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. Author manuscript; available in PMC: 2015 Sep 1.
Published in final edited form as: Arthritis Rheumatol. 2014 Sep;66(9):2532–2544. doi: 10.1002/art.38703

Figure 2. NET-derived MPO, NOS and NOX modify human HDL.

Figure 2

Immunofluorescent staining and immunoblotting was used to identify possible enzymatic sources of HDL nitration. (A) NOX subunits, p22 and p47, and two NOS isoforms, eNOS and iNOS, were detected in human NETs. Control neutrophil and lupus LDG NETs were added to control, unoxidized HDL. Resulting levels of (B) MPO-specific Cl-Tyr, and (C) RNS-mediated N-Tyr oxidation were quantified by mass spectrometry. 3-AT, NMMA and DPI were added to block MPO, NOS and NOX activity, respectively. The PAD inhibitor Cl-Am was added to LDGs to block spontaneous NETosis. For control neutrophils, absence of PMA stimulation was used as a negative control for NETosis. (N= 6/group; ** p<0.007, *** p=0.0002, **** p< 0.0001. Data are displayed as mean ± SEM).