Medical Journals

Expression and Selective Up-regulation of Toxin-related Mono Adp-ribosyltransferases by Pathogen-associated Molecular Patterns in Alveolar Epithelial Cells.

Authors:
  • Balducci Enrico
  • Micossi Luigi G
  • Soldaini Elisabetta
  • Rappuoli Rino

From: Department of Comparative Morphology and Biochemistry, University of Camerino, 62032 Camerino, Italy. enrico_balducci@chiron.com

FEBS letters

  • Publish Date: Sep 2007
  • ISSN: 0014-5793
  • Volume: 581
  • Issue: 22
  • Pages: 4199-204
  • Medium: Print
  • Language: English
  • Citation (JAMA): Balducci Enrico, Micossi Luigi G, Soldaini Elisabetta, et al. Expression and Selective Up-regulation of Toxin-related Mono Adp-ribosyltransferases by Pathogen-associated Molecular Patterns in Alveolar Epithelial Cells.. FEBS Lett. Sep 2007;581:4199-204

Abstract

Mono ADP-ribosyltransferases (ARTs) are a family of enzymes related to bacterial toxins that possess adenosine diphosphate ribosyltransferase activity. We have assessed that A549 constitutively expressed ART1 on the cell surface and shown that lipotheicoic acid (LTA) and flagellin, but not lipopolysaccharide (LPS), peptidoglycan (PG) and poly (I:C), up-regulate ART1 in a time and dose dependent manner. These agonists did not alter the expression of ART3 and ART5 genes. Indeed, LTA and flagellin stimulation increased the level of ART1 protein and transcript while ART4 gene was activated after stimulation of cells with LPS, LTA, PAM and PG via TLR2 and TLR4 receptors. These results show that human ARTs possess a differential capacity to respond to bacteria cell wall components and might play a crucial role in innate immune response in airways.

Mesh Headings (Keywords): ADP Ribose Transferases, Animals, Arginine, Bacterial Toxins, Cell Line, Cricetinae, Cricetulus, Enzyme Activation, Epithelial Cells, Flagellin, Gene Expression Regulation, Enzymologic, Humans, Lipopolysaccharides, Peptides, Peptidoglycan, Pulmonary Alveoli, RNA, Messenger, Substrate Specificity, Teichoic Acids, Up-Regulation


Check for Full Text / PubMed Unique Identifier (PMID): 17707376


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

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The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


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