Modulation of human neutrophil chemotactic responses by cyclic 3′,5′-guanosine monophosphate and cyclic 3′,5′-adenosine monophosphate

Hill, Harry R.; Estensen, Richard D.; Quie, Paul G.; Hogan, Nancy A.; Goldberg, Nelson D.

doi:10.1016/0026-0495(75)90124-9

Cited by 163 publications

(46 citation statements)

References 8 publications

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“…PGE 2 can modulate the migration of other cell types as well as fibroblasts (35,36,37,38,39,40). The PGE 2 inhibition of neutrophil (36,37), lymphocyte (38,39), and eosinophil (18,40) chemotaxis was reported. In contrast, PGE 2 was reported to stimulate airway epithelial cell migration (41).…”

Section: Discussionmentioning

confidence: 98%

Prostaglandin E₂Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors

Li¹,

Wang²,

Satô³

et al. 2011

Am J Respir Cell Mol Biol

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The migration of fibroblasts is believed to play a key role in both normal wound repair and abnormal tissue remodeling. Prostaglandin E (PGE) 2 , a mediator that can inhibit many fibroblast functions including chemotaxis, was reported to be mediated by the E-prostanoid (EP) receptor EP2. PGE 2 , however, can act on four receptors. This study was designed to determine if EP receptors, in addition to EP2, can modulate fibroblast chemotaxis. Using human fetal lung fibroblasts, the expression of all four EP receptors was demonstrated by Western blotting. EP2-selective and EP4-selective agonists inhibited both chemotaxis toward fibronectin in the blindwell assay and migration in a wound-closure assay. In contrast, EP1-selective and EP3-selective agonists stimulated cell migration in both assay systems. These results were confirmed using EP-selective antagonists. The role of both EP2 and EP4 receptors in mediating the PGE 2 inhibition of chemotaxis was also confirmed by small interfering RNA suppression. Furthermore, the role of EP receptors was confirmed by blocking the expected signaling pathways. Taken together, these results demonstrate that PGE 2 can act on multiple EP receptors in human lung fibroblasts, to exert disparate effects. Alterations in EP receptor expression may have the potential to alter PGE 2 action. Targeting specific EP receptors may offer therapeutic opportunities in conditions characterized by abnormal tissue repair and remodeling.

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Section: Discussionmentioning

confidence: 98%

Prostaglandin E₂Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors

Li¹,

Wang²,

Satô³

et al. 2011

Am J Respir Cell Mol Biol

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“…Thus, the results suggest that a G protein distinct from Gs and transducin, most likely the 40 kDa substrate, gives rise to the cholera toxin-sensitive GTPase activity in response to FMLP. There is the distinct possibility that the cholera toxin-dependent ADP-ribosylation of the G protein coupled to the formyl peptide receptor also inhibits the stimulation of FMLP-dependent effector enzymes, including phospholipase C. Inhibition of several neutrophil functions has been noticed by several investigators [20][21][22][23][24]. Specifically, the inhibition of macrophage chemotaxis by cholera toxin has been reported to be independent of a toxin-dependent increase in cellular cAMP [11].…”

Section: Gtp[s]mentioning

confidence: 99%

Receptor‐mediated ADP‐ribosylation of a phospholipase C‐stimulating G protein

1987

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In membranes of myeloid differentiated HL 60 cells, the chemotactic peptide FMLP stimulates phospholipase C via a pertussis toxin-sensitive G protein. FMLP markedly stimulates the cholera toxin-dependent ADP-ribosylation of a 40 kDa protein in these membranes. This effect of FMLP is inhibited by GTP and GTP [S], and is almost completely abolished in membranes of pertussis toxin-pretreated HL 60 cells. Treatment of HL 60 membranes with cholera toxin and NAD markedly inhibits FMLP-stimulated high affinity GTPase. These results suggest that a 40 kDa G protein sensitive to both pertussis and cholera toxin functionally interacts with the formyl peptide receptor of HL 60 cells and, thus, very likely is the G protein that stimulates phospholipase C in this system.

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“…

ABSTRACT Addition of arachidonic acid and the divalent cation ionophore A23187 to a suspension of human peripheral blood polymorphonuclear leukocytes led to the formation of 8,11,8,11, and (5S,8,10, A method based on high-pressure liquid chromatography has been developed for assay of these metabolites. The addition of arachidonic acid to human polyinorphonuclear leukocytes always resulted in formation of the isomeric monohydroxy acids.

…”

mentioning

confidence: 99%

Arachidonic acid metabolism in polymorphonuclear leukocytes

Borgeat

Samuelsson

1979

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

697

235

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Addition of arachidonic acid and the divalent cation ionophore A23187 to a suspension of human peripheral blood polymorphonuclear leukocytes led to the formation of 8,11,8,11, and (5S,8,10, A method based on high-pressure liquid chromatography has been developed for assay of these metabolites. The addition of arachidonic acid to human polyinorphonuclear leukocytes always resulted in formation of the isomeric monohydroxy acids. However, cells prepared from blood of different subjects were found to vary with respect to formation of the 5,12-dihydroxy acid. Addition of the ionophore alone strongly stimulated the formation of the 5-monohydroxy acid and more specifically the 5,12-dihydroxy acid from endogenous arachidonic acid. In all experiments performed the formation of the 5-hydroxy acid and the 5,12-dihydroxy acid was maximally stimulated when both arachidonic acid and the ionophore were added to the incubation mixture. Under these conditions, stimulation of 40-fold or more of the formation of both compounds was observed. The data demonstrate that, in addition to causing release of endogenous substrate, the ionophore also activated the enzymatic system involved in the further transformations of arachidonic acid. This finding raises the possibility that this pathway of arachidonic acid metabolism is involved in the biological response (e.g., release of lysosomal enzymes, the slow reacting substance of anaphylaxis, and chemotactic factors) of leukocytes to A23187 and other stimuli.Recent studies have indicated that polyunsaturated fatty acids and their metabolites are involved in the functions of leukocytes (1, 2). It was thus reported that two hydroxy acids formed from arachidonic acid-namely, 12-hydroxy-5,8,10,14-icosatetraenoic acid and 12-hydroxy-5,8,10-heptadecatrienoic acid-induced chemotaxis by polymorphonuclear leukocytes (PMNL) (3-5). It was also recently shown that unsaturated fatty acid peroxides, such as arachidonic acid peroxides, stimulate platelet guanyl cyclase activity (6, 7). This last finding might be particularly significant in view of the effects of 3',5'-guanosine monophosphate on lysosomal enzyme release (8, 9) and leukocyte locomotion (10-12). Several studies have also demonstrated a stimulatory effect of ionophore A23187 on the formation of thromboxane B2 (13, 14) and prostaglandins (13)(14)(15) in leukocytes. It is of interest in this context that ionophore A23187 has also been found to stimulate some phagocytosis-associated responses of leukocytes-i.e., oxidative metabolism (16, 17), chemiluminescence (14), and secretion of lysosomal enzymes (18, 19).We have recently demonstrated the formation of two metabolites of arachidonic acid in rabbit peritoneal PMNLnamely, (SS)-hydroxy-6,8,11,14-icosatetraenoic acid (20) and (5S. 12R)-dihydroxy-6,8,10,14-icosatetraenoic acid (21). It was therefore of interest to extend our studies to the metabolism of arachidonic acid in human PMNL. In addition, the effect of ionophore A23187 on the formation of the metabolites has been studied. Our find...

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Modulation of human neutrophil chemotactic responses by cyclic 3′,5′-guanosine monophosphate and cyclic 3′,5′-adenosine monophosphate

Cited by 163 publications

References 8 publications

Prostaglandin E₂Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors

Prostaglandin E₂Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors

Receptor‐mediated ADP‐ribosylation of a phospholipase C‐stimulating G protein

Arachidonic acid metabolism in polymorphonuclear leukocytes

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Modulation of human neutrophil chemotactic responses by cyclic 3′,5′-guanosine monophosphate and cyclic 3′,5′-adenosine monophosphate

Cited by 163 publications

References 8 publications

Prostaglandin E2Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors

Prostaglandin E2Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors

Receptor‐mediated ADP‐ribosylation of a phospholipase C‐stimulating G protein

Arachidonic acid metabolism in polymorphonuclear leukocytes

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Product

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Prostaglandin E₂Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors

Prostaglandin E₂Inhibits Human Lung Fibroblast Chemotaxis through Disparate Actions on Different E-Prostanoid Receptors