Abstract
Besides being a natural antibiotic, the human cathelicidin LL37, produced by epithelial cells and neutrophils, is an important immune-modulator. LL37 alone, or in complex with DNA, can activate inflammatory pathways in psoriasis, Systemic Lupus Erythematosus (SLE) and Rheumatoid Arthritis (RA). In this work, we describe the capacity of the recombinant monoclonal antibody RB137, previously shown to specifically recognize LL37 in its native form by ELISA, to detect LL37 by immunofluorescence in human tissues derived from SLE and RA patients. In these tissues, LL37 decorates DNA filaments resembling neutrophil-extracellular-trap (NET) structures. This antibody represents a valuable tool to detect the presence, the native state and the exact localization of LL37 in human tissues in health and disease.
Highlights
Human cathelicidin antimicrobial peptide (Uniprot P49913), called CAP18 or FALL39, is encoded by the human gene CAMP
RB137 detected LL37 in the proximity or in the same area of the MPO staining. This indicates that the antibody recognized LL37 expressed in neutrophils (MPO-positive cells) and LL37 was possibly released in the neutrophil-derived granules in the proximal environment
We addressed the presence of native LL37 in the joints of Rheumatoid Arthritis (RA) patients, and we found that LL37 co-localized with MPO (Fig. 2)
Summary
Human cathelicidin antimicrobial peptide (Uniprot P49913), called CAP18 or FALL39, is encoded by the human gene CAMP. Protocol: Biopsies were saturated with blocking buffer (PBS, 0.05% Tween 20, 4% BSA), for 1 hour at room temperature, and stained. The antibody RB137 was added at 1:50 dilution in blocking buffer (isotype control was added at 1:100 concentration) for 1 hour at room temperature in a humidified chamber.
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