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Identification of a complement receptor 1 peptide for inhibition of immune hemolysis.

Abstract：

:Complement sensitization of red blood cells (RBCs) can cause life-threatening hemolytic anemias. We have previously shown that complement receptor 1 (CR1) derivatives specifically the N-terminal region with decay accelerating activity (DAA) for inactivation of a key enzyme in the complement cascade can reduce complement-mediated RBC destruction in vitro and in an in vivo mouse model of hemolytic transfusion reaction. In the present study, we have modeled the N-terminal CR1 molecule based on the X-ray crystal structure of decay accelerating factor and the NMR structure of a homologous CR1 domain. Based on the homology model, we identified a 34-mer peptide encompassing the putative DAA which in vitro reduced hemolysis, C3a release and surface C3 deposition. More importantly, this peptide at 0.6 mM was effective in prolonging survival of transfused incompatible RBCs in vivo. Our results indicate that CR1-based structure-function studies may provide insights for developing structure-derived transfusion therapeutics in the future.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yu J,Heck S,Debnath A,Yazdanbakhsh K

doi

10.1016/j.bbrc.2006.12.020

subject

Has Abstract

pub_date

2007-02-09 00:00:00

pages

363-368

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)02675-1

journal_volume

353

pub_type

杂志文章

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