Disintegrins: The Naturally-Occurring Antagonists of Platelet Fibrinogen Receptor

References

• Ouyang C., Teng C. M., Huang T. F. Characterization of the purified principles of Formosan snake venoms which affect blood coagulation and platelet aggregation. J. Formosan Med. Assoc. 1982; 81: 781
   Google Scholar
• Ouyang C., Teng C. M., Huang T. F. Characterization of snake venom principles affecting blood coagulation and platelet aggregation. Asia Pacific J. Pharmacol. 1987; 2: 169
   Google Scholar
• Ouyang C., Teng C. M., Huang T. F. Characterization of snake venom components acting on blood coagulation and platelet function. Toxicon 1992; 30: 945
   PubMed Web of Science ®Google Scholar
• Teng C. M., Huang T. F. Snake venom constituents that affect platelet function. Platelets 1991; 2: 77
   PubMedGoogle Scholar
• Ouyang C., Teng C. M., Huang T. F. Characterization of snake venom principles affecting blood coagulation and platelet aggregation. Fibrinogen, Thrombosis, Coagulation and Fibrinolysis, C. Y. Liu, S. Chien. Plenum Press, NY 1990; 151
   Google Scholar
• Teng C. M., Huang T. F. Inventory of exogenous inhibitors of platelet aggregation. Thrombos. Haemostas. 1991; 65: 624
   PubMed Web of Science ®Google Scholar
• Pirkle H., Theodor I. Handbook of natural toxins, Reptile venom and toxins, A. Tu. Marcel Dekker, New York 1991; Vol. 5: 226
   Google Scholar
• Teng C. M., Ko F. N., Tsai I. H., Huang M. L., Huang T. F. Trimucytin: a collagen-like aggregation inducer isolated from Trimeresurus mucrosquamatus snake venom. Thrombos. Haemostas. 1993; 69: 286
   PubMed Web of Science ®Google Scholar
• Peng M., Lu W., Kirby E. P. Alboaggregin B: A new platelet agonist that binds to platelet membrane glycoprotein lb. Biochemistry 1991; 12: 11529
   Google Scholar
• Ouyang C., Huang T. F. Potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom. Biochim. Biophys. Acta 1983; 757: 332
   PubMedGoogle Scholar
• Huang T. F., Ouyang C. Action mechanism of the potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom. Thromb. Res. 1984; 33: 125
   PubMed Web of Science ®Google Scholar
• Ouyang C., Yeh H. I., Huang T. F. A potent platelet aggregation inhibitor purified from Agkistrodon halys (Mamushi) snake venom. Toxicon 1983; 21: 979
   Web of Science ®Google Scholar
• Huang T. F., Yeh H. I., Ouyang C. Mechanism of action of the platelet aggregation inhibitor purified from Agkistrodon halys (Mamushi) snake venom. Toxicon 1984; 22: 243
   PubMed Web of Science ®Google Scholar
• Huang T. F., Wu Y. J., Ouyang C. Action mechanism of the platelet aggregation inhibitor from Calloselasma rhodostoma venom. Biochim. Biophys. Act 1987; 925: 248
   PubMedGoogle Scholar
• Ouyang C., Ma Y. H., Jih H. C., Teng C. M. Characterization of the platelet aggregation inducer and inhibitor from Echis carinatus snake venom. Biochim. Biophys. Acta 1985; 841: 1
   PubMed Web of Science ®Google Scholar
• Teng C. M., Ma Y. H., Ouyang C. Action mechanism of the platelet aggregation inducer and inhibitor from Echis carinatus snake venom. Biochim. Biophys. Acta 1985; 841: 8
   PubMedGoogle Scholar
• Huang T. F., Holt J. C., Lukasiewicz H., Niewiarowski S. Trigramin: A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex. J. Biol. Chem. 1987; 262: 16157
   PubMed Web of Science ®Google Scholar
• Huang T. F., Holt J. C., Kirby E. P., Niewiarowski S. Trigramin: Primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets. Biochemistry 1989; 28: 661
   PubMed Web of Science ®Google Scholar
• Gan Z. R., Gould R. J., Jacobs J. W., Friedman P. A., Polokoff M. A. Echistatin: A potent platelet aggregation inhibitor from the venom of the viper. Echis carinatus. J. Biol. Chem. 1988; 263: 19827
   PubMed Web of Science ®Google Scholar
• Dennis M. S., Henzel W. J., Piti R. M., Lipari M. T., Napier M. A., Deisher T. A., Bunting S., Lazarus R. A. Platelet glycoprotein IIb-IIIa protein antagonists from snake venom: evidence for a family of platelet-aggregation inhibitors. Proc. Natl. Acad. Sci. USA 1990; 87: 2471
   PubMed Web of Science ®Google Scholar
• Gould R. J., Polokoff M. A., Friedman P. A., Huang T. P., Holt J. C., Cook J. C., Niewiarowski S. Disintegrins: a family of integrin inhibitory proteins from viper venoms. Proc. Soc. Exper. Biol. Med. 1990; 195: 168
   PubMed Web of Science ®Google Scholar
• Scaborough R. M., Rose J. W., Naughton M. A., Phillips D. R., Nannizzi L., Arfsten A., Campbell A. M., Charo I. F. Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms. J. Biol. Chem. 1993; 268: 1058
   PubMed Web of Science ®Google Scholar
• Gartner T. J., Bennett J. S. The tetrapeptide analogue of cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets. J. Biol. Chem. 1985; 260: 11891
   PubMed Web of Science ®Google Scholar
• Kloczewiak M., Timmons S., Lukas T. J., Hawiger J. Platelet receptor recognition site on human fibrinogen: synthesis and structure function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain. Biochemistry 1984; 23: 1767
   PubMed Web of Science ®Google Scholar
• Takeya H., Oda K., Omori-Satoh T., Iwanaga S. The complete amino acid sequence of the high molecular mass haemorrhagic protein HRlb isolated from the venom of. Trimeresurus flavoridis. J. Biol. Chem. 1990; 265: 16068
   PubMed Web of Science ®Google Scholar
• Au L. C., Huang Y. B., Huang T. F., Choo K. B. A common precursor for a putative haemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodostoma: Molecular cloning and sequence analysis. Biochem. Biophys. Res. Comm. 1991; 181: 585
   PubMed Web of Science ®Google Scholar
• Au L. C., Chou J. S., Chang K. J., Teh G. W., Lin S. B. Nucleated sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and haemorrhagic protein from Calloselasma rhodostoma venom. Biochim. Biophys. Acta 1993; 1173: 243
   PubMedGoogle Scholar
• Neeper M. P., Jacobson M. A. Sequence of a cDNA encoding the platelet aggregation inhibitor trigramin. Nucl. Acids. Res. 1990; 18: 4255
   PubMed Web of Science ®Google Scholar
• Kini R. M., Evans H. J. Structural domains in venom proteins: Evidence that metalloproteinases and non enzymatic platelets aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon 1992; 30: 265
   PubMed Web of Science ®Google Scholar
• Peng M., Lu W., Beviglia L., Niewiarowski S., Kirby E. P. Echicetin: A snake venom protein that inhibits binding of von Willebrand factor and alboaggregin to platelet glycoprotein Ib. Blood 1993; 81: 321
   Google Scholar
• Huang T. F., Chang M. C., Peng H. C., Teng C. M. A novel α -type fibrinogenase from Agkistrodon rhodostoma snake venom. Biochim. Biophys. Acta 1992; 1160: 262
   PubMedGoogle Scholar
• Huang T. F., Chang M. C., Teng C. M. Antiplatelet protease, kistomin, selectively cleaves human platelet glycoprotein Ib. Biochim. Biophys. Acta 1993; 1158: 293
   PubMedGoogle Scholar
• Knudsen K. A., Tuszynski G. P., Huang T. F., Niewiarowski S. Trigramin, an RGD-containing peptide from snake venom, inhibits cell-substratum adhesion of human melanoma cells. Exp. Cell. Res. 1988; 179: 42
   PubMed Web of Science ®Google Scholar
• Calvete J. J., Schafer W., Soszka T., Lu W., Cork J. J., Jameson B. A., Niewiarowski S. Identification of the disulfide bond pattern in albolabrin, an RGD containing peptide from the venom of Trimeresurus albolabris: Significance for the expression of platelet aggregation inhibitory activity. Biochemistry 1991; 30: 5225
   PubMed Web of Science ®Google Scholar
• Scarborough R. M., Rose J. W., Hsu M. A., Phillips D. R., Fried V. A., Campbell A. M., Nannizzi L., Charo I. Barbourin: A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri. J. Biol. Chem. 1991; 266: 9359
   PubMed Web of Science ®Google Scholar
• Calvete J. J., Wang Y., Mann K., Schafer W., Niewiarowski S., Stewart G. J. The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin. FEBS. Lett. 1992; 309: 316
   PubMed Web of Science ®Google Scholar
• Gray W. R. Echistatin disulfide bridges: Selective reduction and linkage assignment. Protein Sci. 1993; 2: 1749
   PubMed Web of Science ®Google Scholar
• Adler M., Lazarus R. A., Dennis M. S., Wagner G. Solution structure of kistrin, a potent platelet aggregation inhibitor of GPIIb-IIIa antagonist. Science 1991; 253: 445
   PubMed Web of Science ®Google Scholar
• Adler M., Carter P., Lazarus R. A. Cysteine pairing in the glycoprotein IIb-IIIa antagonist kistrin using NMR, chemical analysis, and structure calculations. Biochemistry 1993; 32: 282
   PubMed Web of Science ®Google Scholar
• Cooke R. M., Carter B. G., Martin D. M., Murray R. Nuclear magnetic resonance studies of the snake toxin echistatin: 1H resonance assignments and secondary structure. Eur. J. Biochem. 1991; 202: 323
   PubMedGoogle Scholar
• Cooke R. M., Carter B., Rust P., Hartshorn M. J., Herzyki P., Hubband R. E. The solution structure of echistatin: evidence for disulfide bond rearrangement in homologus snake toxins. Protein Eng. 1992; 5: 473
   PubMedGoogle Scholar
• Klaus W., Broger C., Gerber P. Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data: Application to flavoridin. J. Mol. Biol. 1993; 232: 897
   PubMed Web of Science ®Google Scholar
• Saudek V., Atkinson R. A., Pelton J. T. Three-dimensional structure of echistatin, the smallest active RGD protein. Biochemistry 1991; 30: 7639
   Web of Science ®Google Scholar
• Senn H., Klaus W. The nuclear magnetic resonance solution structure of falvoridin, an antagonist of the platlelet GPIIb-IIIa receptor. J. Mol. Biol. 1993; 232: 907
   PubMed Web of Science ®Google Scholar
• Creighton T. E. Proteins: Structures and Molecular Principles. Freeman, New York 1984
   Google Scholar
• Garsky V. M., Lumma P. K., Freidinger R. M., Pitzenberger S. M., Randall W. C., Veber D. F., Gould R. J., Friedman P. A. Chemical synthesis of echistatin, a potent inhibitor of platelet aggregation from Echis carinatus: Synthesis and biological activity of selected analogs. Proc. Natl. Acad. Sci. USA 1989; 86: 4022
   PubMed Web of Science ®Google Scholar
• Dennis M. S., Carter P., Lazarus R. S. Binding interactions of kistrin with platelet glycoprotein IIb-IIIa. Analysis by site-directed mutagenesis. Proteins 1993; 15: 312
   PubMed Web of Science ®Google Scholar
• Williams J., Rucinski B., Holt J. C., Niewiarowski S. Elegantin and albolabrin purified peptides from viper venoms: Homologies with the RGDS domain of fibrinogen and von Willebrand factor. Biochim. Biophys. Acta 1990; 1039: 81
   PubMed Web of Science ®Google Scholar
• Mc Dowell R. S., Dennis M. S., Louie A., Schuster M., Mulkerrin M., Lazarus R. A. Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins. Biochemistry 1992; 31: 4766
   PubMed Web of Science ®Google Scholar
• Seymour J. L., Henzel W. J., Nevins B., Stults J. T., Lazarus R. A. Decorsin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora. J. Biol. Chem. 1990; 265: 10143
   PubMed Web of Science ®Google Scholar
• Mazur P., Henzel W. J., Seymour J. L., Lazarus R. A. Ornatins: Potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata. Eur. J. Biochem. 1991; 202: 1073
   PubMedGoogle Scholar
• Musial J., Niewiarowski S., Rucinski B., Stewart G. J., Cook J. J., Williams J. A., Edmunds L. H. Inhibition of platelet adhesion to surfaces of extracoporeal circuit by disintegrins. Circulation 1990; 82: 261
   PubMedGoogle Scholar
• Beviglia L., Poggi A., Rossi C., McLane M. A., Calabrese R., Scanziani E., Cook J. J., Niewiarowski S. Mouse antithrombotic assay. Inhibition of platelet thromboembolism by disintegrins. Thromb. Res. 1993; 71: 301
   PubMed Web of Science ®Google Scholar
• Shebuski R. T., Ramjit D. R., Bencen G. H., Polokoff M. A. Characterization of the platelet inhibitory acitvity of bitistatin, a potent arginine-glycine-aspartic acid-containing peptide from the venom of the viper. Bitis arietans. J. Biol. Chem. 1989; 264: 21550
   PubMed Web of Science ®Google Scholar
• Huang T. F., Sheu J. K., Teng C. M., Chen S. W., Lui C. S. Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex. J. Biochem. 1991; 109: 328
   PubMed Web of Science ®Google Scholar
• Huang T. F., Wang W. J., Teng C. M., Ouyang C. Mechanism of action of the antiplatelet peptide, arietin, from Bitis arietans venom. Biochim. Biophys. Acta 1991; 1074: 144
   PubMedGoogle Scholar
• Huang T. F., Peng H. C., Peng I. S., Teng C. M. An antiplatelet peptide, gabonin, from Bitis gabonica snake venom. Arch. Biochem. Biophys. 1992; 298: 13
   PubMed Web of Science ®Google Scholar
• Huang T. F., Liu C. Z., Ouyang C., Teng C. M. Halysin, an antiplatelet Arg-Gly-Asp-containing snake venom peptide, as fibrinogen receptor antagonist. Biochem. Pharmacol. 1991; 42: 1209
   PubMed Web of Science ®Google Scholar
• Williams J., Ashby B., Daniel J. L. Ligands to the platelet receptor GPIIb/IIIa do not affect agonist-induced second messengers Ca2+ or cyclic AMP. Biochem. J. 1990; 270: 149
   PubMed Web of Science ®Google Scholar
• Savage B., Marzec U. M., Chao B. H., Harker L. A., Maraganone J. M., Ruggeri Z. M. Binding of the snake venom-derived proteins applagin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb/IIIa complex inhibits receptor function. J. Biol. Chem. 1990; 265: 11766
   PubMed Web of Science ®Google Scholar
• Chao B., Jakubowski J. A., Savage B., Ping C. E., Marzee U. M., Harker L. A., Maraganore J. M. Agkistrodon pisicivorus piscivorus platelet aggregation inhibitor: A potent inhibitor of platelet activation. Proc. Natl. Acad. Sci. USA 1989; 86: 8050
   PubMed Web of Science ®Google Scholar
• Mc Lane M. A., Kowalska M. A., Silver L. Interaction of disintegrins with the αIIbβ 3 receptor on resting and activated platelets. Biochem. J. 1994
   Web of Science ®Google Scholar
• Sheu J. R., Teng C. M., Huang T. F. Triflavin, an RGD-containing anti-platelet peptide, binds to GPIIIa of ADP-stimulated platelets. Biochem. Biophys. Res. Comm. 1992; 189: 1236
   PubMed Web of Science ®Google Scholar
• Cook J. J., Huang T. F., Rucinski B., Stezyzewski M., Tuma R. F., Williams J. A., Niewiarowski S. Inhibition of platelets haemostatic plug formation by trigramin, a novel RGD-peptide. Am. J. Physiol. 1989; 256: 1038
   Google Scholar
• Shebuski R. J., Ramjit D. R., Sitko G. R., Lumma P. K., Garsky U. M. Prevention of canine coronary artery thrombosis with echistatin, a potent inhibitor of platelet aggregation from the venom of the viper. Echis carinatus. Thromb. Haemost. 1990; 64: 576
   PubMed Web of Science ®Google Scholar
• Yasuda T., Gold H. K., Leinbach R. G., Yaoita H., Fallon J. T., Guerrero L., Napier M. A., Bunting S., Collen D. Kistrin, a polypeptide platelet GPIIb/IIIa receptor antagonist, enhances and sustains coronary arterial thrombolysis with recombinant tissue-type plasminogen activator in a canine preparation. Circulation 1991; 83: 1038
   PubMed Web of Science ®Google Scholar
• Rote E. E., Mu D. X., Ronsinske R. Prevention of experimental carotid artery thrombosis by applagin. J. Pharm. Exp. Ther. 1993; 267: 828
   PubMed Web of Science ®Google Scholar
• Sheu J. R., Huang T. F. Ex-vivo and in-vivo antithrombotic effect of triflavin, an RGD-containing peptide. J. Pharm. Pharmacol. 1994; 46: 58
   PubMed Web of Science ®Google Scholar
• Shigeta O., Gluszko P., Downing S. W., Lu W., Niewiarowski S., Edmund W. H. Protection of platelets during long-term extracorporeal membrane oxygenation in sheep with a single dose of a disintegrin. Circulation 1992; 86(Suppl. II)398
   Google Scholar
• Jacobson M. A., Forma F. M., Buenage R. F. Expression and secretion of biologically active echistatin in. Saccaromyces cerevisiae. Gene 1989; 85: 511
   Google Scholar
• Chang H. H., Hu S. T., Huang T. F., Chen S., 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. Comm. 1993; 190: 242
   PubMed Web of Science ®Google Scholar
• Lazarus R., Dowell R. S. Structural and function aspects of RGD-containing protein antagonists of glycoprotein IIb-IIIa. Current Opinion Biotech 1993; 4: 438
   PubMedGoogle Scholar
• Barker P. L., Bullens S., Bunting S., Burdick D. J., Chan K. S., Deisher T., Eigenbrot C., Gadek T. R., Gantzos R., Lipari M. T., Muir G. D., Napier M. A., Pitti R. M., Padua A., Quan C., Stanley M., Struble M., Jeffrey Y. K., Burnier J. P. Cyclic RGD peptide analogues as anti-platelet antithrombotics. J. Med. Chem. 1992; 35: 2040
   PubMed Web of Science ®Google Scholar
• Hartman G. D., Egbertson M. S., Halczenko W., Laswell W. L., Duggan M. E., Smith R. L., Naylor A. M., Manno P. D., Lynch R. J., Zhang G., Chang T. C., Gould R. J. Non-peptide fibrinogen receptor antagonists. 1. Discovery and design of exosite inhibitors. J. Med. Chem. Pharm. 1992; 35: 4640
   PubMed Web of Science ®Google Scholar
• Scarborough R. M., Naughton M. A., Teng W., Rose J. W., Phillips D. R., Nannizzi L., Arfsten A., Campbell A. M., Chao I. F. Design of potent and specific integrin antagonists. Peptide antagonists with high specificity for glycoprotein IIb-IIIa. J. Biol. Chem. 1993; 268: 1066
   PubMed Web of Science ®Google Scholar
• Rucinski B., Niewiarowski S., Holt J. C., Soszka T., Knudsen K. A. Batroxostatin, an Arg-Gly-Asp containing peptide from Bothrops atrox, a potent inhibitor of platelet aggregation and cell interaction with fibronectin. Biochim. Biophys. Acta 1990; 1054: 257
   PubMedGoogle Scholar
• Soszka T., Knudsen K. A., Beviglia L., Cosmo R., Poggi A., Niewiarowski S. Inhibition of murine melanoma cell matrix adhesion and experimental metastasis by albolabrin, an RGD-containing peptide isolated from the venom of. Trimeresurus albolabris. Exp. Cell. Res. 1991; 196: 6
   PubMed Web of Science ®Google Scholar
• Sheu J. R., Lin C. H., Chung J. L., Teng C. M., Huang T. F. Triflavin, an Arg-Gly-Asp-containing anti platelet peptide inhibits cell-substratum adhesion and melanoma cell-induced lung colomization. Japn. J. Cancer. Res. 1992; 83: 885
   PubMedGoogle Scholar
• Sheu J. R., Lin C. H., Huang T. F. Triflavin, an antiplatelet peptide inhibits tumor cell-extra cellular matrix adhesion via an RGD-dependent mechanism. J. Lab. Clin. Med. 1994; 123: 256
   PubMed Web of Science ®Google Scholar
• Fidler I. J. Origin and biology of cancer metastasis. Cytometry 1989; 10: 673
   PubMedGoogle Scholar
• Menter D. G., Steinert B. W., Sloane B. F., Gundlach N., O'GaM C. Y., Marnett L. A., Diglio C., Walz D., Taylor J. D., Honn K. V. Role of platelet membrane in enhancement of tumor cell adhesion to endothelial cell extra cellular matrix. Cancer Res 1987; 47: 6751
   PubMed Web of Science ®Google Scholar
• Beviglia L., Kowalska M. A., Stewart G., et al. Disintegrins inhibit B16F10 melanoma cell metastasis by interfering with platelet aggregation and cell adhesion. J. Lab. Clin. Med.
   Google Scholar
• Sheu J. R., Lin C. H., Chung J. L., Teng C. M., Huang T. F. Triflavin, an Arg-Gly-Asp-containing snake venom peptide, inhibits aggregation of human platelets induced by human hepatoma cell line. Thromb. Res. 1992; 66: 679
   PubMed Web of Science ®Google Scholar
• Sheu J. R., Lin C. H., Peng H. C., Teng C. M., Huang T. F. Triflavin, an Arg-Gly-Asp-containing peptide, inhibits tumor cell-induced platelet aggregation. Japn. J. Cancer Res. 1993; 84: 1062
   PubMedGoogle Scholar
• Chiang H. S., Swain M. W., Huang T. F. Characterization of platelet aggregation induced by human colon adenocarcinoma cells and its inhibition by snake venom peptides, trigramin and rhodostomin. Br. J. Haematol. 1994; 87
   PubMed Web of Science ®Google Scholar
• Sato M., Sardana M. K., Grasser W. A., Garsky V. M., Murray J. M., Gould R. J. Echistain is a potent inhibitor of bone resporption in culture. J. Cell. Biol. 1990; 111: 1713
   PubMed Web of Science ®Google Scholar
• Fisher J. E., Caulfield M. P., Sato M., Quartuccio H. A., Gould R. J., Garsky V. M., Rodan G. A., Rosenblatt M. Inhibition of osteoclastic bone resorption in vivo by echistatin, an arginyl-glycyl-aspartyl (RGD)-containing protein. Endocrinol. 1993; 132: 1411
   PubMed Web of Science ®Google Scholar
• Frelinger A. L., Du X., Plow E. F., Ginsberg M. H. Monoclonal antibodies to ligand-occupied conformers of integrin α IIb β 3 (glycoprotein IIb-IIIa) alter affinity, specificity and function. J. Biol. Chem. 1991; 266: 17106
   PubMed Web of Science ®Google Scholar