Literature DB >> 24594012

Airborne acrolein induces keratin-8 (Ser-73) hyperphosphorylation and intermediate filament ubiquitination in bronchiolar lung cell monolayers.

Philip C Burcham1, Albert Raso2, Peter J Henry2.   

Abstract

The combustion product acrolein is a key mediator of pulmonary edema in victims of smoke inhalation injury. Since studying acrolein toxicity in conventional in vitro systems is complicated by reactivity with nucleophilic culture media constituents, we explored an exposure system which delivers airborne acrolein directly to lung cell monolayers at the air-liquid interface. Calu-3 lung adenocarcinoma cells were maintained on membrane inserts such that the basal surface was bathed in nucleophile-free media while the upper surface remained in contact with acrolein-containing air. Cells were exposed to airborne acrolein for 30 min before they were allowed to recover in fresh media, with cell sampling at defined time points to allow evaluation of toxicity and protein damage. After prior exposure to acrolein, cell ATP levels remained close to controls for 4h but decreased in an exposure-dependent manner by 24h. A loss of transepithelial electrical resistance and increased permeability to fluorescein isothiocyanate-labeled dextran preceded ATP loss. Use of antibody arrays to monitor protein expression in exposed monolayers identified strong upregulation of phospho-keratin-8 (Ser(73)) as an early consequence of acrolein exposure. These changes were accompanied by chemical damage to keratin-8 and other intermediate filament family members, while acrolein exposure also resulted in controlled ubiquitination of high mass proteins within the intermediate filament extracts. These findings confirm the usefulness of systems allowing delivery of airborne smoke constituents to lung cell monolayers during studies of the molecular basis for acute smoke intoxication injury.
Copyright © 2014 Elsevier Ireland Ltd. All rights reserved.

Entities:  

Keywords:  Acrolein; Air–liquid interface; Keratin phosphorylation; Lung injury; Protein adducts; Ubiquitination

Mesh:

Substances:

Year:  2014        PMID: 24594012     DOI: 10.1016/j.tox.2014.02.010

Source DB:  PubMed          Journal:  Toxicology        ISSN: 0300-483X            Impact factor:   4.221


  4 in total

Review 1.  Molecular mechanisms of acrolein toxicity: relevance to human disease.

Authors:  Akshata Moghe; Smita Ghare; Bryan Lamoreau; Mohammad Mohammad; Shirish Barve; Craig McClain; Swati Joshi-Barve
Journal:  Toxicol Sci       Date:  2015-02       Impact factor: 4.849

2.  Alda-1 Protects Against Acrolein-Induced Acute Lung Injury and Endothelial Barrier Dysfunction.

Authors:  Qing Lu; Miles Mundy; Eboni Chambers; Thilo Lange; Julie Newton; Diana Borgas; Hongwei Yao; Gaurav Choudhary; Rajshekhar Basak; Mahogany Oldham; Sharon Rounds
Journal:  Am J Respir Cell Mol Biol       Date:  2017-12       Impact factor: 6.914

Review 3.  Phosphorylation and Reorganization of Keratin Networks: Implications for Carcinogenesis and Epithelial Mesenchymal Transition.

Authors:  Hyun Ji Kim; Won Jun Choi; Chang Hoon Lee
Journal:  Biomol Ther (Seoul)       Date:  2015-07-01       Impact factor: 4.634

4.  Keratins Are Altered in Intestinal Disease-Related Stress Responses.

Authors:  Terhi O Helenius; Cecilia A Antman; Muhammad Nadeem Asghar; Joel H Nyström; Diana M Toivola
Journal:  Cells       Date:  2016-09-10       Impact factor: 6.600

  4 in total

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