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. 1974 Aug 1;140(2):426–436. doi: 10.1084/jem.140.2.426

PROPERDIN FACTOR D

II. ACTIVATION TO D BY PROPERDIN

Douglas T Fearon 1, K Frank Austen 1, Shaun Ruddy 1
PMCID: PMC2139584  PMID: 4211020

Abstract

The protein in the properdin pathway responsible for conversion of precursor factor D to D has been isolated and found to be identical with properdin. Sequential ion exchange and gel filtration chromatography demonstrated identity between properdin protein, measured by radial immunodiffusion, and the capacity to activate D to D, assessed by formation of the intermediate, EAC43B(D). Properdin, purified in this manner, was homogeneous on acid polyacrylamide disc gel electrophoretic analysis, with the band of protein corresponding to the position of eluates in the replicate gel capable of activating highly purified D. Demonstration of the homogeneity of purified D by alkaline disc gel electrophoresis, coupled with the linear stoichiometric hemolytic titrations of each factor, indicates that direct interaction between properdin and D generates D. Thus, activation of D by properdin represents a mechanism in the properdin pathway by which D becomes available for formation of the C3b-dependent C3 convertase.

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Selected References

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

  1. Alper C. A., Goodkofsky I., Lepow I. H. The relationship of glycine-rich -glycoprotein to factor B in the properdin system and to the cobra factor-binding protein of huan serum. J Exp Med. 1973 Feb 1;137(2):424–437. doi: 10.1084/jem.137.2.424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alpert E., Monroe M., Schur P. H. A method for increasing the sensitivity of radial-immunodiffusion assay. Lancet. 1970 May 23;1(7656):1120–1120. doi: 10.1016/s0140-6736(70)92796-0. [DOI] [PubMed] [Google Scholar]
  3. Cooper N. R. Formation and function of a complex of the C3 proactivator with a protein from cobra venom. J Exp Med. 1973 Feb 1;137(2):451–460. doi: 10.1084/jem.137.2.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ensky J., Hinz C. F., Jr, Todd E. W., Wedgwood R. J., Boyer J. T., Lepow I. H. Properties of highly purified human properdin. J Immunol. 1968 Jan;100(1):142–158. [PubMed] [Google Scholar]
  5. Fearon D. T., Austen K. F., Ruddy S. Formation of a hemolytically active cellular intermediate by the interaction between properdin factors B and D and the activated third component of complement. J Exp Med. 1973 Dec 1;138(6):1305–1313. doi: 10.1084/jem.138.6.1305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fearon D. T., Austen K. F., Ruddy S. Properdin factor D: characterization of its active site and isolation of the precursor form. J Exp Med. 1974 Feb 1;139(2):355–366. doi: 10.1084/jem.139.2.355. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hunsicker L. G., Ruddy S., Austen K. F. Alternate complement pathway: factors involved in cobra venom factor (CoVF) activation of the third component of complement (C3). J Immunol. 1973 Jan;110(1):128–138. [PubMed] [Google Scholar]
  8. Hunsicker L. G., Ruddy S., Carpenter C. B., Schur P. H., Merrill J. P., Müller-Eberhard H. J., Austen K. F. Metabolism of third complement component (C3) in nephritis. Involvement of the classic and alternate (properdin) pathways for complement activation. N Engl J Med. 1972 Oct 26;287(17):835–840. doi: 10.1056/NEJM197210262871701. [DOI] [PubMed] [Google Scholar]
  9. Kaplan A. P., Austen K. F. The fibrinolytic pathway of human plasma. Isolation and characterization of the plasminogen proactivator. J Exp Med. 1972 Dec 1;136(6):1378–1393. doi: 10.1084/jem.136.6.1378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Minta J. O., Goodkofsky I., Lepow I. H. Solid phase radioimmunoassay of properdin. Immunochemistry. 1973 May;10(5):341–350. doi: 10.1016/0019-2791(73)90082-7. [DOI] [PubMed] [Google Scholar]
  12. Müller-Eberhard H. J., Götze O. C3 proactivator convertase and its mode of action. J Exp Med. 1972 Apr 1;135(4):1003–1008. doi: 10.1084/jem.135.4.1003. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Müller-Eberhard H. J., Polley M. J., Calcott M. A. Formation and functional significance of a molecular complex derived from the second and the fourth component of human complement. J Exp Med. 1967 Feb 1;125(2):359–380. doi: 10.1084/jem.125.2.359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. NILSSON U. R., MUELLER-EBERHARD H. J. ISOLATION OF BETA IF-GLOBULIN FROM HUMAN SERUM AND ITS CHARACTERIZATION AS THE FIFTH COMPONENT OF COMPLEMENT. J Exp Med. 1965 Aug 1;122:277–298. doi: 10.1084/jem.122.2.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. PILLEMER L., BLUM L., LEPOW I. H., ROSS O. A., TODD E. W., WARDLAW A. C. The properdin system and immunity. I. Demonstration and isolation of a new serum protein, properdin, and its role in immune phenomena. Science. 1954 Aug 20;120(3112):279–285. doi: 10.1126/science.120.3112.279. [DOI] [PubMed] [Google Scholar]
  16. Ruddy S., Austen K. F. C3 inactivator of man. I. Hemolytic measurement by the inactivation of cell-bound C3. J Immunol. 1969 Mar;102(3):533–543. [PubMed] [Google Scholar]
  17. TODD E. W., PILLEMER L., LEPOW I. H. The properdin system and immunity. IX. Studies on the purification of human properdin. J Immunol. 1959 Oct;83:418–427. [PubMed] [Google Scholar]
  18. Tenenhouse H. S., Deutsch H. F. Some physical-chemical properties of chicken gamma-globulins and their pepsin and papain digestion products. Immunochemistry. 1966 Jan;3(1):11–20. doi: 10.1016/0019-2791(66)90277-1. [DOI] [PubMed] [Google Scholar]

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