ADP-ribosyltransferase-specific Modification of Human Neutrophil Peptide-1

摘要: Epithelial cells lining human airways and recruited to participate in the innate immune response part by releasing neutrophil peptides (HNP). Arginine-specific ADP-ribosyltransferases (ART) on surface of these can catalyze transfer ADP-ribose from NAD proteins. We reported that ART1, a mammalian ADP-ribosyltransferase, present epithelial airway, modified HNP-1, altering its function. ADP-ribosylated HNP-1 was identified bronchoalveolar lavage fluid (BALF) patients with asthma, idiopathic pulmonary fibrosis, or history smoking (and having two common polymorphic forms ART1 differ activity), but not normal volunteers lymphangioleiomyomatosis. Modified found sputum cystic fibrosis leukocyte granules volunteers. The finding ADP-ribosyl-HNP-1 BALF suggests modification occurred airway. Most individuals was, fact, mono- di-ADP-ribosylated. synthesized Escherichia coli, glycosylphosphatidylinositol-anchored released phosphatidylinositol-specific phospholipase C transfected NMU cells, expressed endogenously C2C12 myotubes arginine 14 secondary site 24. ADP-ribosylation substantially greater than ART3, ART4, ART5, Pseudomonas aeruginosa exoenzyme S, cholera toxin A subunit. Mouse ART2, which is an NAD:arginine able modify lesser extent ART1. Although significant degree it inhibited ART5 as well activities. Human β-defensin-1 (HBD1) poor transferase substrate. Reduction cysteine-rich defensins enhanced their ability serve acceptors. conclude appears be primarily activity occurs inflammatory conditions disease.