Nucleotide-, Chemotactic Peptide- and Phorbol Ester-Induced Exocytosis in HL-60 Leukemic Cells

Wenzel-Seifert, Katharina; Seifert, Roland

doi:10.1016/s0171-2985(11)80499-7

Cited by 23 publications

(37 citation statements)

References 47 publications

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“…This transient increase in intracellular free calcium correlates with acidification and stimulation of superoxide (O 2− ) release. The level of free fMLF required for half-maximal effect on Ca 2+ release has been reported to be 2-4 nM (Wenzel-Seifert and Seifert, 1990), in approximate agreement with our determination of 5 nM, while the EC 50 for superoxide production has been reported to be 15-30 nM fMLF (Klinker et al, 1996). In this study all conjugates with four or more copies of fMLF and free fMLF displayed an EC 50 value of about 5 nM for calcium release (Table 1 and Figure 4).…”

Section: Discussionmentioning

confidence: 99%

Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

et al. 2002

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N -Formyl-methionyl peptides can specifically bind to surface receptors on phagocytic cells. A single copy of N-formyl-methionine-leucine-phenylalanine (fMLF) covalently linked to a poly(ethylene glycol)-based polymer displayed reduced binding avidity (K d = 190 nM) for differentiated HL-60 cells relative to free fMLF (K d = 28 nM). Increasing the number of fMLF residues (up to eight) attached to a single polymer results in enhanced avidity for these cells (K d = 0.18 nM), which appears to be independent of whether the polymer backbone is linear or branched. However, no conjugate showed enhanced ability to activate phagocytic cells, relative to the free peptide (EC 50 = 5 nM), as measured by transient stimulation of release of calcium ions from intracellular stores into the cytoplasm. A polymer bearing four fMLF and four digoxigenin residues showed specific enhancement in binding to differentiated HL-60 cells and mouse peritoneal macrophages in situ relative to a polymer lacking fMLF; no such enhancement was seen in binding to receptor-negative lymphocytic Jurkat cells. These results suggest that multiple fMLF residues linked to a drug-delivery polymer can be used to target appended drugs to phagocytic cells with relatively little toxicity due to cellular activation.

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Section: Discussionmentioning

confidence: 99%

Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

et al. 2002

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“…Measurement of Enzyme Release-Release of ␤-glucuronidase and N-acetyl-␤-glucosaminidase enzymes from HL-60 cells was assessed as described (21). Briefly, differentiated HL-60 cells (3.5-5 ϫ 10 6 cells) were suspended in 500 l of Hanks' balanced salt solution and incubated for 5 min at 37°C in the presence of cytochalasin B (5 g/ml).…”

Section: Myo-[2-mentioning

confidence: 99%

Formyl Peptide Receptor Signaling in HL-60 Cells through Sphingosine Kinase

Alemany

Heringdorf

Koppen

et al. 1999

Journal of Biological Chemistry

100

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Sphingosine-1-phosphate (SPP) produced from sphingosine by sphingosine kinase has recently been reported to act as intracellular second messenger for a number of plasma membrane receptors. In the present study, we investigated whether the sphingosine kinase/SPP pathway is involved in cellular signaling of the G i proteincoupled formyl peptide receptor in myeloid differentiated human leukemia (HL-60) cells. Receptor activation resulted in rapid and transient production of SPP by sphingosine kinase, which was abolished after pertussis toxin treatment. Direct activation of heterotrimeric G proteins by AlF 4 Ϫ also rapidly increased SPP formation in intact HL-60 cells. In cytosolic preparations of HL-60 cells, sphingosine kinase activity was stimulated by the stable GTP analog, guanosine 5-O-(3-thiotriphosphate). Inhibition of sphingosine kinase by DL-threo-dihydrosphingosine and N,N-dimethylsphingosine did not affect phospholipase C stimulation and superoxide production but markedly inhibited receptor-stimulated Ca 2؉ mobilization and enzyme release. We conclude that the formyl peptide receptor stimulates through G i -type G proteins SPP production by sphingosine kinase, that the enzyme is also stimulated by direct G protein activation, and that the sphingosine kinase/SPP pathway apparently plays an important role in chemoattractant signaling in myeloid differentiated HL-60 cells.During the last few years, it has become clear that sphingolipids, in addition to being structural constituents of cell membranes, are sources of important signaling molecules. Particularly, the sphingolipid metabolites, ceramide and sphingosine-1-phosphate (SPP), 1 have emerged as a new class of potent bioactive molecules, implicated in a variety of cellular processes such as cell differentiation, apoptosis, and proliferation (1-4). Interest in SPP focused recently on two distinct cellular actions of this lipid, namely its function as extracellular ligand activating specific G protein-coupled membrane receptors and its role as intracellular second messenger (5). Important clues to a specific intracellular action of SPP were the following findings. First, activation of various plasma membrane receptors, such as the platelet-derived growth factor receptor (6, 7), the Fc⑀RI (8), and the Fc␥RI antigen receptors (9), was found to rapidly increase intracellular SPP production through stimulation of sphingosine kinase. Second, inhibition of sphingosine kinase stimulation strongly reduced or even prevented cellular events triggered by these tyrosine kinase-linked receptors, such as receptor-stimulated DNA synthesis, Ca 2ϩ mobilization, and vesicular trafficking (6,8,9). Finally, intracellular SPP was found to mimic the receptor responses, i.e. it stimulated DNA synthesis and mobilized Ca 2ϩ from internal stores (10 -14). We recently reported that the G protein-coupled muscarinic acetylcholine receptor subtypes m2 and m3 expressed in HEK-293 cells also induce a rapid and transient SPP production by sphingosine kinase. Furthermore, intracellular in...

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“…Stock solutions of 12-AS (1 raM) were prepared in 80% ethanol (v/v) and were kept at -20°C. Sources of other materials have been described elsewhere (Seifert et al 1989a(Seifert et al , b, 1992Wenzel-Seifert and Seifert 1990;Wenzel-Seifert et al 1991).…”

Section: Materials Fk-506 Was Kindly Provided By Fujisawa Pharmaceutmentioning

confidence: 99%

“…Exocytosis was assessed as described (Seifert et al 1989b;Wenzel-Seifert and Seifert 1990;Wenzel-Seifert et al 1991). In one set of experiments, neutrophils (4.0-5.0x106 cells) were incubated for 5min at 37°C in the buffer (0.5 ml) described above supplemented with cytochaiasin B (5 gg/ml) in the presence of FK-506 or solvent.…”

Section: Materials Fk-506 Was Kindly Provided By Fujisawa Pharmaceutmentioning

confidence: 99%

“…Reaction mixtures were centrifuged for 10min at 1000xg. The determinations of the activities of flglucuronidase, lysozyme and lactate dehydrogenase of the supernatant fluids of reaction mixtures and of cell lysates were performed as described (Seifert et al 1989b;Wenzel-Seifert and Seifert 1990;WenzelSeifert et al 1991). Basal fl-glucuronidase, lysozyme and lactate dehydrogenase release amounted to less than 5°70 of cellular content (data not shown).…”

Section: Materials Fk-506 Was Kindly Provided By Fujisawa Pharmaceutmentioning

confidence: 99%

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Partial inhibition of human neutrophil activation by FK-506 at supratherapeutic concentrations

Wenzel-Seifert

Seifert

1993

Naunyn-Schmiedeberg's Arch Pharmacol

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Summary. The macrolide, FK-506, is a potent and effective inhibitor of lymphocyte activation. We studied the effects of FK-506 on human neutrophil activation induced by chemoattractants and by various substances which circumvent receptor stimulation. After preincubation for 5 min at 37 °C, FK-506(fMet-LeuPhe)-or platelet-activating factor-induced superoxide production in neutrophils by about 30°7o. At therapeutic concentrations (0.1-1nM) FK-506 was ineffective. FK-506 did not inhibit exocytosis and rises in cytosolic Ca 2÷ concentration [Ca2+] i mediated by these stimuli, and it did not at all inhibit neutrophil activation induced by C5a, leukotriene B 4 and 4fl-phorbol 12-myristate 13-acetate. FK-506 (1 gM) inhibited A23187-induced exocytosis by about 35%, but A23187-induced superoxide production was unaffected. After preincubation for 5 min at 37 °C, FK-506 inhibited fMet-Leu-Phe-induced superoxide production in dibutyryl cAMP-differentiated HL-60 cells by about 20%; preincubation with the drug for 24 h did not result in inhibition of superoxide production. FK-506 did not inhibit agonist-binding to formyl peptide receptors and fMet-Leu-Phe-stimulated GTP hydrolysis of heterotrimeric regulatory guanine nucleotidebinding proteins (G-proteins) in membranes from dibutyryl cAMP-differentiated HL-60 cells. FK-506 did not change steady-state and differential polarized phase fluorescence in Hb60 membranes using 1,6-diphenylhexa-1,3,5-triene and 12-(9-anthroyloxy)-stearate as probes. Our results show that FK-506 at supratherapeutic concentrations partially inhibits neutrophil activation. Inhibition by FK-506 of fMet-Leu-Phe-induced superoxide production is rapid in onset and is not due to inhibition of agonist-binding to receptors, interference with G-proteins or protein kinase C, reduction of rises in [Ca2+]i or alteration in physical membrane state.

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Nucleotide-, Chemotactic Peptide- and Phorbol Ester-Induced Exocytosis in HL-60 Leukemic Cells

Cited by 23 publications

References 47 publications

Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

Formyl Peptide Receptor Signaling in HL-60 Cells through Sphingosine Kinase

Partial inhibition of human neutrophil activation by FK-506 at supratherapeutic concentrations

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