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Volumn 52, Issue 4, 2008, Pages 589-593

Hemorrhagic activity of the vascular apoptosis-inducing proteins VAP1 and VAP2 from Crotalus atrox

Author keywords

Apoptosis; Endothelial cell; Hemorrhage; Snake venom; Vascular

Indexed keywords

SNAKE VENOM; TOXIN; UNCLASSIFIED DRUG; VASCULAR APOPTOSIS INDUCING PROTEIN 1; VASCULAR APOPTOSIS INDUCING PROTEIN 2;

EID: 50949110231     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2008.06.027     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0025288244 scopus 로고
    • Apoptosis of vascular endothelial cells by fibroblast growth factor deprivation
    • Araki S., Shimada Y., Kaji K., and Hayashi H. Apoptosis of vascular endothelial cells by fibroblast growth factor deprivation. Biochem. Biophys. Res. Commun. 168 (1990) 1194-1200
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 1194-1200
    • Araki, S.1    Shimada, Y.2    Kaji, K.3    Hayashi, H.4
  • 3
    • 0036162143 scopus 로고    scopus 로고
    • Involvement of specific integrins in apoptosis induced by vascular apoptosis-inducing protein 1
    • Araki S., Masuda S., Maeda H., Ying M.J., and Hayashi H. Involvement of specific integrins in apoptosis induced by vascular apoptosis-inducing protein 1. Toxicon 40 (2002) 535-542
    • (2002) Toxicon , vol.40 , pp. 535-542
    • Araki, S.1    Masuda, S.2    Maeda, H.3    Ying, M.J.4    Hayashi, H.5
  • 5
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • Bjarnason J.B., and Fox J.W. Hemorrhagic metalloproteinases from snake venoms. Pharmacol. Ther. 62 (1994) 325-372
    • (1994) Pharmacol. Ther. , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 6
    • 0017883906 scopus 로고
    • Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin
    • Bjarnason J.B., and Tu A.T. Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin. Biochemistry 17 (1978) 3395-3404
    • (1978) Biochemistry , vol.17 , pp. 3395-3404
    • Bjarnason, J.B.1    Tu, A.T.2
  • 7
    • 0027724639 scopus 로고
    • Purification and partial characterization of a haemorrhagin (VRH-1) from Vipera russelli russelli venom
    • Chakrabarty D., Bhattacharyya D., Sarkar H.S., and Lahiri S.C. Purification and partial characterization of a haemorrhagin (VRH-1) from Vipera russelli russelli venom. Toxicon 31 (1993) 1601-1614
    • (1993) Toxicon , vol.31 , pp. 1601-1614
    • Chakrabarty, D.1    Bhattacharyya, D.2    Sarkar, H.S.3    Lahiri, S.C.4
  • 8
    • 33750729279 scopus 로고    scopus 로고
    • Novel insights into capillary vessel basement membrane damage by snake venom hemorrhagic metalloproteinases: a biochemical and immunohistochemical study
    • Escalante T., Shannon J., Moura-da-Silva A.M., Gutiérrez J.M., and Fox J.W. Novel insights into capillary vessel basement membrane damage by snake venom hemorrhagic metalloproteinases: a biochemical and immunohistochemical study. Arch Biochem Biophys. 455 (2006) 144-153
    • (2006) Arch Biochem Biophys. , vol.455 , pp. 144-153
    • Escalante, T.1    Shannon, J.2    Moura-da-Silva, A.M.3    Gutiérrez, J.M.4    Fox, J.W.5
  • 9
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage
    • Gutiérrez J.M., Rucavado A., Escalante T., and Di'az C. 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
    • Gutiérrez, J.M.1    Rucavado, A.2    Escalante, T.3    Di'az, C.4
  • 10
    • 34248594754 scopus 로고    scopus 로고
    • Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins
    • Igarashi T., Araki S., Mori H., and Takeda S. Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins. FEBS Lett. 581 13 (2007) 2416-2422
    • (2007) FEBS Lett. , vol.581 , Issue.13 , pp. 2416-2422
    • Igarashi, T.1    Araki, S.2    Mori, H.3    Takeda, S.4
  • 11
    • 0027522654 scopus 로고
    • Isolation of a hemorrhagic toxin from the venom of Agkistrodon contortrix laticinctus (broad-banded copperhead) and pathogenesis of the hemorrhage induced by the toxin in mice
    • Johnson E.K., and Ownby C.L. Isolation of a hemorrhagic toxin from the venom of Agkistrodon contortrix laticinctus (broad-banded copperhead) and pathogenesis of the hemorrhage induced by the toxin in mice. Int. J. Biochem. 25 (1993) 267-278
    • (1993) Int. J. Biochem. , vol.25 , pp. 267-278
    • Johnson, E.K.1    Ownby, C.L.2
  • 12
    • 0029949611 scopus 로고    scopus 로고
    • Inhibition of collagen-induced platelet aggregation as the result of cleavage of alpha 2 beta 1-integrin by the snake venom metalloproteinase jararhagin
    • Kamiguti A.S., Hay C.R., and Zuzel M. Inhibition of collagen-induced platelet aggregation as the result of cleavage of alpha 2 beta 1-integrin by the snake venom metalloproteinase jararhagin. Biochem. J. 320 Pt 2 (1996) 635-641
    • (1996) Biochem. J. , vol.320 , Issue.PART 2 , pp. 635-641
    • Kamiguti, A.S.1    Hay, C.R.2    Zuzel, M.3
  • 13
    • 0021159440 scopus 로고
    • Comparative study of Agkistrodon acutus venoms from China and Taiwan
    • Komori Y., Nikai T., and Sugihara H. Comparative study of Agkistrodon acutus venoms from China and Taiwan. Comp. Biochem. Physiol. C 79 (1984) 51-57
    • (1984) Comp. Biochem. Physiol. C , vol.79 , pp. 51-57
    • Komori, Y.1    Nikai, T.2    Sugihara, H.3
  • 14
    • 33746754703 scopus 로고    scopus 로고
    • Ox-LDL induces apoptosis in human coronary artery endothelial cells: role of PKC, PTK, bcl-2, and Fas
    • Li D., Yang B., and Mehta J.L. Ox-LDL induces apoptosis in human coronary artery endothelial cells: role of PKC, PTK, bcl-2, and Fas. Am. J. Physiol. 275 (1998) H568-H576
    • (1998) Am. J. Physiol. , vol.275
    • Li, D.1    Yang, B.2    Mehta, J.L.3
  • 15
    • 20444438034 scopus 로고    scopus 로고
    • Severe cell fragmentation in the endothelial cell apoptosis induced by snake apoptosis toxin VAP1 is an apoptotic characteristic controlled by caspases
    • Maruyama J., Hayashi H., Miao J.Y., Sawada H., and Araki S. Severe cell fragmentation in the endothelial cell apoptosis induced by snake apoptosis toxin VAP1 is an apoptotic characteristic controlled by caspases. Toxicon 46 (2005) 1-6
    • (2005) Toxicon , vol.46 , pp. 1-6
    • Maruyama, J.1    Hayashi, H.2    Miao, J.Y.3    Sawada, H.4    Araki, S.5
  • 16
    • 0031560913 scopus 로고    scopus 로고
    • Purification of a vascular apoptosis-inducing factor from hemorrhagic snake venom
    • Masuda S., Araki S., Kaji K., and Hayashi H. Purification of a vascular apoptosis-inducing factor from hemorrhagic snake venom. Biochem. Biophys. Res. Commun. 235 (1997) 59-63
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 59-63
    • Masuda, S.1    Araki, S.2    Kaji, K.3    Hayashi, H.4
  • 17
    • 0032054052 scopus 로고    scopus 로고
    • Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family
    • Masuda S., Hayashi H., and Araki S. Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family. Eur. J. Biochem. 253 (1998) 36-41
    • (1998) Eur. J. Biochem. , vol.253 , pp. 36-41
    • Masuda, S.1    Hayashi, H.2    Araki, S.3
  • 18
    • 0034838815 scopus 로고    scopus 로고
    • Purification, cDNA cloning and characterization of the vascular apoptosis-inducing protein, HV1, from Trimeresurus flavoviridis
    • Masuda S., Hayashi H., Atoda H., Morita T., and Araki S. Purification, cDNA cloning and characterization of the vascular apoptosis-inducing protein, HV1, from Trimeresurus flavoviridis. Eur. J. Biochem. 268 (2001) 3339-3345
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3339-3345
    • Masuda, S.1    Hayashi, H.2    Atoda, H.3    Morita, T.4    Araki, S.5
  • 19
    • 34248549047 scopus 로고    scopus 로고
    • cDNA cloning and some additional peptide characterization of a single-chain vascular apoptosis-inducing protein, VAP2
    • Masuda S., Maeda H., Miao J.Y., Hayashi H., and Araki S. cDNA cloning and some additional peptide characterization of a single-chain vascular apoptosis-inducing protein, VAP2. Endothelium 14 (2007) 89-96
    • (2007) Endothelium , vol.14 , pp. 89-96
    • Masuda, S.1    Maeda, H.2    Miao, J.Y.3    Hayashi, H.4    Araki, S.5
  • 23
    • 0018800011 scopus 로고
    • Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts
    • Omori-Satoh T., and Sadahiro S. Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts. Biochim. Biophys. Acta 580 (1979) 392
    • (1979) Biochim. Biophys. Acta , vol.580 , pp. 392
    • Omori-Satoh, T.1    Sadahiro, S.2
  • 24
    • 0015445187 scopus 로고
    • Studies on snake venom hemorrhagic factor I (HR-I) in the venom of Agkistrodon halys blomhoffi
    • Oshima G., Ohmari-Satoh T., Iwanaga S., and Suzuki T. Studies on snake venom hemorrhagic factor I (HR-I) in the venom of Agkistrodon halys blomhoffi. J. Biochem. 72 (1972) 1483
    • (1972) J. Biochem. , vol.72 , pp. 1483
    • Oshima, G.1    Ohmari-Satoh, T.2    Iwanaga, S.3    Suzuki, T.4
  • 25
    • 0002645946 scopus 로고
    • Locally acting agents: myotoxins, hemorrhagic toxins and dermonecrotic factors
    • Shier W.T., and Mebs D. (Eds), Marcel Dekker, New York
    • Ownby C.L. Locally acting agents: myotoxins, hemorrhagic toxins and dermonecrotic factors. In: Shier W.T., and Mebs D. (Eds). Handbook of Toxinology (1990), Marcel Dekker, New York 602-654
    • (1990) Handbook of Toxinology , pp. 602-654
    • Ownby, C.L.1
  • 27
    • 0014965886 scopus 로고
    • Purification and some properties of two hemorrhagic principles (HR2a and HR2b) in the venom of Trimeresurus flavoviridis; complete separation of the principles from proteolytic activity
    • Takahashi T., and Osaka A. Purification and some properties of two hemorrhagic principles (HR2a and HR2b) in the venom of Trimeresurus flavoviridis; complete separation of the principles from proteolytic activity. Biochim. Biophys. Acta 207 (1970) 65-75
    • (1970) Biochim. Biophys. Acta , vol.207 , pp. 65-75
    • Takahashi, T.1    Osaka, A.2
  • 28
    • 33745731954 scopus 로고    scopus 로고
    • Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
    • Takeda S., Igarashi T., Mori H., and Araki S. Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J. 25 (2006) 2388-2396
    • (2006) EMBO J. , vol.25 , pp. 2388-2396
    • Takeda, S.1    Igarashi, T.2    Mori, H.3    Araki, S.4
  • 29
    • 0024997837 scopus 로고
    • The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis
    • Takeya H., Oda K., Miyata T., Omori-Satoh T., and Iwanaga S. The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis. J. Biol. Chem. 265 (1990) 16068-16073
    • (1990) J. Biol. Chem. , vol.265 , pp. 16068-16073
    • Takeya, H.1    Oda, K.2    Miyata, T.3    Omori-Satoh, T.4    Iwanaga, S.5
  • 30
    • 0344517097 scopus 로고
    • Distribution of 125 I-labelled Russell's viper (Vipera russell) venom in mice
    • Than T., Thwin M.M., Pe U., and San M.K. Distribution of 125 I-labelled Russell's viper (Vipera russell) venom in mice. Snake 17 (1985) 124-130
    • (1985) Snake , vol.17 , pp. 124-130
    • Than, T.1    Thwin, M.M.2    Pe, U.3    San, M.K.4
  • 31
    • 0021061641 scopus 로고
    • Development of simple standard assay procedures for the characterization of snake venoms
    • Theakston R.D.G., and Reid H.A. Development of simple standard assay procedures for the characterization of snake venoms. Bull. WHO 61 (1983) 949-956
    • (1983) Bull. WHO , vol.61 , pp. 949-956
    • Theakston, R.D.G.1    Reid, H.A.2
  • 33
    • 27644597567 scopus 로고    scopus 로고
    • Primary structure and antiplatelet mechanism of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom
    • Wang W.J., Shih C.H., and Huang T.F. Primary structure and antiplatelet mechanism of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom. Biochimie 87 (2005) 1065-1077
    • (2005) Biochimie , vol.87 , pp. 1065-1077
    • Wang, W.J.1    Shih, C.H.2    Huang, T.F.3
  • 34
    • 0347993780 scopus 로고    scopus 로고
    • A novel metalloprotease from Gloydius halys venom induces endothelial cell apoptosis through its protease and disintegrin-like domains
    • You W.K., Seo H.J., Chung K.H., and Kim D.S. A novel metalloprotease from Gloydius halys venom induces endothelial cell apoptosis through its protease and disintegrin-like domains. J. Biochem. (Tokyo) 134 (2003) 739-749
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 739-749
    • You, W.K.1    Seo, H.J.2    Chung, K.H.3    Kim, D.S.4
  • 35
    • 0029105096 scopus 로고
    • Molecular cloning and expression of catrocollastatin, a snake venom protein from Crotarus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen
    • Zhou Q., Smith J.B., and Grossman M.H. Molecular cloning and expression of catrocollastatin, a snake venom protein from Crotarus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen. Biochem. J. 307 (1995) 411-417
    • (1995) Biochem. J. , vol.307 , pp. 411-417
    • Zhou, Q.1    Smith, J.B.2    Grossman, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.