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Citations to this article

Neoantigen of the polymerized ninth component of complement. Characterization of a monoclonal antibody and immunohistochemical localization in renal disease.
R J Falk, … , H Gewurz, A F Michael
R J Falk, … , H Gewurz, A F Michael
Published August 1, 1983
Citation Information: J Clin Invest. 1983;72(2):560-573. https://doi.org/10.1172/JCI111004.
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Research Article Article has an altmetric score of 3

Neoantigen of the polymerized ninth component of complement. Characterization of a monoclonal antibody and immunohistochemical localization in renal disease.

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Abstract

A monoclonal antibody to a neoantigen of the C9 portion of the membrane attack complex (MAC) of human complement has been developed and characterized. The distribution of this neoantigen was assessed by indirect immunofluorescence microscopy in nephritic and nonnephritic renal diseases. The antibody (Poly C9-MA) reacted on enzyme-linked immunosorbent assay (ELISA) with a determinant in complement-activated serum that was undetectable in normal human serum (NHS). Zymosan particles incubated in NHS had positive immunofluorescent staining with Poly C9-MA; however, binding of Poly C9-MA was not observed with zymosan particles incubated in sera deficient in individual complement components C3, C5, C6, C7, C8, or C9. Reconstitution of C9-deficient sera with purified C9 restored the fluorescence with Poly C9-MA. Poly C9-MA reacted positively by ELISA in a dose-dependent manner with purified MC5b-9 solubilized from membranes of antibody-coated sheep erythrocytes treated with NHS but not with intermediate complement complexes. Poly C9-MA also reacted in a dose-dependent manner on ELISA and in a radioimmunoassay with polymerized C9 (37 degrees C, 64 h) (poly C9) but not with monomeric C9. Increasing amounts of either unlabeled poly C9 or purified MC5b-9 inhibited the 125I-poly C9 RIA in an identical manner. These studies demonstrate that Poly C9-MA recognizes a neoantigen of C9 common to both the MAC and to poly C9. By immunofluorescence, Poly C9-MA reacted minimally with normal kidney tissue in juxtaglomerular loci, the mesangial stalk, and vessel walls. Poly C9-MA stained kidney tissue from patients with glomerulonephritis in a pattern similar to that seen with polyclonal anti-human C3. In tissue from patients with nonnephritic renal disease--diabetes, hypertension, and obstructive uropathy--Poly C9-MA was strongly reactive in the mesangial stalk and juxtaglomerular regions, tubular basement membranes, and vascular walls. Poly C9-MA binding was especially prominent in areas of advanced tissue injury. Poly C9-MA frequently stained loci where C3 was either minimally present or absent. These studies provide strong evidence for complement activation not only in nephritic but also in nonnephritic renal diseases.

Authors

R J Falk, A P Dalmasso, Y Kim, C H Tsai, J I Scheinman, H Gewurz, A F Michael

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Total citations by year

Year: 2024 2021 2019 2018 2017 2016 2015 2014 2012 2011 2010 2008 2007 2006 2005 2004 2003 2002 2000 1999 1998 1997 1996 1995 1994 1993 1992 1991 1990 1989 1988 1987 1986 1985 1984 1981 1971 Total
Citations: 1 1 27 2 1 1 4 1 3 4 2 1 1 1 2 2 2 2 3 1 3 3 7 7 3 4 10 9 5 16 8 19 15 12 8 1 1 193
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Citations to this article in year 2015 (4)

Title and authors Publication Year
Urinary candidate biomarker discovery in a rat unilateral ureteral obstruction model
Y Yuan, F Zhang, J Wu, C Shao, Y Gao
Scientific Reports 2015
Role of Complement and Complement Regulatory Proteins in the Complications of Diabetes
P Ghosh, R Sahoo, A Vaidya, M Chorev, JA Halperin
Endocrine reviews 2015
Pediatric Nephrology
ED Avner, WE Harmon, P Niaudet, N Yoshikawa, F Emma, S Goldstein
Pediatric Nephrology 2015
Inflammatory Pathways in Diabetes
M Pugia
2015

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