ADP-ribosyltransferase-specific modification of human neutrophil peptide-1.

The Journal of Biological Chemistry
Gregorino PaoneJoel Moss

Abstract

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 p...Continue Reading

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Citations

Jul 24, 2010·Amino Acids·Sabrina LaingFriedrich Haag
Nov 10, 2009·Proceedings of the National Academy of Sciences of the United States of America·Linda A StevensJoel Moss
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Mar 24, 2021·Cellular and Molecular Life Sciences : CMLS·Massimiliano GasparriniNadia Raffaelli
Mar 26, 2021·Frontiers in Immunology·Stephan MenzelFriedrich Koch-Nolte

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