Open AccessRB137 recognizes LL37 in neutrophil-extracellular trap-like (NET) structures in systemic lupus erythematosus and rheumatoid arthritis inflamed tissues by immunofluorescence in histological sections
Author(s) -
Roberto Lande,
Stefano Alivernini,
Barbara Tolusso,
Francesca Spadaro,
Mario Falchi,
Raffaella Palazzo,
Immacolata Pietraforte,
Carlo Chizzolini,
Kostantino Giannakakis,
Francesca Romana Spinelli,
Cristiano Alessandri,
Elisa Gremese,
Fabrizio Conti,
Loredana Frasca
Publication year - 2020
Publication title -
antibody reports
Language(s) - English
Resource type - Journals
ISSN - 2624-8557
DOI - 10.24450/journals/abrep.2020.e235
Subject(s) - neutrophil extracellular traps , rheumatoid arthritis , immunology , medicine , immunofluorescence , monoclonal antibody , immune system , antibody , arthritis , inflammation , recombinant dna , biology , gene , biochemistry
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.