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Science 9 June 1989:
Vol. 244. no. 4909, pp. 1163 - 1165
DOI: 10.1126/science.2786251

Articles

Science, Vol 244, Issue 4909, 1163-1165
Copyright © 1989 by American Association for the Advancement of Science


articles

Autoimmune target in Heymann nephritis is a glycoprotein with homology to the LDL receptor

R Raychowdhury, JL Niles, RT McCluskey, and JA Smith

Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.

The pathogenesis of Heymann nephritis, a rat model of human membranous glomerulonephritis, depends on the interaction of autoantibodies with a renal glycoprotein (GP330) on glomerular podocytes. Partial complementary DNAs coding for GP330 were isolated and sequenced. The deduced amino acid sequence from 4.3 kilobases of complementary DNA contains the sequences identical to two peptides derived from the isolated glycoprotein. The deduced amino acid sequence of this protein contains regions with homology to the human low density lipoprotein (LDL) receptor, an indication that GP330 and the LDL receptor may be members of the same gene family. Autoantibodies from the kidneys of rats with Heymann nephritis reacted with a nonglycosylated segment of GP330 that contains cysteine-rich 40-amino acid repeats, which are also features of the LDL receptor. GP330 is also similar in some regions to the mouse epidermal growth factor precursor.


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