Please use this identifier to cite or link to this item: https://doi.org/10.1007/s13238-010-0020-3
Title: The class A macrophage scavenger receptor type I (SR-AI) recognizes complement iC3b and mediates NF-κB activation
Authors: Goh, J.W.K. 
Tan, Y.S.
Dodds, A.W.
Reid, K.B.M.
Lu, J. 
Keywords: 293T cells
complement
iC3b
macrophage
signalling
SR-AI
Issue Date: Feb-2010
Source: Goh, J.W.K., Tan, Y.S., Dodds, A.W., Reid, K.B.M., Lu, J. (2010-02). The class A macrophage scavenger receptor type I (SR-AI) recognizes complement iC3b and mediates NF-κB activation. Protein and Cell 1 (2) : 174-187. ScholarBank@NUS Repository. https://doi.org/10.1007/s13238-010-0020-3
Abstract: The macrophage scavenger receptor SR-AI binds to host tissue debris to perform clearance and it binds to bacteria for phagocytosis. In addition, SR-AI modulates macrophage activation through cell signaling. However, investigation of SR-AI signaling on macrophages is complicated due to its promiscuous ligand specificity that overlaps with other macrophage receptors. Therefore, we expressed SR-AI on HEK 293T cells to investigate its ligand binding and signaling. On 293Tcells, SR-AI could respond to E. coli DH5α, leading to NF-κB activation and IL-8 production. However, this requires E. coli DH5α to be sensitized by fresh serum that is treated with heat-inactivation or complement C3 depletion. Anti-C3 antibody inhibits the binding of SR-AI to serum-sensitized DH5α and blocks DH5α stimulation of SR-AI signaling. Further analysis showed that SR-AI can directly bind to purified iC3b but not C3 or C3b. By mutagenesis, The SRCR domain of SR-AI was found to be essential in SR-AI binding to serum-sensitized DH5α. These results revealed a novel property of SR-AI as a complement receptor for iC3b-opsonized bacteria that can elicit cell signaling. © 2010 Higher Education Press and Springer-Verlag Berlin Heidelberg.
Source Title: Protein and Cell
URI: http://scholarbank.nus.edu.sg/handle/10635/53215
ISSN: 1674800X
DOI: 10.1007/s13238-010-0020-3
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