메뉴 건너뛰기




Volumn 57, Issue 5, 2011, Pages 646-656

Functional analysis of a recombinant PIII-SVMP, GST-acocostatin; an apoptotic inducer of HUVEC and HeLa, but not SK-Mel-28 cells

Author keywords

Apoptosis; Cell adhesion assays; PIII SVMP; Recombinant disintegrin like

Indexed keywords

ANNEXIN; COMPLEMENTARY DNA; DISINTEGRIN; GLUTATHIONE TRANSFERASE ACOCOSTATIN FUSION PROTEIN; HYBRID PROTEIN; INTEGRIN; INTEGRIN RECEPTOR; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 79953272002     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2011.01.007     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 50549083491 scopus 로고    scopus 로고
    • The CXC-chemokine CXCL4 interacts with integrins implicated with angiogenesis
    • Aidoudi A., Bujakowski K., Kieffer N., Bikfalvi A. The CXC-chemokine CXCL4 interacts with integrins implicated with angiogenesis. PLOS One 2008, 3:1-14.
    • (2008) PLOS One , vol.3 , pp. 1-14
    • Aidoudi, A.1    Bujakowski, K.2    Kieffer, N.3    Bikfalvi, A.4
  • 2
    • 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., Hayashi H. Involvement of specific integrins in apoptosis induced by vascular apoptosis-inducing protein 1. Toxicon 2002, 40:535-542.
    • (2002) Toxicon , vol.40 , pp. 535-542
    • Araki, S.1    Masuda, S.2    Maeda, H.3    Ying, M.J.4    Hayashi, H.5
  • 4
    • 63449129028 scopus 로고    scopus 로고
    • Syndecan-1 regulates avb3 and avb5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor
    • Beauvais D.M., Ell B.J., McWhorter A.R., Rapraeger A.C. Syndecan-1 regulates avb3 and avb5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor. J. Exp. Med. 2009, 206:691-705.
    • (2009) J. Exp. Med. , vol.206 , pp. 691-705
    • Beauvais, D.M.1    Ell, B.J.2    McWhorter, A.R.3    Rapraeger, A.C.4
  • 5
    • 0028670833 scopus 로고
    • Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels
    • Brooks P.C., Montgomery A.M., Rosenfeld M., Reisfeld R.A., Hu T., Klier G., Cheresh D.A. Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. Cell 1994, 79:1157-1164.
    • (1994) Cell , vol.79 , pp. 1157-1164
    • Brooks, P.C.1    Montgomery, A.M.2    Rosenfeld, M.3    Reisfeld, R.A.4    Hu, T.5    Klier, G.6    Cheresh, D.A.7
  • 6
  • 8
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • Carmeliet P., Jain R.K. Angiogenesis in cancer and other diseases. Nature 2000, 407:249-257.
    • (2000) Nature , vol.407 , pp. 249-257
    • Carmeliet, P.1    Jain, R.K.2
  • 9
    • 0027182176 scopus 로고
    • Rhodostomin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells
    • Chang H.H., Hu S.T., Huang T.F., Chen S.H., Lee Y.H., Lo S.J. Rhodostomin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells. Biochem. Biophys. Res. Commun. 1993, 190:242-249.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 242-249
    • Chang, H.H.1    Hu, S.T.2    Huang, T.F.3    Chen, S.H.4    Lee, Y.H.5    Lo, S.J.6
  • 11
    • 0033121275 scopus 로고    scopus 로고
    • The role of alphav integrins during angiogenesis:insights into potential mechanisms of action and clinical development
    • Eliceiri B.P., Cheresh D.A. The role of alphav integrins during angiogenesis:insights into potential mechanisms of action and clinical development. J. Clin. Invest. 1999, 103:1227-1230.
    • (1999) J. Clin. Invest. , vol.103 , pp. 1227-1230
    • Eliceiri, B.P.1    Cheresh, D.A.2
  • 13
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • Fox J.W., Serrano S.M. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45:969-985.
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.2
  • 14
    • 44349151718 scopus 로고    scopus 로고
    • Insights and speculations into snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity
    • Fox J.W., Serrano S.M. Insights and speculations into snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 2008, 275:3016-3030.
    • (2008) FEBS J. , vol.275 , pp. 3016-3030
    • Fox, J.W.1    Serrano, S.M.2
  • 17
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood J.D., Cheresh D.A. Role of integrins in cell invasion and migration. Nat. Rev. Cancer 2002, 2:91-100.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 20
    • 0026770377 scopus 로고
    • Integrins: versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 1992, 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 21
    • 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., Takeda S. Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins. FEBS Lett. 2007, 581:2416-2422.
    • (2007) FEBS Lett. , vol.581 , pp. 2416-2422
    • Igarashi, T.1    Araki, S.2    Mori, H.3    Takeda, S.4
  • 22
    • 0033958729 scopus 로고    scopus 로고
    • Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom methalloproteinase, atrolysin-A
    • Jia L.G., Wang X.M., Shannon J.D., Bjarnason J.B., Fox J.W. Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom methalloproteinase, atrolysin-A. Arch. Biochem. Biophys. 2000, 373:281-286.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 281-286
    • Jia, L.G.1    Wang, X.M.2    Shannon, J.D.3    Bjarnason, J.B.4    Fox, J.W.5
  • 23
    • 0042564783 scopus 로고    scopus 로고
    • Identification of sites in the cysteine-rich domain of the class PIII snake venom methalloproteinases responsible for inhibition of platelet function
    • Kamigutti A.S., Gallagher P., Marcinkiewicz C., Theaskston R.D., Zuzel M., Fox J.W. Identification of sites in the cysteine-rich domain of the class PIII snake venom methalloproteinases responsible for inhibition of platelet function. FEBS Lett. 2003, 549:129-134.
    • (2003) FEBS Lett. , vol.549 , pp. 129-134
    • Kamigutti, A.S.1    Gallagher, P.2    Marcinkiewicz, C.3    Theaskston, R.D.4    Zuzel, M.5    Fox, J.W.6
  • 25
    • 12844285639 scopus 로고    scopus 로고
    • The disintegrin domain of ADAM9: a ligand for multiple beta1 renal integrins
    • Mahimkar R.M., Visaya O., Pollock A.S., Lovett D.H. The disintegrin domain of ADAM9: a ligand for multiple beta1 renal integrins. Biochem. J. 2005, 385:461-468.
    • (2005) Biochem. J. , vol.385 , pp. 461-468
    • Mahimkar, R.M.1    Visaya, O.2    Pollock, A.S.3    Lovett, D.H.4
  • 27
    • 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., Sawada H., Araki S. Severe cell fragmentation in the endothelial cell apoptosis induced by snake apoptosis toxin VAP1 is an apoptotic characteristic controlled by caspases. Toxicon 2005, 46:1-6.
    • (2005) Toxicon , vol.46 , pp. 1-6
    • Maruyama, J.1    Hayashi, H.2    Miao, J.3    Sawada, H.4    Araki, S.5
  • 28
    • 0032054052 scopus 로고    scopus 로고
    • Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family
    • Masuda S., Hayashi H., Araki S. Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family. Eur. J. Biochem. 1998, 253:36-41.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 36-41
    • Masuda, S.1    Hayashi, H.2    Araki, S.3
  • 34
    • 33845693751 scopus 로고    scopus 로고
    • Mapping von Willerand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain
    • Pinto A.F.M., Terra R.M.S., Guimaraes J.A., Fox J.W. Mapping von Willerand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain. Arch. Biochem. Biophys. 2007, 457:41-46.
    • (2007) Arch. Biochem. Biophys. , vol.457 , pp. 41-46
    • Pinto, A.F.M.1    Terra, R.M.S.2    Guimaraes, J.A.3    Fox, J.W.4
  • 36
    • 0032532104 scopus 로고    scopus 로고
    • Modulation of RGD sequence motifs regulates disintegrin recognition of alphaIIb beta3 and alpha5 beta1 integrin complexes. Replacement of elegantin alanine-50 with proline, N-terminal to the RGD sequence, diminishes recognition of the alpha5 beta1 complex with restoration induced by Mn2+ cation
    • Rahman S., Aitken A., Flynn G., Formstone C., Savidge G.F. Modulation of RGD sequence motifs regulates disintegrin recognition of alphaIIb beta3 and alpha5 beta1 integrin complexes. Replacement of elegantin alanine-50 with proline, N-terminal to the RGD sequence, diminishes recognition of the alpha5 beta1 complex with restoration induced by Mn2+ cation. Biochem. J. 1998, 335:247-257.
    • (1998) Biochem. J. , vol.335 , pp. 247-257
    • Rahman, S.1    Aitken, A.2    Flynn, G.3    Formstone, C.4    Savidge, G.F.5
  • 41
    • 34447309053 scopus 로고    scopus 로고
    • Interaction of the cysteine-rich domain of snake venom methalloproteinase with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation
    • Serrano A.M.T., Wang D., Shannon J.D., Pinto A.F.M., Polanowska-Grabowska R.K., Fox J.W. Interaction of the cysteine-rich domain of snake venom methalloproteinase with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation. FEBS J. 2007, 274:3611-3621.
    • (2007) FEBS J. , vol.274 , pp. 3611-3621
    • Serrano, A.M.T.1    Wang, D.2    Shannon, J.D.3    Pinto, A.F.M.4    Polanowska-Grabowska, R.K.5    Fox, J.W.6
  • 42
    • 4444329286 scopus 로고    scopus 로고
    • Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression
    • Swenson S., Costa F., Minea R., Sherwin R.P., Ernst W., Fujii G., Yang D., Markland F.S. Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression. Mol. Cancer Ther. 2004, 3:499-511.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 499-511
    • Swenson, S.1    Costa, F.2    Minea, R.3    Sherwin, R.P.4    Ernst, W.5    Fujii, G.6    Yang, D.7    Markland, F.S.8
  • 43
  • 44
    • 38449122195 scopus 로고    scopus 로고
    • Anti-angiogenesis and RGD-containing snake venom disintegrins
    • Swenson S., Ramu S., Markland F.S. Anti-angiogenesis and RGD-containing snake venom disintegrins. Curr. Pharm. Des 2007, 13:2860-2871.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 2860-2871
    • Swenson, S.1    Ramu, S.2    Markland, F.S.3
  • 45
    • 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., Araki S. Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J. 2006, 25:2388-2396.
    • (2006) EMBO J. , vol.25 , pp. 2388-2396
    • Takeda, S.1    Igarashi, T.2    Mori, H.3    Araki, S.4
  • 49
    • 0041829403 scopus 로고    scopus 로고
    • A novel disintegrin-like domain of a high molecular weight metalloprotease inhibits platelet aggregation
    • You W.K., Jang Y.J., Chung K.H., Kim D.S. A novel disintegrin-like domain of a high molecular weight metalloprotease inhibits platelet aggregation. Biochem. Biophys. Res. Commun. 2003, 309:637-642.
    • (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
  • 50
    • 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., Kim D.S. A novel metalloprotease from Gloydius halys venom induces endothelial cell apoptosis through its protease and disintegrin-like domains. J. Biochem. 2003, 134:739-749.
    • (2003) J. Biochem. , vol.134 , pp. 739-749
    • You, W.K.1    Seo, H.J.2    Chung, K.H.3    Kim, D.S.4
  • 51
    • 28844437147 scopus 로고    scopus 로고
    • Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation
    • You W.K., Jang Y.J., Chung K.H., Jeon O.H., Kim D.S. Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation. Biochem. Biophys. Res. Commun. 2006, 339:964-970.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 964-970
    • You, W.K.1    Jang, Y.J.2    Chung, K.H.3    Jeon, O.H.4    Kim, D.S.5
  • 54
    • 77954568888 scopus 로고    scopus 로고
    • Thy-1- Integrin avb5 interactions inhibit lung fibroblast contraction-induced latent transforming growth factor-b1 activation and myofibroblast differentiation
    • Zhou Y., Hagood J.S., Lu B., Merryman W.D., Murphy-Ulrich J.E. Thy-1- Integrin avb5 interactions inhibit lung fibroblast contraction-induced latent transforming growth factor-b1 activation and myofibroblast differentiation. J. Biol. Chem. 2010, 285:22382-22393.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22382-22393
    • Zhou, Y.1    Hagood, J.S.2    Lu, B.3    Merryman, W.D.4    Murphy-Ulrich, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.