Relationship of phosphatidylinositol bisphosphate hydrolysis to calcium mobilization and functional activation in fluoride-treated neutrophils.

English, Denis; Debono, D J; Gabig, Theodore G.

doi:10.1172/jci113040

Cited by 34 publications

(12 citation statements)

References 48 publications

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“…This InsP3-independent action of mastoparan is relatively insensitive to 15-HETE also suppressed the PMN oxidative burst elicited with another G protein activator AIFZ (35). In contrast to mastoparan, however, the AlFZ-induced rise in [Ca2+]i is quite slow (36), and PMN responsiveness to AIF-is pertussis toxin-insensitive (37 (42). In addition, in some cells 15-HETE is preferentially incorporated into phosphatidylinositol, which yields altered species of diacylglycerol when the cells are hormonally stimulated (39).…”

Section: Discussionmentioning

confidence: 85%

Transmembrane signaling in human polymorphonuclear neutrophils: 15(S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid modulates receptor agonist-triggered cell activation.

Smith

Justen

Nidy

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACT15(S)-Hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid (15-HETE) exerted a time-and concentrationdependent inhibition of superoxide anion (O°) production and exocytosis of both azurophil and specific granule constituents from human polymorphonuclear neutrophils (PMN) stimulated with the receptor-specific agonists, N-formylmethionylleucylphenylalanine (FMLP), platelet-activating factor, and leukotriene B4, but not that elicited by phorbol 12-myristate 13-acetate. 15-HETE did not alter the binding of FMLP to its specific receptors on PMN but, rather, appeared to interfere with a subsequent process in signal transduction. Receptorcoupled production of inositol 1,4,5-trisphosphate (InsP3) and increases in cytosolic free calcium elicited with FMLP, plateletactivating factor, and leukotriene B4 were suppressed by 15-HETE. 15--HETE did not, however, inhibit the mobilization of45Ca from intracellular stores elicited by the addition ofInsP3 to permeabilized PMN. 15-HETE suppressed 0-production and increases in intracellular [Ca2+] induced when cell-surface receptors were bypassed and the PMN were activated directly by the guanine nucleotide-binding protein (G protein) activators aluminum fluoride (AIF ) and mastoparan. 15-HETE, however, did not perturb all G protein functions because cAMP production in FMLP-activated PMN was essentially unaffected by 15-HETE. These data support the proposition that 15-HETE modulates receptor-triggered activation of PMN either by uncoupling G protein stimulation of phospholipase C or by directly inhibiting phospholipase C, thus inhibiting the InsP3-dependent rise in intracellular [Ca2+] that is prerequisite for PMN responsiveness to receptor agonists.

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Section: Discussionmentioning

confidence: 85%

Transmembrane signaling in human polymorphonuclear neutrophils: 15(S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid modulates receptor agonist-triggered cell activation.

Smith

Justen

Nidy

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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“…Despite the absence of any putative signals prior to G-protein activation, AlF-induced an extensive and sustained increase in F-actin content in intact human neutrophils. The AlF-response was characterized by an initial lag period, similar to that preceding AlF -induced activation of the respiratory burst in human neutrophils (27,28). A reason for this lag period could be that AlF-diffuses slowly to its binding site on G proteins.…”

Section: Discussionmentioning

confidence: 97%

Involvement of GTP-binding proteins in actin polymerization in human neutrophils.

Bengtsson

Särndahl

Stendahl

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

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The motility of human neutrophils, which is of vital importance for the role of these cells in host defense, is based on rapid and dynamic changes of the filamentous actin (F-actin) network. Consequently, to understand how neutrophils move and ingest particles, we need to know how polymerization and depolymerization of actin are regulated. Previous studies by several investigators have, based on indirect evidence obtained with pertussis toxin, suggested a role for GTP-binding protein(s) (G protein) in chemotaxis-induced, but not phagocytosis-induced, reorganization of the F-actin network. The aim of the present investigation was to study the effects of directly activated G proteins (i.e., without prior ligand-receptor complex formation) on the F-actin content in human neutrophils. AMF4 induced a pronounced and sustained increase in F-actin in intact neutrophils. This effect coincided with an increase in cytosolic free Ca2+, indicating that phospholipase C and the subsequent transduction mechanism were also activated. Inhibition of phospholipase C activity by extensive depression of the cytosolic free Ca2+ level (< 20 nM) only marginally affected the AlFj,-induced rise in F-actin content. The major part of the AMFj -induced rise in F-actin content was also resistant to pertussis toxin, suggesting that pertussis toxin-insensitive G proteins in neutrophils are also able to trigger actin polymerization. The specificity of AIFZ in activating G proteins was also tested in permeabilized cells. In this case the effect was more rapid and could be totally abolished by guanosine 5'-[13-thioldiphosphate. In analogy, in permeabilized cells guanosine 5'-[y-thioltriphosphate mimicked the effect of AIF4 on actin polymerization, and the effect induced by this nonhydrolyzable GTP analogue could also be totally abolished by guanosine 5'-[P-thio]diphosphate. In summary, the present data support our previous hypothesis that G proteins are intimately linked to actin polymerization in human neutrophils.

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“…For diradylglycerol mass, this stimulus is far more potent than fMLP (including with cytochalasin B or other forms of priming), consistent with its derivation from multiple mechanisms and phospholipid pools. Regarding phospholipase C activation, English and colleagues [37] previously showed that fluoride is an extremely potent stimulus for phosphoinositide hydrolysis and inositol phosphate release. Based on ethanol inhibition, the present studies suggest that phospholipase C also acts on PC under these conditions.…”

Section: Discussion Referencesmentioning

confidence: 99%

“…In contrast to the rapid activation of superoxide by fMLP, fluoride activates after a prolonged lag (about 5 to 8 min). Previously, English and colleagues [37] demonstrated that fluoride activates the phospholipase C-dependent hydrolysis of PIP2. In addition, fluoride causes calcium mobilization [4], arachidonic acid release [31], and increased cyclic AMP levels in neutrophils [38].…”

Section: Introductionmentioning

confidence: 99%

Fluoride activates diradylglycerol and Superoxide generation in human neutrophils via PLD/PA phosphohydrolase‐dependent and ‐independent pathways

1990

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In contrast to the rapid, ethanol-inhibited superoxide generation by the receptor-linked agonist formyl-methionyl-leucyl-phenylalanine (fMLP), fluoride-activated superoxide generation occurs after a prolonged lag, and as shown herein is relatively ethanol-insensitive. We have investigated fluoride-activation of diradylglycerol generation and phospholipase D activity. Fluoride induces a very large increase in diradylglycerol mass (both 1,2-diacylglycerol (DAG) and I-O-alkyl,2-acylglycerol (EAG)), with kinetics similar to superoxide generation. Unlike fMLP-activated diglyceride generation which is completely inhibited by ethanol, that produced by fluoride is only partially (30%) blocked. When the phosphatidylcholine pool is 3H-prelabeled, fluoride activates both PHlphosphatidic acid (PA) and PH]diglyceride generation with similar kinetics. Partial inhibition of the production of these species by ethanol was seen, coincident with the appearance of PHlphosphatidylethanol, indicating phospholipase D-dependent transphosphatidylation had occurred. The data are consistent with the fluoride activation of PA and diglyceride generation by both phospholipase D-dependent and -independent (presumably phospholipase C) mechanisms.

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Relationship of phosphatidylinositol bisphosphate hydrolysis to calcium mobilization and functional activation in fluoride-treated neutrophils.

Cited by 34 publications

References 48 publications

Transmembrane signaling in human polymorphonuclear neutrophils: 15(S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid modulates receptor agonist-triggered cell activation.

Transmembrane signaling in human polymorphonuclear neutrophils: 15(S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid modulates receptor agonist-triggered cell activation.

Involvement of GTP-binding proteins in actin polymerization in human neutrophils.

Fluoride activates diradylglycerol and Superoxide generation in human neutrophils via PLD/PA phosphohydrolase‐dependent and ‐independent pathways

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