| http://purl.uniprot.org/citations/16627471 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16627471 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/16627471 | http://www.w3.org/2000/01/rdf-schema#comment | "Epithelial cells lining human airways and cells recruited to airways participate in the innate immune response in part by releasing human neutrophil peptides (HNP). Arginine-specific ADP-ribosyltransferases (ART) on the surface of these cells can catalyze the transfer of ADP-ribose from NAD to proteins. We reported that ART1, a mammalian ADP-ribosyltransferase, present in epithelial cells lining the human airway, modified HNP-1, altering its function. ADP-ribosylated HNP-1 was identified in bronchoalveolar lavage fluid (BALF) from patients with asthma, idiopathic pulmonary fibrosis, or a history of smoking (and having two common polymorphic forms of ART1 that differ in activity), but not in normal volunteers or patients with lymphangioleiomyomatosis. Modified HNP-1 was not found in the sputum of cystic fibrosis patients or in leukocyte granules of normal volunteers. The finding of ADP-ribosyl-HNP-1 in BALF but not in leukocyte granules suggests that the modification occurred in the airway. Most of the HNP-1 in the BALF from individuals with a history of smoking was, in fact, mono- or di-ADP-ribosylated. ART1 synthesized in Escherichia coli, glycosylphosphatidylinositol-anchored ART1 released with phosphatidylinositol-specific phospholipase C from transfected NMU cells, or ART1 expressed endogenously on C2C12 myotubes modified arginine 14 on HNP-1 with a secondary site on arginine 24. ADP-ribosylation of HNP-1 by ART1 was substantially greater than that by ART3, ART4, ART5, Pseudomonas aeruginosa exoenzyme S, or cholera toxin A subunit. Mouse ART2, which is an NAD:arginine ADP-ribosyltransferase, was able to modify HNP-1, but to a lesser extent than ART1. Although HNP-1 was not modified to a significant degree by ART5, it inhibited ART5 as well as ART1 activities. Human beta-defensin-1 (HBD1) was a poor transferase substrate. Reduction of the cysteine-rich defensins enhanced their ability to serve as ADP-ribose acceptors. We conclude that ADP-ribosylation of HNP-1 appears to be primarily an activity of ART1 and occurs in inflammatory conditions and disease."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m603042200"xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/author | "Moss J."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/author | "Stevens L.A."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/author | "Levine R.L."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/author | "Bourgeois C."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/author | "Steagall W.K."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/author | "Paone G."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/author | "Gochuico B.R."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/pages | "17054-17060"xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/title | "ADP-ribosyltransferase-specific modification of human neutrophil peptide-1."xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://purl.uniprot.org/core/volume | "281"xsd:string |
| http://purl.uniprot.org/citations/16627471 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16627471 |
| http://purl.uniprot.org/citations/16627471 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16627471 |
| http://purl.uniprot.org/citations/16627471 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16627471 |
| http://purl.uniprot.org/citations/16627471 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16627471 |
| http://purl.uniprot.org/enzyme/2.4.2.31 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16627471 |
| http://purl.uniprot.org/uniprot/#_P52961-mappedCitation-16627471 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16627471 |
| http://purl.uniprot.org/uniprot/P52961 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/16627471 |