Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Feb 1;90(3):928–932. doi: 10.1073/pnas.90.3.928

Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca.

Y Usami 1, Y Fujimura 1, M Suzuki 1, Y Ozeki 1, K Nishio 1, H Fukui 1, K Titani 1
PMCID: PMC45783  PMID: 8430107

Abstract

The complete amino acid sequence and location of the disulfide bonds of two-chain botrocetin, which promotes platelet agglutination in the presence of von Willebrand factor, from venom of the snake Bothrops jararaca are presented. Sequences of the alpha and beta subunits were determined by analysis of peptides generated by digestion of the S-pyridylethylated protein with Achromobacter protease I or alpha-chymotrypsin and by chemical cleavage with cyanogen bromide or 2-(2'-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine. Two-chain botrocetin is a heterodimer composed of the alpha subunit (consisting of 133 amino acid residues) and the beta subunit (consisting of 125 amino acid residues) held together by a disulfide bond. Seven disulfide bonds link half-cystine residues 2 to 13, 30 to 128, and 103 to 120 of the alpha subunit; 2 to 13, 30 to 121, and 98 to 113 of the beta subunit; and 80 of the alpha subunit to 75 of the beta subunit. In terms of amino acid sequence and disulfide bond location, two-chain botrocetin is homologous to echinoidin (a sea urchin lectin) and other C-type (Ca(2+)-dependent) lectins.

Full text

PDF
928

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews R. K., Booth W. J., Gorman J. J., Castaldi P. A., Berndt M. C. Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex. Biochemistry. 1989 Oct 17;28(21):8317–8326. doi: 10.1021/bi00447a009. [DOI] [PubMed] [Google Scholar]
  2. Brinkhous K. M., Read M. S., Fricke W. A., Wagner R. H. Botrocetin (venom coagglutinin): reaction with a broad spectrum of multimeric forms of factor VIII macromolecular complex. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1463–1466. doi: 10.1073/pnas.80.5.1463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. De Marco L., Shapiro S. S. Properties of human asialo-factor VIII. A ristocetin-independent platelet-aggregating agent. J Clin Invest. 1981 Aug;68(2):321–328. doi: 10.1172/JCI110259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem. 1988 Jul 15;263(20):9557–9560. [PubMed] [Google Scholar]
  5. Fujimura Y., Holland L. Z., Ruggeri Z. M., Zimmerman T. S. The von willebrand factor domain-mediating botrocetin-induced binding to glycoprotein IB lies between Val449 and Lys728. Blood. 1987 Oct;70(4):985–988. [PubMed] [Google Scholar]
  6. Fujimura Y., Miyata S., Nishida S., Miura S., Kaneda M., Yoshioka A., Fukui H., Katayama M., Tuddenham E. G., Usami Y. The interaction of botrocetin with normal or variant von Willebrand factor (types IIA and IIB) and its inhibition by monoclonal antibodies that block receptor binding. Thromb Haemost. 1992 Oct 5;68(4):464–469. [PubMed] [Google Scholar]
  7. Fujimura Y., Titani K., Usami Y., Suzuki M., Oyama R., Matsui T., Fukui H., Sugimoto M., Ruggeri Z. M. Isolation and chemical characterization of two structurally and functionally distinct forms of botrocetin, the platelet coagglutinin isolated from the venom of Bothrops jararaca. Biochemistry. 1991 Feb 19;30(7):1957–1964. doi: 10.1021/bi00221a032. [DOI] [PubMed] [Google Scholar]
  8. Fujimura Y., Usami Y., Titani K., Niinomi K., Nishio K., Takase T., Yoshioka A., Fukui H. Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4, which inhibits both ristocetin- and botrocetin-induced vWF binding to platelet glycoprotein Ib. Blood. 1991 Jan 1;77(1):113–120. [PubMed] [Google Scholar]
  9. Giga Y., Ikai A., Takahashi K. The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. Homologies with mammalian and insect lectins. J Biol Chem. 1987 May 5;262(13):6197–6203. [PubMed] [Google Scholar]
  10. Hermodson M. A., Ericsson L. H., Neurath H., Walsh K. A. Determination of the amino acid sequence of porcine trypsin by sequenator aalysis. Biochemistry. 1973 Aug 14;12(17):3146–3153. doi: 10.1021/bi00741a002. [DOI] [PubMed] [Google Scholar]
  11. Hirabayashi J., Kusunoki T., Kasai K. Complete primary structure of a galactose-specific lectin from the venom of the rattlesnake Crotalus atrox. Homologies with Ca2(+)-dependent-type lectins. J Biol Chem. 1991 Feb 5;266(4):2320–2326. [PubMed] [Google Scholar]
  12. Howard M. A., Firkin B. G. Ristocetin--a new tool in the investigation of platelet aggregation. Thromb Diath Haemorrh. 1971 Oct 31;26(2):362–369. [PubMed] [Google Scholar]
  13. Howard M. A., Perkin J., Salem H. H., Firkin B. G. The agglutination of human platelets by botrocetin: evidence that botrocetin and ristocetin act at different sites on the factor VIII molecule and platelet membrane. Br J Haematol. 1984 May;57(1):25–35. doi: 10.1111/j.1365-2141.1984.tb02862.x. [DOI] [PubMed] [Google Scholar]
  14. Knecht R., Chang J. Y. Liquid chromatographic determination of amino acids after gas-phase hydrolysis and derivatization with (dimethylamino)azobenzenesulfonyl chloride. Anal Chem. 1986 Oct;58(12):2375–2379. doi: 10.1021/ac00125a006. [DOI] [PubMed] [Google Scholar]
  15. Krusius T., Gehlsen K. R., Ruoslahti E. A fibroblast chondroitin sulfate proteoglycan core protein contains lectin-like and growth factor-like sequences. J Biol Chem. 1987 Sep 25;262(27):13120–13125. [PubMed] [Google Scholar]
  16. Mahoney W. C., Hermodson M. A. Separation of large denatured peptides by reverse phase high performance liquid chromatography. Trifluoroacetic acid as a peptide solvent. J Biol Chem. 1980 Dec 10;255(23):11199–11203. [PubMed] [Google Scholar]
  17. Masaki T., Tanabe M., Nakamura K., Soejima M. Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties. Biochim Biophys Acta. 1981 Jul 24;660(1):44–50. doi: 10.1016/0005-2744(81)90106-6. [DOI] [PubMed] [Google Scholar]
  18. Mohri H., Fujimura Y., Shima M., Yoshioka A., Houghten R. A., Ruggeri Z. M., Zimmerman T. S. Structure of the von Willebrand factor domain interacting with glycoprotein Ib. J Biol Chem. 1988 Dec 5;263(34):17901–17904. [PubMed] [Google Scholar]
  19. Nishio K., Fujimura Y., Niinomi K., Takahashi Y., Yoshioka A., Fukui H., Usami Y., Titani K., Ruggeri Z. M., Zimmerman T. S. Enhanced botrocetin-induced type IIB von Willebrand factor binding to platelet glycoprotein Ib initiates hyperagglutination of normal platelets. Am J Hematol. 1990 Apr;33(4):261–266. doi: 10.1002/ajh.2830330409. [DOI] [PubMed] [Google Scholar]
  20. Omenn G. S., Fontana A., Anfinsen C. B. Modification of the single tryptophan residue of staphylococcal nuclease by a new mild oxidizing agent. J Biol Chem. 1970 Apr 25;245(8):1895–1902. [PubMed] [Google Scholar]
  21. Read M. S., Potter J. Y., Brinkhous K. M. Venom coagglutinin for detection of von Willebrand factor activity in animal plasmas. J Lab Clin Med. 1983 Jan;101(1):74–82. [PubMed] [Google Scholar]
  22. Read M. S., Shermer R. W., Brinkhous K. M. Venom coagglutinin: an activator of platelet aggregation dependent on von Willebrand factor. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4514–4518. doi: 10.1073/pnas.75.9.4514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Read M. S., Smith S. V., Lamb M. A., Brinkhous K. M. Role of botrocetin in platelet agglutination: formation of an activated complex of botrocetin and von Willebrand factor. Blood. 1989 Aug 15;74(3):1031–1035. [PubMed] [Google Scholar]
  24. Rüegg U. T., Rudinger J. Reductive cleavage of cystine disulfides with tributylphosphine. Methods Enzymol. 1977;47:111–116. doi: 10.1016/0076-6879(77)47012-5. [DOI] [PubMed] [Google Scholar]
  25. Sadler J. E. von Willebrand factor. J Biol Chem. 1991 Dec 5;266(34):22777–22780. [PubMed] [Google Scholar]
  26. Spiess M., Lodish H. F. Sequence of a second human asialoglycoprotein receptor: conservation of two receptor genes during evolution. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6465–6469. doi: 10.1073/pnas.82.19.6465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Sugimoto M., Mohri H., McClintock R. A., Ruggeri Z. M. Identification of discontinuous von Willebrand factor sequences involved in complex formation with botrocetin. A model for the regulation of von Willebrand factor binding to platelet glycoprotein Ib. J Biol Chem. 1991 Sep 25;266(27):18172–18178. [PubMed] [Google Scholar]
  28. Weiss H. J., Hoyer I. W. Von Willebrand factor: dissociation from antihemophilic factor procoagulant activity. Science. 1973 Dec 14;182(4117):1149–1151. doi: 10.1126/science.182.4117.1149. [DOI] [PubMed] [Google Scholar]
  29. Wilbur W. J., Lipman D. J. Rapid similarity searches of nucleic acid and protein data banks. Proc Natl Acad Sci U S A. 1983 Feb;80(3):726–730. doi: 10.1073/pnas.80.3.726. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES