JCI - Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome

Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome

Tamara Manuelian, Jens Hellwage, Seppo Meri, Jessica Caprioli, Marina Noris, Stefan Heinen, Mihaly Jozsi, Hartmut P.H. Neumann, Giuseppe Remuzzi, Peter F. Zipfel

Published in Volume 111, Issue 8

J Clin Invest. 2003; 111(8):1181–1190 doi:10.1172/JCI16651

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Figure 7

Binding of recombinant mutant, mutant factor H (E1172Stop), and wild-type proteins to endothelial cells. (a) Dose-dependent binding of recombinant wild-type factor H (FH 8-20). HUVECs incubated in serum-free medium were incubated with the indicated amounts of purified recombinant wild-type factor H 8-20, and binding was assayed by FACS analysis. (b) Comparison of recombinant mutant R1210C (i.e., FH 8-20/R1210C), or R1215G (i.e., FH 8-20/R1215G), or wild-type factor H (FH 8-20). HUVECs cultivated in serum-free medium were incubated with the indicated proteins, and binding was assayed by FACS analysis. (c) Binding of purified factor H protein with the E1172Stop mutation isolated from serum of patient R043 and of purified wild-type factor H to HUVECs. HUVECs were treated with either 5 μg of mutant factor H protein purified from plasma of patient R043 or with 5 μg purified intact wild-type factor H, and binding was assayed by FACS.