sheu, C.M. Teng, S.W. Chen, and C.S. Liu Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex J. Biochem. 109 1991 328 334
    • (1991) J. Biochem. , vol.109 , pp. 328-334
    • Huang, T.F.1    Sheu, J.R.2    Teng, C.M.3    Chen, S.W.4    Liu, C.S.5
  • 18
    • 0032527808 scopus 로고    scopus 로고
    • Purification and molecular cloning of a platelet aggregation inhibitor from the snake (Agkistrodon halys brevicaudus) venom
    • I.C. Kang, K.H. Chung, S.J. Lee, Y.D. Yun, H.M. Moon, and D.S. Kim Purification and molecular cloning of a platelet aggregation inhibitor from the snake (Agkistrodon halys brevicaudus) venom Thromb. Res. 91 1998 65 73
    • (1998) Thromb. Res. , vol.91 , pp. 65-73
    • Kang, I.C.1    Chung, K.H.2    Lee, S.J.3    Yun, Y.D.4    Moon, H.M.5    Kim, D.S.6
  • 19
    • 0036027969 scopus 로고    scopus 로고
    • Purification and characterisation of two hemorrhagic metalloproteinases from the venom of the long-nosed viper, Vipera ammodytes ammodytes
    • A. Leonardi, F. Gubensek, and I. Krizaj Purification and characterisation of two hemorrhagic metalloproteinases from the venom of the long-nosed viper, Vipera ammodytes ammodytes Toxicon 40 2002 55 62
    • (2002) Toxicon , vol.40 , pp. 55-62
    • Leonardi, A.1    Gubensek, F.2    Krizaj, I.3
  • 22
    • 0037410214 scopus 로고    scopus 로고
    • Platelets in hemostasis and thrombosis: Role of integrins and their ligands
    • H. Ni, and J. Freedman Platelets in hemostasis and thrombosis: role of integrins and their ligands Transfus. Apheresis Sci. 28 2003 257 264
    • (2003) Transfus. Apheresis Sci. , vol.28 , pp. 257-264
    • Ni, H.1    Freedman, J.2
  • 23
    • 23944518374 scopus 로고    scopus 로고
    • Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 a resolution
    • S. Bilgrami, S. Yadav, P. Kaur, S. Sharma, M. Perbandt, C. Betzel, and T.P. Singh Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 A resolution Biochemistry 44 2005 11058 11066
    • (2005) Biochemistry , vol.44 , pp. 11058-11066
    • Bilgrami, S.1    Yadav, S.2    Kaur, P.3    Sharma, S.4    Perbandt, M.5    Betzel, C.6    Singh, T.P.7
  • 24
    • 0032582674 scopus 로고    scopus 로고
    • Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus
    • W. Gong, X. Zhu, S. Liu, M. Teng, and L. Niu Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus J. Mol. Biol. 283 1998 657 668
    • (1998) J. Mol. Biol. , vol.283 , pp. 657-668
    • Gong, W.1    Zhu, X.2    Liu, S.3    Teng, M.4    Niu, L.5
  • 26
    • 0035783370 scopus 로고    scopus 로고
    • Three-dimensional structure of fibrolase, the fibrinolytic enzyme from southern copperhead venom, modeled from the X-ray structure of adamalysin II and atrolysin C
    • M.B. Bolger, S. Swenson, and F.S. Markland Jr. Three-dimensional structure of fibrolase, the fibrinolytic enzyme from southern copperhead venom, modeled from the X-ray structure of adamalysin II and atrolysin C AAPS Pharm. Sci. 3 2001 E16
    • (2001) AAPS Pharm. Sci. , vol.3 , pp. 16
    • Bolger, M.B.1    Swenson, S.2    Markland Jr., F.S.3
  • 27
    • 0028176523 scopus 로고
    • Refined 2.0 Å X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin
    • F.X. Gomis-Rüth, L.F. Kress, J. Kellermann, I. Mayr, X. Lee, R. Huber, and W. Bode Refined 2.0 Å X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin J. Mol. Biol. 239 1994 513 544
    • (1994) J. Mol. Biol. , vol.239 , pp. 513-544
    • Gomis-Rüth, F.X.1    Kress, L.F.2    Kellermann, J.3    Mayr, I.4    Lee, X.5    Huber, R.6    Bode, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.