HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Daha, M. R. Articles by Austen, K. F. Search for Related Content PubMed Articles by Daha, M. R. Articles by Austen, K. F.

C3 Nephritic Factor (C3NeF): Stabilization of Fluid Phase and Cell-Bound Alternative Pathway Convertase¹

From the Departments of Medicine, Harvard Medical School and Robert B. Brigham Hospital, Boston, Massachusetts 02120

Abstract

C3 nephritic factor (C3NeF) defined by the capacity of nephritic serum and its fractions to initiate loss of the B antigen of C3 in normal serum was purified from the serum of three different donors and shown to function by stabilization of membrane-bound and fluid phase alternative pathway C3 convertase. C3NeF converts cell-bound C3 sites in a dose-related manner to C3(NeF) sites, which exhibit and approximate 10-fold increase in half-life. The linear relationship between the C3NeF input and the residual hemolytic sites on EAC43B present after incubation for 20 min at 30°C, during which labile C3 sites, have decayed, indicates that the number of residual C3 sites is directly related to the dose of C3NeF. The capacity of C3NeF to stabilize the C3 convertase in a temperature- and dose-dependent manner, which is independent of binding or consumption of C3NeF, in a fluid phase reaction mixture of ¹²⁵I-B, ¹³¹I-C3, and permits isolation of a 10S complex containing radiolabeled C3 and B and exhibiting C3 convertase activity on an exogenous C3 source. Thus, the stabilizing effect of C3NeF is not limited to membrane-bound C3 but is also sufficient to permit recovery of a fluid phase C3 convertase formed during the interaction of C3, B, and .

Footnotes

¹ This work was supported by Grants AI-07722 and AM-05577 from the National Institutes of Health.

² Postdoctoral Fellow of the Netherlands Organization for the Advancement of Pure Research (ZWO).

³ Postdoctoral Fellow of the Helen Hay Whitney Foundation.

This article has been cited by other articles:

				S. MERI Loss of Self-Control in the Complement System and Innate Autoreactivity Ann. N.Y. Acad. Sci., August 1, 2007; 1109(1): 93 - 105. [Abstract] [Full Text] [PDF]

				M. C. Pickering, J. Warren, K. L. Rose, F. Carlucci, Y. Wang, M. J. Walport, H. T. Cook, and M. Botto Prevention of C5 activation ameliorates spontaneous and experimental glomerulonephritis in factor H-deficient mice PNAS, June 20, 2006; 103(25): 9649 - 9654. [Abstract] [Full Text] [PDF]

				M. Kirschfink and T. E. Mollnes Modern Complement Analysis Clin. Vaccine Immunol., November 1, 2003; 10(6): 982 - 989. [Full Text] [PDF]

				M. C. Pickering and M. J. Walport Links between complement abnormalities and systemic lupus erythematosus Rheumatology, February 1, 2000; 39(2): 133 - 141. [Full Text] [PDF]

				T. S. Jokiranta, A. Solomon, M. K. Pangburn, P. F. Zipfel, and S. Meri Nephritogenic {lambda} Light Chain Dimer: A Unique Human Miniautoantibody Against Complement Factor H J. Immunol., October 15, 1999; 163(8): 4590 - 4596. [Abstract] [Full Text] [PDF]

				B. Rosen, K. Cook, J Yaglom, D. Groves, J. Volanakis, D Damm, T White, and B. Spiegelman Adipsin and complement factor D activity: an immune-related defect in obesity Science, June 23, 1989; 244(4911): 1483 - 1487. [Abstract] [PDF]