The Journal of Experimental Medicine
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Published 3 December 2001. doi:10.1084/jem.194.11.1609
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© Rockefeller University Press, 0022-1007/2001/12/1609/ $5.00
The Journal of Experimental Medicine, Volume 194, Number 11, December 3, 2001 1609-1616

Original Article

Complement 1 Inhibitor Is a Regulator of the Alternative Complement Pathway

Haixiang Jiang, Eric Wagner, Huamei Zhang and Michael M. Frank

Department of Pediatrics, Duke University Medical Center, Durham, NC 27710

Address correspondence to Dr. Michael M. Frank, Department of Pediatrics, Box 3352, Duke University Medical Center, Durham, NC 27710. Phone: 919-681-4080; Fax: 919-681-2714; E-mail: frank007{at}mc.duke.edu

We studied complement 1 inhibitor (C1-INH) as an inhibitor of the alternative complement pathway. C1-INH prevented lysis, induced by the alternative complement pathway, of paroxysmal nocturnal hemoglobinuria (PNH) erythrocytes in human serum. It inhibited the binding of both factors B and C3 to PNH and rabbit erythrocytes and blocked the ability of factor B to restore alternative-pathway function in factor B–depleted serum. C1-INH did not bind to factors B or D but did bind to immobilized C3b and cobra venom factor (CVF), a C3b analogue. C1-INH prevented factor B from binding to CVF-coated beads and dissociated bound factor B from such beads. Factor B and C1-INH showed cross competition in binding to CVF-coated beads. Factor D cleaved factor B into Bb and Ba in the presence of C3b. Cleavage was markedly inhibited when C3b was preincubated with C1-INH. C1-INH inhibited the formation of CVFBb and decreased the C3 cleavage. Removal of C1-INH from serum, in the presence of Mg-EGTA with an anti–C1-INH immunoabsorbant, markedly increased alternative-pathway lysis. C1-INH interacts with C3b to inhibit binding of factor B to C3b. At physiologic concentrations, it is a downregulator of the alternative pathway convertase.

Key Words: complement • serpins • hematological diseases • regulation • immunity


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