Scavenger cells with Gram-positive bacterial lipoteichoic acid infiltrate around the damaged interlobular bile ducts of primary biliary cirrhosis

CLA-1 and its splicing variant CLA-2 mediate bacterial adhesion and cytosolic bacterial invasion in mammalian cells

“…In addition to live bacteria, we also showed that CLA-1 and CLA-2 bind dead bacteria, pointing to a potential role of these receptors in the clearance of damaged bacteria. Supporting this possibility is the earlier observation of extensive colocalization of LTA with scavenger cells in the liver of patients with primary biliary cirrhosis (18). Competition experiments where both LPS and LTA nearly completely blocked Alexa Fluor 488 E. coli K12 uptake indicate that LPS and LTA may play important roles as HDL-receptor recognition motifs.…”

Altered monocyte responses to defined TLR ligands in patients with primary biliary cirrhosis

“…Interestingly, a previous study demonstrated that LTA-containing mononuclear cells were frequently detected in the portal tracts of patients with PBC, particularly surrounding the damaged interlobular bile ducts. 23 Finally, the effects of polyIC, a synthetic analog of double-stranded RNA associated with viral infection, 24 were also examined on PBC and control monocytes. We discovered that polyIC significantly elevated the production of IL-8 and TNF-␣ in patients with PBC, albeit the increases were only 12% and 22% over controls, respectively.…”

Targeting of Scavenger Receptor Class B Type I by Synthetic Amphipathic α-Helical-containing Peptides Blocks Lipopolysaccharide (LPS) Uptake and LPS-induced Pro-inflammatory Cytokine Responses in THP-1 Monocyte Cells

“…In contrast to L-37pA, no effect was observed for the non-helical peptides L1D-37pA, L2D-37pA, or L3D-37pA. Importantly, the peptides made with a mixture of L-and D-amino acids had lower lipid affinity, as assessed by monitoring their ability to act as detergents in the solubilization of dimyristoylphosphatidylcholine vesicles in the order L-37pA Ͼ L1D-37pA Ͼ L2D37pA Ͼ L3D-37pA (56). However, a similar ability to stimulate cholesterol efflux was demonstrated in HeLa cells with these peptides (56).…”

“…Importantly, the peptides made with a mixture of L-and D-amino acids had lower lipid affinity, as assessed by monitoring their ability to act as detergents in the solubilization of dimyristoylphosphatidylcholine vesicles in the order L-37pA Ͼ L1D-37pA Ͼ L2D37pA Ͼ L3D-37pA (56). However, a similar ability to stimulate cholesterol efflux was demonstrated in HeLa cells with these peptides (56). Because the L-to D-substituted peptides are neither CLA-1 ligands nor effective anti-inflammatory blockers, it appears that non-selective cholesterol depletion was not a factor in L-37pA-related blockage of LPS/LTA/Gro-EL-stimulated cytokine production.…”