Kinins pp 157-175 | Cite as

Mechanism of Clostripain-Induced Kinin Release from Human, Rat and Canine Plasma

  • B. B. Vargaftig
  • E. L. Giroux
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 70)


Clostripain (clostridiopeptidase B, E.C. is a thiol proteinase found in extracts from cultures of Clostridium histolyticum (Ogle and Tytell, 1953; Labouesse and Gros, 1960), and displays a marked specificity for the carboxyl linkage of arginine (Gros and Labouesse, 1960; Mitchell and Harrington, 1968). Clostripain has been reported to release kinin-like polypeptides directly from bovine or horse kininogen-containing preparations (Prado, et al., 1956; Prado and Prado, 1962). In the course of investigations concerning the haemorrhagic and pro-inflammatory activity of bacterial collagenase (Giroux, Lefort and Vargaftig, 1976) we found that clostripain, a contaminant of one collagenase preparation, displayed indirect kinin-releasing activities which had not been described before. This communication reports our investigation of the mechanism of such release.


Trypsin Inhibitor Kinin Activity Amidase Activity Dexamethasone Phosphate Hexadimethrine Bromide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Back, N. and Steger, R. (1968), Fed. Proc., 27 96–99.PubMedGoogle Scholar
  2. Cochrane, C.G., and Wuepper, K.D. (1971), in Immunopathology of Inflammation (B.K. Forscher and J.C. Houck, eds.), Exerpta Medica, Amsterdam, p. 137–145.Google Scholar
  3. Eisen, V. (1964), Br. J. Pharmacol., 22. 87–103.Google Scholar
  4. Eisen, V., and Vogt, W. (1970), in Handbook Exp. Pharmacol. 25 (E.G. Erdos, ed.), Springer, Berlin, p. 82–130.Google Scholar
  5. Erdos, E.G., McMennamin, M.A., and Wohler, J.R. (1962), Life Sci., 111 765–769.CrossRefGoogle Scholar
  6. Erdos, E.G., and Sloane, E.M. (1962), Biochem. Pharmacol., 11 585–592.PubMedCrossRefGoogle Scholar
  7. Erspamer, G.F., Negri, L., and Piccinelli, D. (1973), Arch. Pharmacol., 279 61–74.CrossRefGoogle Scholar
  8. Ferreira, S.H., and Vane, J.R. (1967), Br. J. Pharmacol., 29 367–377.Google Scholar
  9. Giroux, E.L., Lefort, J., and Vargaftig, B.B. (1976), submitted for publication.Google Scholar
  10. Gros, P., and Labouesse, B. (1960), Bull. Soc. Chim. Biol., 42 559–568.PubMedGoogle Scholar
  11. Guimaraes, J.A., Lu, R.C., Webster, M.E., and Pierce, J.V. (1974), Fed. Proc, abstract 2431.Google Scholar
  12. Habal, F.M., Movat, H.Z., and Burrowes, C.E. (1974), Biochem. Pharmacol., 23 2291–2303.PubMedCrossRefGoogle Scholar
  13. Hamberg, M., (1975), Proc. Nat. Acad. Sci., in press.Google Scholar
  14. Hamberg, M., and Samuelsson, B. (1974), Proc. Nat. Acad. Sci., 71 3400–3404.PubMedCrossRefGoogle Scholar
  15. Hamberg, M., Svensson, J., Wakabayashi, T., and Samuelsson, B. (1974), Proc. Nat. Acad. Sci., 71 345–349.PubMedCrossRefGoogle Scholar
  16. Jahrreiss, R., and Habermann, E. (1971), Arch. Pharmacol., 269 85–100.Google Scholar
  17. Kassell, B. (1970), in Methods in Enzymology 19 (G.E. Perlmann and L. Lorand, eds.), Acad. Press, New York, p. 844–852.Google Scholar
  18. Labouesse, B., and Gros, P. (1960), Bull. Soc. Chim. Biol., 42 543–558.PubMedGoogle Scholar
  19. Lewis, G.P. (1960), Physiol. Rev. 40 647–676.PubMedGoogle Scholar
  20. Mitchell, W.M. (1968), Science, 162 374–375.PubMedCrossRefGoogle Scholar
  21. Mitchell, U.M., and Harrington, W.F. (1968), J. Biol. Chem., 243 4683–4692.PubMedGoogle Scholar
  22. Nakahara, M. (1974), Biochem. Pharmacol., 23 3009–3015.PubMedCrossRefGoogle Scholar
  23. Ogle, J.D., and Tytell, A.A. (1953), Arch. Biochem. Biophys., 42 327–336.CrossRefGoogle Scholar
  24. Piper, P.J., and Vane, J.R. (1969), Nature, 223 20–35.CrossRefGoogle Scholar
  25. Porter, W.H., Cunningham, L.W., and Mitchell, W.M. (1971), J. Biol. Chem., 246 7675–7682.PubMedGoogle Scholar
  26. Prado, J.L. (1970), in Handbook Exp. Pharmacol. 25 (E.G. Erdos, ed.), Springer, Berlin, p. 156–192.Google Scholar
  27. Prado, J.L., Monier, R., Prado, E.S., and Fromageot, C. (1956), Biochim. Biophys. Acta, 22 87–95.PubMedCrossRefGoogle Scholar
  28. Prado, J.L., and Prado, E.S. (1962), An. Acad. Bras. Cien., 34 51–55.Google Scholar
  29. Rothschild, A.M. (1967), in Int. Symp. Vaso-Active Polypeptides: Bradykinin and Related Kinins (M. Rocha e Silva and H.A. Rothschild, eds.), Edart, Sao Paulo, p. 197–203.Google Scholar
  30. Schoenmakers, J.G.G., Matze, R., Haanen, C., and Zilliken, F. (1965), Biochim. Biophys. Acta, 101 166–176.PubMedGoogle Scholar
  31. Trautschold, I. and Werle, E. (1961), Z. Physiol. Chem. 325 48–59.CrossRefGoogle Scholar
  32. Vane, J.R. (1964), Br. J. Pharmacol., 23 360–373.Google Scholar
  33. Vane, J.R. (1971), Nature New Biol., 231 232–235.PubMedGoogle Scholar
  34. Vargaftig, B.B., Bhargava, N., de Vos, C.J., and Bonta, I.L. (1970), Advan. Exp. Med. Biol., 8 477–485.Google Scholar
  35. Vargaftig, B.B., and Chignard, M. (1975), Agents and Actions, 5 137–144.PubMedCrossRefGoogle Scholar
  36. Vargaftig, B.B., and Dao, N. (1971), Pharmacology, 6 99–108.PubMedCrossRefGoogle Scholar
  37. Vargaftig, B.B., Tranier, Y., and Chignard, M. (1974), Prostaglandins, 8 133–156.PubMedCrossRefGoogle Scholar
  38. Vargaftig, B.B., and Zirinis, P. (1973), Nature New Biol., 244 114–116.PubMedGoogle Scholar
  39. Vogt, W. (1966), in Hypotensive Peptides (E.G. Erdos, N. Back and F. Sicuteri, eds.), Springer, Berlin, p. 185–192.CrossRefGoogle Scholar
  40. Willis, A.L. (1974), Prostaglandins, 5 1–25.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • B. B. Vargaftig
    • 1
  • E. L. Giroux
    • 1
  1. 1.Centre de Recherche Merrell InternationalStrasbourgFrance

Personalised recommendations