Chemotactic Factor-Induced Release of Membrane Calcium in Rabbit Neutrophils

Naccache, P.H.; Volpi, M.; Showell, H J; Becker, E L; Sha'afi, R.I.

doi:10.1126/science.760200

Cited by 151 publications

(38 citation statements)

References 16 publications

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“…Under the conditions in Table III, BOC-Phe-Leu-Phe-LeuPhe alone did not affect PMN migration to zymosan-activated serum (see Table III), whereas the PMN chemotactic response to FMLP was significantly decreased (see Table III). The findings using BOC-Phe-Leu-Phe-Leu-Phe suggest that mitochondrial PMN chemoattractants interact with neutrophil N-formylmethionyl peptide receptors (2,17,30) and imply that the chemotactic activity of disrupted mitochondria and purified mitochondrial proteins is mediated, at least in part, through N-formylmethionine residues present in these proteins. * Concentrations: CYOX, 10 6 M; CYOX subunit I (CYOXI), 10-" M; CYOX subunit lI (CYOXn), 10 -~ M; activated (zymosan) human serum, 10% (vol/vol); FMLP, 10 -s M; HeLa WI-38, and foreskin fibroblast mitochondria, 100 ~g (protein).…”

Section: Inhibition Of Mitochondrial Chemotactic Activity By Boc-phe-mentioning

confidence: 99%

“…We further tested the notion that the PMN chemotactic activity of mitochondrially synthesized proteins is mediated through the presence of an N-formylmethionine residue by using the formyl peptide antagonist BOC-Phe-Leu-Phe-Leu-Phe (17,30). BOC-PheLeu-Phe-Leu-Phe is thought to inhibit the PMN response to N-formylmethionine containing peptides by competitively inhibiting the binding of these factors to specific cell surface receptors (2,17,30). As shown in Table III, when BOC-Phe-Leu-PheLeu-Phe was present in both compartments of the chemotaxis chamber, the PMN chemotactic response to purified mitochondrial proteins or disrupted mitochondria was significantly reduced.…”

Section: Inhibition Of Mitochondrial Chemotactic Activity By Boc-phe-mentioning

confidence: 99%

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Mitochondrial N-formylmethionyl proteins as chemoattractants for neutrophils.

Carp¹

1982

The Journal of Experimental Medicine

298

213

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Mitochondria synthesize several hydrophobic proteins. Like bacteria, mitochondria initiate protein synthesis with an N-formylmethionine residue. Because N-formylmethionyl peptides have been found to be chemotactic for polymorphonuclear leukocytes (PMN), mitochondria isolated from cultured human cells and purified bovine mitochondrial proteins were tested for PMN chemotactic activity in vitro. Nondisrupted mitochondria were not chemotactic. However, intact mitochondria that had been incubated with a lysosomal lysate did stimulate PMN migration. Antibodies directed against two mitochondrial enzymes, cytochrome oxidase and ATPase, (both of which contain mitochondrially synthesized subunits) but not anti-C3 or anti-C5 decreased mitochondrially derived chemotactic activity. In addition, purified bovine mitochondrial N-formylmethionyl proteins stimulated PMN migration in vitro, whereas nonformylated mitochondrial proteins did not. Furthermore, the chemotactic activity of purified mitochondrial proteins and disrupted mitochondria was decreased by the formyl peptide antagonist butyloxycarbonyl-phenylalanine-leucine-phenylalanine-leucine-phenylalanine. Finally, disrupted mitochondria and purified mitochondrial proteins stimulated PMN-directed migration (chemotaxis), according to accepted criteria. In addition to other chemotactic factors, release of N-formylmethionyl proteins from mitochondria at sites of tissue damage, may play a role in the accumulation of inflammatory cells at these sites.

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Section: Inhibition Of Mitochondrial Chemotactic Activity By Boc-phe-mentioning

confidence: 99%

Section: Inhibition Of Mitochondrial Chemotactic Activity By Boc-phe-mentioning

confidence: 99%

Mitochondrial N-formylmethionyl proteins as chemoattractants for neutrophils.

Carp¹

1982

The Journal of Experimental Medicine

298

213

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“…In stimulated cells, there was less extramitochondrial fluorescence. Naccache et al (45) have recently reported that chemotactic factors induce release of membrane calcium in rabbit neutrophils; these authors also used the fluorescence of CTC-treated cell suspensions to measure membrane-bound calcium, and Taljedal (64) described methodology for microfluorimetric measurement of CTC. Since the fluorescence signal of interest, when CTC is used as a probe, comes entirely from the cells, one would expect that this procedure could be adapted almost unchanged for flow cytometry.…”

Section: Tetracyclines As Probes For Membrane-bound Calciummentioning

confidence: 99%

Flow cytometric probes of early events in cell activation

Shapiro

1981

Cytometry

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By now, it's well established that the surface of a cell Contains transmembrane proteins which, on binding ligands, tell The biochemical computer inside what to do Without a need for any of the ligands coming through. Receptor‐triggered cytoplasmic “interrupt routines” May lead the nucleus to activate new sets of genes, Or otherwise induce a cell, which never reasons why, To twitch, secrete, endocytose, or reproduce, or die. By merely watching labeled ligands bind, we cannot know Down which of many paths the cells thus tagged are apt to go, But other changes, shortly after binding, may predict Which of its several options any given cell has picked. Flow cytometric methods are described here which allow Membrane potential to be estimated, to show how Potential changes may occur in seconds after binding Of ligand to a functional receptor, or for finding No change when cells don't have the right receptor, or can't see The ligand for antagonists of like affinity. With chlorotetracycline fluorescence, one can find Release of membrane calcium soon after ligands bind; Both this and the potential measurement can help support Decisions in an instrument about which cells to sort, Though narrowing the distributions which these methods yield Would greatly help to broaden applications in this field.

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“…fMLP, PAF and C5a (Naccache et al, 1979;Clancy et al, 1983;Naccache et al, 1986). These compounds bind to specific cell-surface receptors to stimulate the phospholipase C-dependent release of diacylglycerol and inositol trisphosphate, a process mediated by pertussis toxinsensitive, guanine nucleotide-binding proteins (G proteins) (Becker et al, 1985;Naccache et al, 1986;Shirato et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Activation of the human neutrophil 5‐lipoxygenase by leukotriene B₄

McDonald

McColl

Naccache

et al. 1992

British J Pharmacology

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1 In the present study, we demonstrate that leukotriene B4 (LTB4) has the ability to activate the human neutrophil 5-lipoxygenase (5-LO). 2 Stimulation of neutrophils with 30 nM 14,15-dideuterio-LTB4 (D2-LTB4) failed to induce the synthesis of LTB4 from endogenous arachidonic acid (AA), but stimulated the formation of LTB4 from 3.31gM exogenous AA, as determined by GC-MS analysis.3 The stimulatory effect of LTB4 on 5-LO activity was further examined with an alternative substrate; LTB4 time-and dose-dependently stimulated the 5-LO-mediated conversion of exogenous 15(S)-hydroperoxy-5,8, 11,1 3-(Z,Z,Z,E)-eicosatetraenoate (1 5-HpETE) into 5(S),15(S)-dihydroxy-6,8,1 1,13,-(E,Z,Z,E)-eicosatetraenoate (5,15-DiHETE), with a threshold effect at 300pM. 4 The ability of LTB4 to activate the 5-LO showed structural specificity, since LTB4 was found to be 100 times more potent than c-hydroxy-LTB4, and 300 times more potent than its A6-trans-12-epi-isomer.5 The LTB4-induced 5-LO activation was effectively inhibited by MK-886 (an inhibitor of 5-LO translocation), by pertussis toxin, and by the LTB4 receptor antagonist, LY-223982. 6 These results demonstrate that the binding of LTB4 to its cell-surface receptor results in 5-LO activation in a process mediated by pertussis toxin-sensitive guanine nucleotide-binding proteins. Our data also suggest that the underlying mechanism involves a translocation of the 5-LO to the membrane. These findings raise the possibility that LTB4 produced by phagocytes may positively feedback on its own synthesis.

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Chemotactic Factor-Induced Release of Membrane Calcium in Rabbit Neutrophils

Cited by 151 publications

References 16 publications

Mitochondrial N-formylmethionyl proteins as chemoattractants for neutrophils.

Mitochondrial N-formylmethionyl proteins as chemoattractants for neutrophils.

Flow cytometric probes of early events in cell activation

Activation of the human neutrophil 5‐lipoxygenase by leukotriene B₄

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Chemotactic Factor-Induced Release of Membrane Calcium in Rabbit Neutrophils

Cited by 151 publications

References 16 publications

Mitochondrial N-formylmethionyl proteins as chemoattractants for neutrophils.

Mitochondrial N-formylmethionyl proteins as chemoattractants for neutrophils.

Flow cytometric probes of early events in cell activation

Activation of the human neutrophil 5‐lipoxygenase by leukotriene B4

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Activation of the human neutrophil 5‐lipoxygenase by leukotriene B₄