Corriden, R; Chen, Y; Inoue, Y; Beldi, G; Robson, S.C.; Insel, P.A.; Junger, W.G. (2008). Ecto-nucleoside triphosphate diphosphohydrolase 1 (E-NTPDase1/CD39) regulates neutrophil chemotaxis by hydrolyzing released ATP to adenosine. Journal of biological chemistry, 283(42), pp. 28480-6. Bethesda, Md.: American Society for Biochemistry and Molecular Biology 10.1074/jbc.M800039200
Full text not available from this repository.Polymorphonuclear neutrophils release ATP in response to stimulation by chemoattractants, such as the peptide N-formyl-methionyl-leucyl-phenylalanine. Released ATP and the hydrolytic product adenosine regulate chemotaxis of neutrophils by sequentially activating purinergic nucleotide and adenosine receptors, respectively. Here we show that that ecto-nucleoside triphosphate diphosphohydrolase 1 (E-NTPDase1, CD39) is a critical enzyme for hydrolysis of released ATP by neutrophils and for cell migration in response to multiple agonists (N-formyl-methionyl-leucyl-phenylalanine, interleukin-8, and C5a). Upon stimulation of human neutrophils or differentiated HL-60 cells in a chemotactic gradient, E-NTPDase1 tightly associates with the leading edge of polarized cells during chemotaxis. Inhibition of E-NTPDase1 reduces the migration speed of neutrophils but not their ability to detect the orientation of the gradient field. Studies of neutrophils from E-NTPDase1 knock-out mice reveal similar impairments of chemotaxis in vitro and in vivo. Thus, E-NTPDase1 plays an important role in regulating neutrophil chemotaxis by facilitating the hydrolysis of extracellular ATP.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Department of Gastro-intestinal, Liver and Lung Disorders (DMLL) > Clinic of Visceral Surgery and Medicine > Visceral Surgery |
UniBE Contributor: |
Beldi, Guido Jakob Friedrich |
ISSN: |
0021-9258 |
ISBN: |
0021-9258 (Print) 28 |
Publisher: |
American Society for Biochemistry and Molecular Biology |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 15:04 |
Last Modified: |
05 Dec 2022 14:19 |
Publisher DOI: |
10.1074/jbc.M800039200 |
Web of Science ID: |
000259969300050 |
URI: |
https://boris.unibe.ch/id/eprint/27697 (FactScience: 110171) |
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