S1P and plasmalogen derived fatty aldehydes in cellular signaling and functions.


Journal

Biochimica et biophysica acta. Molecular and cell biology of lipids
ISSN: 1879-2618
Titre abrégé: Biochim Biophys Acta Mol Cell Biol Lipids
Pays: Netherlands
ID NLM: 101731727

Informations de publication

Date de publication:
07 2020
Historique:
received: 06 10 2019
revised: 24 01 2020
accepted: 09 03 2020
pubmed: 17 3 2020
medline: 23 10 2020
entrez: 16 3 2020
Statut: ppublish

Résumé

Long-chain fatty aldehydes are present in low concentrations in mammalian cells and serve as intermediates in the interconversion between fatty acids and fatty alcohols. The long-chain fatty aldehydes are generated by enzymatic hydrolysis of 1-alkyl-, and 1-alkenyl-glycerophospholipids by alkylglycerol monooxygenase, plasmalogenase or lysoplasmalogenase while hydrolysis of sphingosine-1-phosphate (S1P) by S1P lyase generates trans ∆2-hexadecenal (∆2-HDE). Additionally, 2-chloro-, and 2-bromo- fatty aldehydes are produced from plasmalogens or lysoplasmalogens by hypochlorous, and hypobromous acid generated by activated neutrophils and eosinophils, respectively while 2-iodofatty aldehydes are produced by excess iodine in thyroid glands. The 2-halofatty aldehydes and ∆2-HDE activated JNK signaling, BAX, cytoskeletal reorganization and apoptosis in mammalian cells. Further, 2-chloro- and 2-bromo-fatty aldehydes formed GSH and protein adducts while ∆2-HDE formed adducts with GSH, deoxyguanosine in DNA and proteins such as HDAC1 in vitro. ∆2-HDE also modulated HDAC activity and stimulated H3 and H4 histone acetylation in vitro with lung epithelial cell nuclear preparations. The α-halo fatty aldehydes elicited endothelial dysfunction, cellular toxicity and tissue damage. Taken together, these investigations suggest a new role for long-chain fatty aldehydes as signaling lipids, ability to form adducts with GSH, proteins such as HDACs and regulate cellular functions.

Identifiants

pubmed: 32171908
pii: S1388-1981(20)30073-1
doi: 10.1016/j.bbalip.2020.158681
pmc: PMC7214093
mid: NIHMS1575179
pii:
doi:

Substances chimiques

Aldehydes 0
Plasmalogens 0
Histone Deacetylases EC 3.5.1.98
Aldehyde-Lyases EC 4.1.2.-
sphingosine 1-phosphate lyase (aldolase) EC 4.1.2.27
2-hexadecenal Z79H35Z0RU

Types de publication

Journal Article Research Support, N.I.H., Extramural Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

158681

Subventions

Organisme : NHLBI NIH HHS
ID : P01 HL060678
Pays : United States
Organisme : NHLBI NIH HHS
ID : P01 HL126609
Pays : United States

Informations de copyright

Copyright © 2020 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare no conflict of interest and no financial obligations.

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Auteurs

David L Ebenezer (DL)

Department of Pharmacology, University of Illinois, Chicago, IL, United States of America.

Panfeng Fu (P)

Department of Pharmacology, University of Illinois, Chicago, IL, United States of America.

Ramaswamy Ramchandran (R)

Department of Pharmacology, University of Illinois, Chicago, IL, United States of America.

Alison W Ha (AW)

Department of Biochemistry and Molecular Genetics, University of Illinois, Chicago, IL, United States of America.

Vijay Putherickal (V)

Department of Pharmacology, University of Illinois, Chicago, IL, United States of America.

Tara Sudhadevi (T)

Department of Pediatrics, University of Illinois, Chicago, IL, United States of America.

Anantha Harijith (A)

Department of Pediatrics, University of Illinois, Chicago, IL, United States of America.

Fabian Schumacher (F)

Institute of Nutritional Sciences, University of Potsdam, Germany; Department of Molecular Biology, University of Duisburg-, Essen, Germany.

Burkhard Kleuser (B)

Institute of Nutritional Sciences, University of Potsdam, Germany.

Viswanathan Natarajan (V)

Department of Pharmacology, University of Illinois, Chicago, IL, United States of America; Department of Medicine, University of Illinois, Chicago, IL, United States of America. Electronic address: visnatar@uic.edu.

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