Conversion of extracellular ATP into adenosine: a master switch in renal health and disease.

Dwyer, Karen, Kishore, BK and Robson, SC 2020, Conversion of extracellular ATP into adenosine: a master switch in renal health and disease., Nat Rev Nephrol, doi: 10.1038/s41581-020-0304-7.


Title Conversion of extracellular ATP into adenosine: a master switch in renal health and disease.
Author(s) Dwyer, KarenORCID iD for Dwyer, Karen orcid.org/0000-0002-4376-9720
Kishore, BK
Robson, SC
Journal name Nat Rev Nephrol
Place of publication England
Publication date 2020-07-08
ISSN 1759-507X
Summary ATP and its ultimate degradation product adenosine are potent extracellular signalling molecules that elicit a variety of pathophysiological functions in the kidney through the activation of P2 and P1 purinergic receptors, respectively. Extracellular purines can modulate immune responses, balancing inflammatory processes and immunosuppression; indeed, alterations in extracellular nucleotide and adenosine signalling determine outcomes of inflammation and healing processes. The functional activities of ectonucleotidases such as CD39 and CD73, which hydrolyse pro-inflammatory ATP to generate immunosuppressive adenosine, are therefore pivotal in acute inflammation. Protracted inflammation may result in aberrant adenosinergic signalling, which serves to sustain inflammasome activation and worsen fibrotic reactions. Alterations in the expression of ectonucleotidases on various immune cells, such as regulatory T cells and macrophages, as well as components of the renal vasculature, control purinergic receptor-mediated effects on target tissues within the kidney. The role of CD39 as a rheostat that can have an impact on purinergic signalling in both acute and chronic inflammation is increasingly supported by the literature, as detailed in this Review. Better understanding of these purinergic processes and development of novel drugs targeting these pathways could lead to effective therapies for the management of acute and chronic kidney disease.
Language eng
DOI 10.1038/s41581-020-0304-7

Document type: Journal Article
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in TR Web of Science
Scopus Citation Count Cited 1 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 3 Abstract Views  -  Detailed Statistics
Created: Fri, 17 Jul 2020, 13:09:05 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.