Induction of prostacyclin receptor expression in human erythroleukemia cells

Murray, Rosemary; Furci, Lucinda; FitzGerald, Garret A.

doi:10.1016/0014-5793(89)81084-1

Cited by 16 publications

(9 citation statements)

References 13 publications

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“…Parallel but independently regulated increases cAMP and [Ca2+]i have been reported for prostaglandin receptors in human erythroleukaemia (HEL) cells and H2-receptors in HL-60 promyelocytes and rat hepatoma cells Murray et al 1989;DelValle et al 1992;Schwaner et al 1992). This is evidently not the consequence of AC-mediated increases in cAMP, as various cAMP-increasing substances acting at post-receptor sites failed to mimic the stimulatory effects of histamine on [Ca2+] i.…”

Section: Discussionmentioning

confidence: 92%

Stimulation of histamine H2- (and H1)-receptors activates Ca2+ influx in all-atrans-retinoic acid-differentiated HL-60 cells independently of phospholipase C or adenylyl cyclase

Burde

Seifert

1996

Naunyn-Schmiedeberg's Arch Pharmacol

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In human neutrophils, histamine H2-receptors mediate activation of adenylyl cyclase (AC) and inhibition of N-formyl-L-methionyl-L-leucyl-L-phenylalanine (FMLP)-induced superoxide anion (O2-) formation, and in HL-60 promyelocytes, H2-receptors mediate parallel activation of AC, phospholipase C (PLC) and non-selective cation (NSC) channels. As all-trans-retinoic acid (RA) is successfully used in the differentiation therapy of acute promyelocytic leukaemia, we studied signal transduction in RA-differentiated HL-60 cells. Histamine and the H2-receptor agonist, impromidine, induced both rises in cAMP levels and cytosolic Ca2+ ([Ca2+]i). Substances acting at post-receptor sites to increase cAMP did not increase [Ca2+]i. H2- but not H1-receptor antagonists inhibited histamine-induced cAMP accumulation and rises in [Ca2+]i were more effectively inhibited by H2- than by H1-receptor antagonists. Histamine-induced rises in [Ca2+]i were completely dependent on the presence of extracellular Ca2+ and were abolished by the blocker of NSC channels, Gd3+, but were resistant to inhibition by pertussis toxin. Unlike FMLP, histamine did not activate PLC. The effects of FMLP on [Ca2+]i were less sensitive to blockade by Gd3+ than those of histamine, and there was no cross-desensitization between the two stimuli. FMLP, but not histamine, inhibited transiently thapsigargin-induced rises in [Ca2+]. Taken together, our results show that histamine activates AC-mediated cAMP accumulation in RA-differentiated HL-60 cells via H2-receptors and NSC channel-mediated Ca2+ influx via H2- (and H1)-receptors. Histamine-induced NSC channel activation is not the consequence of AC- or PLC stimulation and occurs, directly or indirectly, via pertussis toxin-insensitive guanine nucleotide-binding proteins. FMLP and histamine activate Ca2+ influx by different mechanisms. There are similarities in H2-receptor-mediated signal transduction between RA-differentiated HL-60 cells and HL-60 promyelocytes and differences between the former cells and neutrophils, indicating that RA-differentiated HL-60 cells must be considered as partially immature.

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Section: Discussionmentioning

confidence: 92%

Stimulation of histamine H2- (and H1)-receptors activates Ca2+ influx in all-atrans-retinoic acid-differentiated HL-60 cells independently of phospholipase C or adenylyl cyclase

Burde

Seifert

1996

Naunyn-Schmiedeberg's Arch Pharmacol

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“…HEL cells are known to express a functional IP receptor (Murray et al, 1989). To analyze the binding of 3 Hlabeled iloprost to HEL membranes, a Scatchard analysis was performed (Fig.…”

Section: Resultsmentioning

confidence: 99%

A Prostacyclin Receptor Antagonist Inhibits the Sensitized Release of Substance P from Rat Sensory Neurons

Nakae

Saito²,

Iino³

et al. 2005

J Pharmacol Exp Ther

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Prostacyclin, one of the cyclooxygenase metabolites, causes various biological effects, including vasodilation and antithrombogenicity, and is also involved in several pathophysiological effects, such as inflammatory pain and bladder disorders. The prostacyclin receptor (IP receptor) agonists iloprost, cicaprost, and carbacyclin have been useful for clarifying the role of the IP receptor signaling, since the endogenous ligand, prostacyclin, is very unstable. On the other hand, only a few IP receptor antagonists have been reported to date. Here, we characterized the biological activities of 2-[4-(1H-indol-4-yloxymethyl)-benzyloxycarbonylamino]-3-phenyl-propionic acid (compound A) in various in vitro systems. Compound A inhibited the accumulation of the second messenger cyclic AMP in the UMR-108 rat osteosarcoma cell line and primary cultured rat dorsal root ganglion (DRG) neurons in a concentration-dependent manner up to 10 M, without affecting other eicosanoid receptors. Functionally, the IP receptor plays an important role in DRG neuron sensitization, which is measured by release of the neurotransmitter substance P. Although the effects of iloprost or Lys-bradykinin, an inflammatory peptide, alone on substance P release were limited, stimulation of the neurons with both these ligands induced substantial amounts of substance P release. This synergistic effect was suppressed by compound A. Collectively, these results suggest that compound A is a highly selective IP receptor antagonist that inhibits iloprost-induced sensitization of sensory neurons. Furthermore, these findings suggest that IP receptor antagonist administration may be effective for abnormal neural activities of unmyelinated sensory afferents. Compound A should prove useful for further investigations of the IP receptor in various biological processes.Prostanoids (PGD 2 , PGE 2 , PGF 2␣ , PGI 2 , and thromboxane A 2 ) are bioactive lipid mediators generated from membrane phospholipids. They are formed from unsaturated 20-carbon fatty acids and activate second messengers via specific G protein-coupled receptors (prostaglandin D 2 receptor, CRTH2, EP 1 , EP 2 , EP 3 , EP 4 , prostaglandin F receptor, IP, and TP) (Breyer et al., 2001;Samad et al., 2002).

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“…HEL cells are capable of spontaneous and induced globin synthesis [1]. Phorbol 12-myristate 13-acetate (PMA) and dimethyl sulphoxide induce additional macrophage-like and megakaryocytic properties in HEL cells [3][4][5][6][7][8]. These cells express various plasma membrane receptors, i.e.…”

Section: Introductionmentioning

confidence: 99%

“…These cells express various plasma membrane receptors, i.e. for a2-adrenergic agon-ists, neuropeptide Y, prostaglandin I2 (PGI2), thromboxane A2, thrombin, platelet-activating factor (PAF) and ADP [8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

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Receptor-mediated increases in cytosolic Ca2+ in the human erythroleukaemia cell line involve pertussis toxin-sensitive and -insensitive pathways

Schwaner

Seifert

Schultz

1992

Biochemical Journal

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The pluripotent human erythroleukaemia cell line, HEL, possesses erythrocytic, megakaryocytic and macrophage-like properties. With respect to signal transduction, HEL cells have been used as a model system for platelets, but little attention has been paid to their phagocytic properties. We studied the effects of various receptor agonists on the intracellular free Ca2+ concentration ([Ca2+]i) in HEL cells. Thrombin, platelet-activating factor (PAF), ATP, UTP, prostaglandins E1 and E2 (PGE1 and PGE2), the PGE2 analogue sulprostone and the stable PGI2 analogues iloprost and cicaprost increased [Ca2+]i. ADP was less effective than ATP, and UDP was unable to increase [Ca2+]i. The increases in [Ca2+]i induced by thrombin, PAF, ATP, UTP, iloprost and cicaprost were pertussis toxin-insensitive, whereas the increases induced by PGE2 and sulprostone were completely inhibited by the toxin. The increase in [Ca2+]i induced by PGE1 was partially inhibited by pertussis toxin. PGE2 did not desensitize the increase in [Ca2+]i induced by iloprost, and vice versa. PGE1 desensitized the response to PGE2 and iloprost but not vice versa. Adrenaline potentiated the iloprost- but not the PGE2-induced rise in [Ca2+]i. The phorbol ester phorbol 12-myristate 13-acetate completely blocked the rise in [Ca2+]i induced by ATP and PGE1, whereas the increases induced by thrombin and PAF were only partially inhibited. Agonists increased [Ca2+]i through release from internal stores and sustained Ca2+ influx. Thrombin stimulated Mn2+ influx, which was blocked by Ni2+. Diltiazem, isradipine, gramicidin and 1-(beta-[3-(4-methoxyphenyl)propoxy]-4-methoxyphenethyl)-1H-imidazole hydrochloride (SK&F 96365) did not affect agonist-induced rises in [Ca2+]i. HEL cells contained substantial amounts of beta-glucuronidase which, however, could not be released, and they did not aggregate or generate superoxide. Our data suggest that: (1) HEL cells possess nucleotide receptors with properties similar to those of phagocytes; (2) they possess receptors for PGE2 and PGI2, and PGE1 is an agonist at both receptors; (3) agonist-induced increases in [Ca2+]i are mediated through pertussis toxin-sensitive as well as -insensitive signal transduction pathways; and (4) agonists increase [Ca2+]i by mobilization from internal stores and influx from the extracellular space through cation channels with properties similar to those of phagocytes and platelets.

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Induction of prostacyclin receptor expression in human erythroleukemia cells

Cited by 16 publications

References 13 publications

Stimulation of histamine H2- (and H1)-receptors activates Ca2+ influx in all-atrans-retinoic acid-differentiated HL-60 cells independently of phospholipase C or adenylyl cyclase

Stimulation of histamine H2- (and H1)-receptors activates Ca2+ influx in all-atrans-retinoic acid-differentiated HL-60 cells independently of phospholipase C or adenylyl cyclase

A Prostacyclin Receptor Antagonist Inhibits the Sensitized Release of Substance P from Rat Sensory Neurons

Receptor-mediated increases in cytosolic Ca2+ in the human erythroleukaemia cell line involve pertussis toxin-sensitive and -insensitive pathways

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