Rac-1-mediated O2secretion requires Ca2+influx in neutrophil-like HL-60 cells

Valentin, François; Bueb, Jean-Luc; Capdeville-Atkinson, Christine; Tschirhart, Eric

doi:10.1054/ceca.2001.0203

Cited by 21 publications

(20 citation statements)

References 27 publications

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“…The exact source of Ca 2ϩ release in response to oxidants remains controversial, and molecular targets of oxidants have not yet been clearly defined (57). On the other hand, oxygen radicals may not be involved in Ca 2ϩ flux (61), but rather the Ca 2ϩ mobilization may be responsible for ROS production (58). We show that ROS are upstream mediators of Ca 2ϩ flux in MMCs and that ROS-dependent Ca 2ϩ flux negatively regulates PDGF AA-induced migration.…”

Section: Discussionmentioning

confidence: 93%

PDGF receptor-β modulates metanephric mesenchyme chemotaxis induced by PDGF AA

Ricono

Wagner²,

Gorin³

et al. 2009

American Journal of Physiology-Renal Physiology

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PDGF B chain or PDGF receptor (PDGFR)-beta-deficient (-/-) mice lack mesangial cells. To study responses of alpha- and beta-receptor activation to PDGF ligands, metanephric mesenchymal cells (MMCs) were established from embryonic day E11.5 wild-type (+/+) and -/- mouse embryos. PDGF BB stimulated cell migration in +/+ cells, whereas PDGF AA did not. Conversely, PDGF AA was chemotactic for -/- MMCs. The mechanism by which PDGFR-beta inhibited AA-induced migration was investigated. PDGF BB, but not PDGF AA, increased intracellular Ca(2+) and the production of reactive oxygen species (ROS) in +/+ cells. Transfection of -/- MMCs with the wild-type beta-receptor restored cell migration and ROS generation in response to PDGF BB and inhibited AA-induced migration. Inhibition of Ca(2+) signaling facilitated PDGF AA-induced chemotaxis in the wild-type cells. The antioxidant N-acetyl-l-cysteine (NAC) or the NADPH oxidase inhibitor diphenyleneiodonium (DPI) abolished the BB-induced increase in intracellular Ca(2+) concentration, suggesting that ROS act as upstream mediators of Ca(2+) in suppressing PDGF AA-induced migration. These data indicate that ROS and Ca(2+) generated by active PDGFR-beta play an essential role in suppressing PDGF AA-induced migration in +/+ MMCs. During kidney development, PDGFR beta-mediated ROS generation and Ca(2+) influx suppress PDGF AA-induced chemotaxis in metanephric mesenchyme.

show abstract

Section: Discussionmentioning

confidence: 93%

PDGF receptor-β modulates metanephric mesenchyme chemotaxis induced by PDGF AA

Ricono

Wagner²,

Gorin³

et al. 2009

American Journal of Physiology-Renal Physiology

View full text Add to dashboard Cite

show abstract

“…The intracellular mechanisms linking [Ca 2+ ] i elevation to O 2 − U generation are unclear. Rac-1, a monomeric G-protein, has been shown to stimulate NADPH oxidase and Valentin et al [23] hypothesized that [Ca 2+ ] i mobilization leads to Rac-1 activation, which in turn stimulates NAPDH oxidase activity leading to O 2 − U production. Movitz et al [24] reported that the translocation of cytosolic factors, a prerequisite for obtaining the intracellular NADPH-oxidase activity in activated neutrophils, is not induced by Ca 2+ per se, but rather by some additional signalling molecule(s) generated in response to an elevation of intracellular Ca 2+ .…”

Section: Discussionmentioning

confidence: 99%

Isolation and activation of human neutrophils in vitro. The importance of the anticoagulant used during blood collection

Freitas

Porto

Lima

et al. 2008

Clinical Biochemistry

104

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“…Later, it was reported that PKC , activated by thrombin, can phosphorylate RhoGDI and regulates the dissociation of Rac/RhoGDI complex catalyzing the release of bound GTPases, and subsequent Rac translocation to the plasma membrane (Mehta et al, 2001). Consistent with these findings, Valentin et al (Valentin et al, 2001) determined that Ca 2+ influx plays a primordial role in the plasma membrane translocation of Rac1 in neutrophil-like HL-60 cells (Fig. 2).…”

Section: Monomeric G Protein Racmentioning

confidence: 57%