Chemotactic factor causes rapid decreases in phosphatidylinositol,4,5-bisphosphate and phosphatidylinositol 4-monophosphate in rabbit neutrophils

Volpi, M.; Yassin, Rihab R.; Naccache, Paul H.; Sha'afi, R.I.

doi:10.1016/0006-291x(83)91711-4

Cited by 189 publications

(53 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Actin polymerization and actin-gelsolin dissociation are, however, maximal at a time (10 -15 s after fMLP stimulation) when PtdIns(4,5)P 2 levels drop (16,17), implying that PtdIns(4,5)P 2 synthesis does not correlate with these responses in vivo (18,19).…”

mentioning

confidence: 99%

The Small GTP-binding Protein Rac Promotes the Dissociation of Gelsolin from Actin Filaments in Neutrophils

Arcaro

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

Gelsolin is an actin filament-capping protein that has been shown to play a key role in cell migration. Here we have studied the involvement of phosphoinositide 3-kinase (PI 3-kinase) and GTP-binding proteins (G-proteins) in the regulation of gelsolin-actin interactions in neutrophils. Inhibition of PI 3-kinase activity in vivo by wortmannin did not affect the dissociation of actin-gelsolin (1:1) complexes induced by neutrophil stimulation with N-formyl-Met-Leu-Phe. Guanosine 5-[␥-thio]triphosphate (GTP␥S) indirectly promoted the dissociation of actin-gelsolin complexes in a cell-free system using neutrophil cytosol, and this effect was blocked by the GDP dissociation inhibitor for Rho (Rho-GDI). The GTP␥S-loaded i ␣ 2 and the ␤ 1 ␥ 2 subunits of heterotrimeric G-proteins (G i ␣ 2 and G␤ 1 ␥ 2 ) also triggered actingelsolin dissociation in a Rho-GDI-sensitive manner. GTP-loaded activated Rac, but not activated Rho, induced the dissociation of cytosolic actin-gelsolin complexes. The guanine nucleotide exchange on Rac was increased by addition of GTP␥S-loaded G i ␣ 2 or G␤ 1 ␥ 2 to neutrophil cytosol. These findings suggest that activation of Rac by G-protein-coupled receptors in neutrophils triggers uncapping of actin filaments, independently of PI 3-kinase.

show abstract

mentioning

confidence: 99%

The Small GTP-binding Protein Rac Promotes the Dissociation of Gelsolin from Actin Filaments in Neutrophils

Arcaro

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Most studies on inositol lipid-specific PLC in neutrophils dealt with membrane-associated enzyme in intact, permeabilized or broken cell preparations [5][6][7][8][9]. The neutrophil enzyme was stimulated by binding of chemotactic ligands to surface receptors coupled to G proteins [7][8][9][10].…”

Section: Discussionmentioning

confidence: 99%

“…At~ba:viations: PLC, phosphoinositide-specific phospholipase C; DAG, 2-dia~lglycerol; PIP~, phosphatidylinositol 4,5-bisphosphate; IP~, inositoi lA,5-trisphosphate; PE, phosphatidylethanolamine. tion pathways involving inositol lipid turnover [5][6][7][8]. Participation of G proteins in the activation of PLC in intact and permeabilized neutrophils and in neutrophil membranes has been documented [9,10].…”

Section: Introductionmentioning

confidence: 99%

Human neutrophil cytosolic phospholipase C: partial characterization

Faber¹,

Aviram²

1992

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metaboli

View full text Add to dashboard Cite

The activity of n0utrophil cytosolic phospholipase C on PIP, and P! was compared employing ['~H]inositol-labeled heat-inactivated membranes of differentiated HL-60 cells, into which tracer ['~2P]PIP, was incorporated. Hydrolysis of PIP 2 did not require Ca -~+ and was stimulated when the content of PIP, in the i~embrane was increased by incorporation of unlabeled inositoi lipid. At equal concentrations of PI and PIP, in the membrane, hydrolysis of PIP~ was faster and no evidence of competition between the two substrates was obtained. Incorporation of P! into PE-[ "~-" P]PIP, vesicles, accelerated PIP e hydrolysis also at conditions that favor hydrolysis of PI. Partial purification of neutrophil cytosolic PLC on Q Sepharose, phenyl Sepharose and heparin-Agarose columns is described. From heparin-Agarose column, two PLC activity peaks exhibiting different substrate spccificities were elutcd. The elution profile of the main PLC species from Superose 12 gel filtration column was compatible with an approx. 150 kDa protein.

show abstract

Section: Introductionmentioning

confidence: 99%

“…Several studies have indicated the involvement of diacylglycerol (DG) /protein kinase C (PKC) , since PKC activators, phorbol 12-myristate 13-acetate (PMA) (De Chatelet et al, 1 9 7 6 ) and some DGs (Fujita et al, 1984; Cox et al, 1 9 8 6 ) , activate the NADPH-oxidase system. Stimulation of neutrophils with receptor-linked agonists such as Nformyl-methionyl-leucyl-phenylalanine (FMLP) results in the activation of PLC β 2 and hydrolysis of phosphatidylinositol 4,5-bisphosphate, leading to the generation of inositol 1,4,5-triphosphate, a calcium m e s s e n g e r, and DG (Volp et al, 1983; Ohta et al, 1 9 8 5 ;Smith et al, 1986).Activation of the oxidase involves the translocation of a fraction (<10%) of p47-phox and p67-phox to the plasmalemma where the functional complex is assembled Nauseef et al, 1991;Tyagi et al, 1 9 9 2 ) . One route of stimulation that occurs with activators of PKC, such as PMA, involves multisite phosphorylation of p47-phox (Heyworth and Badwey, 1990).…”

mentioning

confidence: 99%

Calyculin A modulates activation of the NADPH-oxidase in Me2SO-differentiated HL-60 cells

Park

Uhlinger²,

Chung³

et al. 1998

Exp Mol Med

View full text Add to dashboard Cite

followed by PMA may be due to diminished translocation of the p47-phox and p67-phox, cytosolic components of the oxidase, and inhibition of arachidonic acid release. Interestingly calyculin A pretreatment followed by either agonist significantly enhanced mitogen-activated-protein kinase (MAPK) activity. The differential effects of pretreatment with calyculin A on subsequent oxidase s t i m u l a t i o n elicited by FMLP or PMA provide further evidence for substantial heterogeneity in the acti-vation of the respiratory burst.Keywords: NADPH-oxidase, calyculin A, p47-phox, p67-phox, arachidonic acid IntroductionStimulation of neutrophils causes a "respiratory burst" including increased oxygen consumption and the generation of reactive oxygen metabolites such as O 2 -and H 2 O 2 , which provide a major bactericidal mechanism in these cells (Babior, 1984a). The enzymatic activity responsible for this respiratory burst resides in membrane-bound NADPH-oxidase, which reduces molecular oxygen to O 2 -( B a b i o r, 1984b). The NADPH-oxidase consists of integral membrane proteins (cytochrome b558) (Cross e t a l . , 1981; Gabig and Lefker, 1984) and "soluble" (cytoplasmic/ cytoskeletal) components. The latter include p47-phox, p67-phox, and rac 2, a ras-related GTP-binding protein (Nunoi et al., 1988;Lomax et al., 1990;Abo et al., 1991a;Abo and Pick, 1991b;Uhlinger et al., 1993). The oxidase is dormant in resting cells, but can be activated by both particulate and soluble stimuli (Babior et al., 1975; Babior, 1984b). The mechanism for the activation of the oxidase is very complex and has been the subject of intense study. Several studies have indicated the involvement of diacylglycerol (DG) /protein kinase C (PKC) , since PKC activators, phorbol 12-myristate 13-acetate (PMA) (De Chatelet et al., 1 9 7 6 ) and some DGs (Fujita et al., 1984; Cox et al., 1 9 8 6 ) , activate the NADPH-oxidase system. Stimulation of neutrophils with receptor-linked agonists such as Nformyl-methionyl-leucyl-phenylalanine (FMLP) results in the activation of PLC β 2 and hydrolysis of phosphatidylinositol 4,5-bisphosphate, leading to the generation of inositol 1,4,5-triphosphate, a calcium m e s s e n g e r, and DG (Volp et al., 1983; Ohta et al., 1 9 8 5 ;Smith et al., 1986).Activation of the oxidase involves the translocation of a fraction (<10%) of p47-phox and p67-phox to the plasmalemma where the functional complex is assembled Nauseef et al., 1991;Tyagi et al., 1 9 9 2 ) . One route of stimulation that occurs with activators of PKC, such as PMA, involves multisite phosphorylation of p47-phox (Heyworth and Badwey, 1990). PKC can catalyze the phosphorylation of p47-phox in vitro ( K r a m e r et al., 1988;Pilloud-Dagher et al., 1992;Uhlinger and Perry, 1992b) and the predicted sequence of p47-phox contains several potential phosphorylation sites for this kinase (Lomax et al., 1989). It has been suggested that the NADPH-oxidase activity in neutrophils may be regulated by the phosphorylation/dephosphorylation state of p47-phox which is a func...

show abstract

Chemotactic factor causes rapid decreases in phosphatidylinositol,4,5-bisphosphate and phosphatidylinositol 4-monophosphate in rabbit neutrophils

Cited by 189 publications

References 6 publications

The Small GTP-binding Protein Rac Promotes the Dissociation of Gelsolin from Actin Filaments in Neutrophils

The Small GTP-binding Protein Rac Promotes the Dissociation of Gelsolin from Actin Filaments in Neutrophils

Human neutrophil cytosolic phospholipase C: partial characterization

Calyculin A modulates activation of the NADPH-oxidase in Me2SO-differentiated HL-60 cells

Contact Info

Product

Resources

About