Complement blockade with a C1 esterase inhibitor in paroxysmal nocturnal hemoglobinuria

Amy E. DeZern, Marc Uknis, Xuan Yuan, Galina L. Mukhina, Juan Varela, Jo Anne Saye, Jeffrey Pu, Robert A. Brodsky

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Paroxysmal nocturnal hemoglobinuria (PNH) is a rare, clonal, hematopoietic stem cell disorder that manifests with a complement-mediated hemolytic anemia, bone marrow failure, and a propensity for thrombosis. These patients experience both intra- and extravascular hemolysis in the context of underlying complement activation. Currently eculizumab effectively blocks the intravascular hemolysis PNH. There remains an unmet clinical need for a complement inhibitor with activity early in the complement cascade to block complement at the classical and alternative pathways. C1 esterase inhibitor (C1INH) is an endogenous human plasma protein that has broad inhibitory activity in the complement pathway through inhibition of the classical pathway by binding C1r and C1s and inhibits the mannose-binding lectin-associated serine proteases in the lectin pathway. In this study, we show that commercially available plasma derived C1INH prevents lysis induced by the alternative complement pathway of PNH erythrocytes in human serum. Importantly, C1INH was able to block the accumulation of C3 degradation products on CD55 deficient erythrocytes from PNH patient on eculizumab therapy. This could suggest a role for inhibition of earlier phases of the complement cascade than that currently inhibited by eculizumab for incomplete or nonresponders to that therapy.

Original languageEnglish (US)
Pages (from-to)857-861.e1
JournalExperimental Hematology
Volume42
Issue number10
DOIs
StatePublished - Oct 1 2014

ASJC Scopus subject areas

  • Molecular Biology
  • Hematology
  • Genetics
  • Cell Biology
  • Cancer Research

Fingerprint

Dive into the research topics of 'Complement blockade with a C1 esterase inhibitor in paroxysmal nocturnal hemoglobinuria'. Together they form a unique fingerprint.

Cite this