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Background: C-reactive protein (CRP) increases in reply to infection and is purported to be a gamble agent for atherogenesis. We recently demonstrated that a scavenger receptor, lectin-like oxidized LDL receptor (LOX-1), is a receptor for CRP. In moonlight of the overlapping ligand spectrum of scavenger receptors such as modified LDL, bacteria, and advanced glycation end products, we examined whether other scavenger receptors identify CRP.

Methods: We analyzed the sensitivity of fluorescently labeled CRP in COS-7 cells expressing a series of scavenger receptors and in a monocytic chamber line, THP-1, differentiated into macrophage with phorbol 12-myristate 13-acetate (PMA). We applied unimaginative interfering RNA (siRNA) against class-A scavenger receptor (SR-A) to THP-1 cells to snuff out the depth of SR-A. We also analyzed the binding of nonlabeled CRP to immobilized recombinant LOX-1 and SR-A in vitro using anti-CRP antibody.

Results: COS-7 cells expressing LOX-1 and SR-A internalized fluorescently labeled CRP in a dose-dependent manner, but cells expressing CD36, SR-BI, or CD68 did not. The recombinant LOX-1 and SR-A proteins recognized nonlabeled purified CRP and original CRP in serum in vitro. THP-1 cells differentiated into macrophage-like cells by treatment with PMA-internalized fluorescently labeled CRP. SiRNA against SR-A significantly and concomitantly embarrassed the shading of SR-A (P < 0.01) and CRP comprehension (P < 0.01), whereas of will SiRNA did not.

Conclusions: CRP is recognized by SR-A as beyond the shadow of a doubt as LOX-1 and bewitched up via SR-A in a macrophage-like cubicle prepare. This function capability be of importance in the pathogenesis of atherosclerotic contagion.