cDNA Cloning and Some Additional Peptide Characterization of a Single-Chain Vascular Apoptosis-Inducing Protein, VAP2

REFERENCES

• Araki S., Ishida T., Yamamoto T., Kaji K., Hayashi H. Induction of apoptosis by hemorrhagic snake venom in vascular endothelial cells. Biochemical and Biophysical Research Communications, 1993; 190: 148–153
   PubMed Web of Science ®Google Scholar
• Araki S., Masuda S., Maeda H., Miao J. Y., Hayashi H. Involvement of specific integrins in apoptosis induced by vascular apoptosis-inducing protein 1. Toxicon, 2002; 40: 535–542
   PubMedGoogle Scholar
• Araki S., Shimada Y., Kaji K., Hayashi H. Apoptosis of vascular endothelial cells by fibroblast growth factor deprivation. Biochemical and Biophysical Research Communications, 1990; 168: 1194–1200
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Gutier´rez J. M., Rucavado A., Escalante T., Diáz C. Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage. Toxicon, 2005; 45: 997–1011
   PubMed Web of Science ®Google Scholar
• Hite L. A., Jia L. G., Bjarnason J. B., Fox J. W. cDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins. Archives of Biochemistry and Biophysics, 1994; 308: 182–191
   PubMed Web of Science ®Google Scholar
• Jaffe E. A., Nachman R. L., Becher C. G., Minick R. C. Culture of human endothelial cells derived from umbilical veins. Journal of Clinical Investigation, 1973; 52: 2745–2756
   PubMed Web of Science ®Google Scholar
• 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 metalloproteinase, atrolysin A. Archives of Biochemistry and Biophysics, 2000; 373: 281–286
   PubMed Web of Science ®Google Scholar
• Kondo S., Kondo Y., Yin D., Barnett G. H., Kaakaji R., Peterson J. W., Morimura T., Kubo H., Takeuchi J., Barna B. P. Involvement of interleukin-1 beta-converting enzyme in apoptosis of bFGF-deprived murine aortic endothelial cells. FASEB Journal 1996; 10: 1192–1197
   PubMed Web of Science ®Google Scholar
• Li D., Yang B., Mehta J. L. Ox-LDL induces apoptosis in human coronary artery endothelial cells: Role of PKC, PTK, bcl-2, and Fas. American Journal of Physiology, 1998; 275: H568–H576
   PubMedGoogle Scholar
• Masuda S., Araki S., Kaji K., Hayashi H. Purification of a vascular apoptosis-inducing factor from hemorrhagic snake venom. Biochemical and Biophysical Research Communications, 1997; 235: 59–63
   PubMed Web of Science ®Google Scholar
• Masuda S., Hayashi H., Araki S. Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family. European Journal of Biochemistry, 1998; 253: 36–41
   PubMedGoogle Scholar
• Masuda S., Hayashi H., Atoda H., Morita T., Araki S. Purification, cDNA cloning and characterization of the vascular apoptosis-inducing protein, HV1, from Trimeresurus flavoviridis. European Journal of Biochemistry, 2001; 268: 3339–3345
   PubMedGoogle Scholar
• Masuda S., Ohta T., Kaji K., Fox J. W., Hayashi H., Araki S. cDNA cloning and characterization of vascular apoptosis-inducing protein 1. Biochemical and Biophysical Research Communications, 2000; 278: 197–204
   PubMedGoogle Scholar
• Maruyama J., Hayashi H., Miao J. Y., 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
   PubMed Web of Science ®Google Scholar
• Meredith J. E., Jr., Fazeli B., Schwartz M. A. The extracellular matrix as a cell survival factor. Molecular Biology of the Cell, 1993; 4: 953–961
   PubMed Web of Science ®Google Scholar
• Paine M. J., Desmond H. P., Theakston R. D., Crampton J. M. Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family. Journal of Biological Chemistry, 1992; 267: 22869–22876
   PubMed Web of Science ®Google Scholar
• Qing Z., Smith J. B., 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. Biochemical Journal, 1995; 307: 411–417
   PubMed Web of Science ®Google Scholar
• Schattner M., Fritzen M., Ventura Jde S., de Albuquerque Modesto J. C., Pozner R. G., Moura-da-Silva A. M., Chudzinski-Tavassi A. M. The snake venom metalloproteases berythractivase and jararhagin activate endothelial cells. Biology Chemistry, 2005; 386: 369–374
   PubMed Web of Science ®Google Scholar
• Serrano S. M., Jia L. G., Wang D., Shannon J. D., Fox J. W. Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: Targeting adhesion proteins collagen I and von Willebrand factor. Biochemical Journal, 2005; 391: 69–76
   PubMed Web of Science ®Google Scholar
• 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
   PubMedGoogle Scholar
• Takeya H., Nishida S., Nishino N., Makinose Y., Omori-Satoh T., Nikai T., Sugihara H., Iwanaga S. Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes. Journal of Biochemistry (Tokyo), 1993; 113: 473–483
   PubMedGoogle Scholar
• Tanjoni I., Weinlich R., Della-Casa M. S., Clissa P. B., Saldanha-Gama R. F., de Freitas M. S., Barja-Fidalgo C., Amarante-Mendes G. P., Moura-da-Silva A. M. Jararhagin, a snake venom metalloproteinase, induces a specialized form of apoptosis (anoikis) selective to endothelial cells. Apoptosis, 2005; 10: 851–861
   PubMed Web of Science ®Google Scholar
• Trummal K., Tonismagi K., Siigur E., Aaspollu A., Lopp A., Sillat T., Saat R., Kasak L., Tammiste I., Kogerman P., Kalkkinen N., Siigur J. A novel metalloprotease from Vipera lebetina venom induces human endothelial cell apoptosis. Toxicon, 2005; 46: 46–61
   PubMed Web of Science ®Google Scholar
• Wu W. B., Chang S. C., Liau M. Y., Huang T. F. Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells. Biochemical J ournal 2001; 357: 719–728
   PubMed Web of Science ®Google Scholar
• 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. Journal of Biochemistry (Tokyo), 2003; 134: 739–749
   PubMed Web of Science ®Google Scholar