Skip to main content
NCBI home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1982 May;69(5):1199–1202. doi: 10.1172/JCI110557

Purified human plasma kallikrein aggregates human blood neutrophils.

M Schapira, E Despland, C F Scott, L A Boxer, R W Colman
PMCID: PMC370186  PMID: 6917855

Abstract

Exposure of human blood polymorphonuclear leukocytes (PMN) to purified active plasma kallikrein resulted in PMN aggregation when kallikrein was present at concentrations ranging from 0.4 to 0.6 U/ml (0.18-0.27 microM). Kallikrein-induced PMN aggregation was not mediated through C5-derived peptides, because identical responses were observed whether or not kallikrein had been preincubated with an antibody to C5. Moreover, kallikrein was specific for aggregating PMN, because no aggregation was observed with Factor XII active fragments (23 nM), Factor XIa (0.6 U/ml or 15nM), thrombin (1.6 microM), plasmin (2 microM), porcine pancreatic elastase (2 microM), bovine pancreatic chymotrypsin (2 microM), or bradykinin (1 microM). Bovine pancreatic trypsin (2 microM) aggregated PMN, but to a lesser extent than kallikrein (0.18 microM). Kallikrein was a potent aggregant agent for PMN because similar responses were observed with kallikrein (0.5 U/ml or 0.23 microM) and an optimal dose (0.2 microM) of N-formyl-methionyl-leucyl-phenylalanine. In addition, PMN incubation with kallikrein resulted in stimulation of their oxidative metabolism as assessed by an increased oxygen uptake. Neutropenia and leukostasis observed in diseases associated with activation of the contact phase system may be the result of PMN aggregation by plasma kallikrein.

Full text

PDF
1199

Selected References

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

  1. Becker C. G., Dubin T., Glenn F. Induction of acute cholecystitis by activation of factor XII. J Exp Med. 1980 Jan 1;151(1):81–90. doi: 10.1084/jem.151.1.81. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Craddock P. R., Hammerschmidt D., White J. G., Dalmosso A. P., Jacob H. S. Complement (C5-a)-induced granulocyte aggregation in vitro. A possible mechanism of complement-mediated leukostasis and leukopenia. J Clin Invest. 1977 Jul;60(1):260–264. doi: 10.1172/JCI108763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Deutsch D. G., Mertz E. T. Plasminogen: purification from human plasma by affinity chromatography. Science. 1970 Dec 4;170(3962):1095–1096. doi: 10.1126/science.170.3962.1095. [DOI] [PubMed] [Google Scholar]
  4. Goetzl E. J., Austen K. F. Stimulation of human neutrophil leukocyte aerobic glucose metabolism by purified chemotactic factors. J Clin Invest. 1974 Feb;53(2):591–599. doi: 10.1172/JCI107594. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Goldstein I. M., Perez H. D. Biologically active peptides derived from the fifth component of complement. Prog Hemost Thromb. 1980;5:41–79. [PubMed] [Google Scholar]
  6. Hammerschmidt D. E., Bowers T. K., Lammi-Keefe C. J., Jacob H. S., Craddock P. R. Granulocyte aggregometry: a sensitive technique for the detection of C5a and complement activation. Blood. 1980 Jun;55(6):898–902. [PubMed] [Google Scholar]
  7. Kaplan A. P. Initiation of the intrinsic coagulation and fibrinolytic pathways of man: the role of surfaces, hageman factor, prekallikrein, high molecular weight kininogen, and factor XI. Prog Hemost Thromb. 1978;4:127–175. [PubMed] [Google Scholar]
  8. Kaplan A. P., Kay A. B., Austen K. F. A prealbumin activator of prekallikrein. 3. Appearance of chemotactic activity for human neutrophils by the conversion of human prekallikrein to kallikrein. J Exp Med. 1972 Jan;135(1):81–97. doi: 10.1084/jem.135.1.81. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Murdoch J. M., Smith C. C. Infection. Clin Haematol. 1972 Oct;1(3):619–644. [PubMed] [Google Scholar]
  10. Oseas R. S., Boxer L. A., Butterick C., Baehner R. L. Differences in polymorphonuclear leukocyte aggregating responses among several species in response to chemotactic stimulation. J Lab Clin Med. 1980 Aug;96(2):213–221. [PubMed] [Google Scholar]
  11. Schapira M., Scott C. F., Colman R. W. Protection of human plasma kallikrein from inactivation by C1 inhibitor and other protease inhibitors. The role of high molecular weight kininogen. Biochemistry. 1981 May 12;20(10):2738–2743. doi: 10.1021/bi00513a006. [DOI] [PubMed] [Google Scholar]
  12. Scott C. F., Liu C. Y., Colman R. W. Human plasma prekallikrein: a rapid high-yield method for purification. Eur J Biochem. 1979 Oct;100(1):77–83. doi: 10.1111/j.1432-1033.1979.tb02035.x. [DOI] [PubMed] [Google Scholar]
  13. Scott C. F., Schapira M., James H. L., Cohen A. B., Colman R. W. Inactivation of factor XIa by plasma protease inhibitors: predominant role of alpha 1-protease inhibitor and protective effect of high molecular weight kininogen. J Clin Invest. 1982 Apr;69(4):844–852. doi: 10.1172/JCI110524. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Weiss H. J. Platelet physiology and abnormalities of platelet function (first of two parts). N Engl J Med. 1975 Sep 11;293(11):531–541. doi: 10.1056/NEJM197509112931105. [DOI] [PubMed] [Google Scholar]
  15. Wiggins R. C., Giclas P. C., Henson P. M. Chemotactic activity generated from the fifth component of complement by plasma kallikrein of the rabbit. J Exp Med. 1981 Jun 1;153(6):1391–1404. doi: 10.1084/jem.153.6.1391. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES