Referenced in: none

Automatically associated channels: TRP , TRPC , TRPC1

Title: Ligation of complement receptor 1 increases erythrocyte membrane deformability.

Authors: Aleksandra M Glodek, Rossen Mirchev, David E Golan, Joseph A Khoory, Jennie M Burns, Sergey S Shevkoplyas, Anne Nicholson-Weller, Ionita C Ghiran

Journal, date & volume: Blood, 2010 Dec 23 , 116, 6063-71

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/20861458

Abstract
Microbes as well as immune complexes and other continuously generated inflammatory particles are efficiently removed from the human circulation by red blood cells (RBCs) through a process called immune-adherence clearance. During this process, RBCs use complement receptor 1 (CR1, CD35) to bind circulating complement-opsonized particles and transfer them to resident macrophages in the liver and spleen for removal. We here show that ligation of RBC CR1 by antibody and complement-opsonized particles induces a transient Ca(++) influx that is proportional to the RBC CR1 levels and is inhibited by T1E3 pAb, a specific inhibitor of TRPC1 channels. The CR1-elicited RBC Ca(++) influx is accompanied by an increase in RBC membrane deformability that positively correlates with the number of preexisting CR1 molecules on RBC membranes. Biochemically, ligation of RBC CR1 causes a significant increase in phosphorylation levels of β-spectrin that is inhibited by preincubation of RBCs with DMAT, a specific casein kinase II inhibitor. We hypothesize that the CR1-dependent increase in membrane deformability could be relevant for facilitating the transfer of CR1-bound particles from the RBCs to the hepatic and splenic phagocytes.