Cyclic ADP-Ribose Mediates Formyl Methionyl Leucyl Phenylalanine (fMLP)-Induced Intracellular Ca(2+) Rise and Migration of Human Neutrophils.

Cyclic ADP-Ribose Mediates Formyl Methionyl Leucyl Phenylalanine (fMLP)-Induced Intracellular Ca(2+) Rise and Migration of Human Neutrophils. Research Abstract Details 

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Cyclic ADP-Ribose Mediates Formyl Methionyl Leucyl Phenylalanine (fMLP)-Induced Intracellular Ca(2+) Rise and Migration of Human Neutrophils. Abstract Text:

Katsuya Morita,Minoru Saida,Norimitsu Morioka,Tomoya Kitayama,Yasumasa Akagawa,Toshihiro Dohi,

Although cyclic ADP-ribose (cADPR), a novel Ca(2+)-mobilizing mediator, is suggested to be involved in the functions of neutrophils in rodents, its role in human neutrophils remains unclear. The present study examined the ability of cADPR to mobilize Ca(2+) and mediate formyl methionyl leucyl phenylalanine (fMLP)-stimulated increase in cytosolic free Ca(2+) concentration ([Ca(2+)](i)) and migration in human neutrophils. cADPR induced Ca(2+) release from digitonin-permeabilized neutrophils, and the release was blocked by 8Br-cADPR, an antagonist of cADPR. Immunophilin ligands, FK506 and rapamycin, but not cyclosporine A, inhibited cADPR-induced Ca(2+) release. 8Br-cADPR partially reduced fMLP-induced [Ca(2+)](i) rise and abolished the rise in combination with 2APB, an IP(3)-receptor antagonist. Anti-CD38Ab and NADase that interfere with cADPR formation, reduced the fMLP-induced [Ca(2+)](i) rise. When beta-NAD(+), a substrate of ADP-ribosyl cyclase, and cADPR were added to the medium, the former gradually increased [Ca(2+)](i) and the latter potentiated the fMLP-induced [Ca(2+)](i) rise. The beta-NAD(+)-induced [Ca(2+)](i) rise in Ca(2+)-free medium was inhibited by anti-CD38Ab, 8Br-cADPR, FK506, ruthenium red, and thapsigargin. mRNAs of nucleoside transporter (NT), ENT1, ENT2, CNT, and CNT3 were expressed in neutrophils; and their inhibitors, inosine, uridine, and s-(4-nitrobenzyl)-6-thioinosine, reduced the [Ca(2+)](i) rise induced by beta-NAD(+) and fMLP. fMLP-timulated migration was inhibited by the removal of Ca(2+) from the medium or by the addition of 8Br-cADPR, anti-CD38Ab, NADase, and NT inhibitors. These results suggest that cADPR was synthesized extracellularly by CD38, transported into the cells through NTs, and then Ca(2+) was mobilized by FK506-binding protein-dependent process. This process may be involved in fMLP-induced intracellular Ca(2+) signaling and migration in human neutrophils.

Cyclic ADP-Ribose Mediates Formyl Methionyl Leucyl Phenylalanine (fMLP)-Induced Intracellular Ca(2+) Rise and Migration of Human Neutrophils. Publishing Authors By Initials

K Morita,M Saida,N Morioka,T Kitayama,Y Akagawa,T Dohi,

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Cyclic ADP-Ribose Mediates Formyl Methionyl Leucyl Phenylalanine (fMLP)-Induced Intracellular Ca(2+) Rise and Migration of Human Neutrophils. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of pharmacological sciences

VOLUME: 106

Page Numbers: 492-504

Journal Abbreviation: J. Pharmacol. Sci.

ISSN: 1347-8613

DAY: 12

MONTH: 03

YEAR: 2008

Cyclic ADP-Ribose Mediates Formyl Methionyl Leucyl Phenylalanine (fMLP)-Induced Intracellular Ca(2+) Rise and Migration of Human Neutrophils. Information

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LANGUAGE: eng

NlmUniqueID: 101167001

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AFFILIATION: Department of Dental Pharmacology, Hiroshima University Graduate School of Biomedical Sciences, Japan.

Country: Japan

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MEDLINETA: J Pharmacol Sci

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