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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Ecto-nucleoside triphosphate diphosphohydrolase 1 (E-NTPDase1/CD39) regulates neutrophil chemotaxis by hydrolyzing released ATP to adenosine
Journal of Biological Chemistry, Volume 283, No. 42, Year 2008
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Description
Polymorphonuclear neutrophils release ATP in response to stimulation by chemoattractants, such as the peptide N-formylmethionyl-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 knockout 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. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
Authors & Co-Authors
Robson, Simon Christopher
United States, Boston
Beth Israel Deaconess Medical Center
Insel, Paul A.
United States, La Jolla
University of California, San Diego
Junger, Wolfgang Georg
United States, La Jolla
University of California, San Diego
United States, Boston
Beth Israel Deaconess Medical Center
Statistics
Citations: 104
Authors: 3
Affiliations: 2
Identifiers
Doi:
10.1074/jbc.M800039200
ISSN:
00219258