Ecto‐enzymes and metabolism of extracellular ATP

Зиганшин, А. У.; Hoyle, Charles H.V.; Burnstock, Geoffrey

doi:10.1002/ddr.430320303

Cited by 99 publications

(62 citation statements)

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“…Ecto-nucleotidases metabolize ATP to adenosine (16,25). Adenosine combines with A2 receptors that are linked to Gs protein (26) and may cross-talk with Gs proteincoupled ACTH receptor.…”

Section: Discussionmentioning

confidence: 99%

Extracellular ATP Potentiates Steroidogenic Effect of Adrenocorticotropic Hormone in Bovine Adrenocortical Fasciculata Cells

Kawamura

Niitsu

Nishi

et al. 2001

Japanese Journal of Pharmacology

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ABSTRACT-We examined the effect of extracellular adenosine 5'-triphosphate (ATP) on adrenocorticotropic hormone (ACTH)-and angiotensin II-induced steroidogenesis in bovine adrenocortical fasciculata cells. The low concentration of ATP (5 mM) potentiated ACTH-induced steroidogenesis synergistically. However, the purine derivative did not affect angiotensin II-induced steroidogenesis. Although adenosine (100 mM) (a metabolite of ATP) showed a weak steroidogenic effect, it did not potentiate ACTH-induced steroidogenesis. ATP also enhanced the steroidogenesis by NaF synergistically in bovine adrenocortical cells, but did not potentiate forskolin-and dibutyryl cyclic AMP-induced steroidogenesis. The stimulating effect of ACTH on cyclic AMP production was synergistically accelerated by ATP (5 mM), which has no effect by itself on cyclic AMP formation. These results suggest that extracellular ATP affected the ACTH receptor-adenylyl cyclase coupling processes, and potentiation of steroidogenesis by ACTH ensued in bovine adrenocortical fasciculata cells.Keywords: Adrenal cortex, Adrenocorticotropic hormone, Steroidogenesis, ATP, P2Y receptor Extracellular adenosine 5'-triphosphate (ATP) plays many biological roles in diverse cell functions via its cell membrane receptors (1 -4). Receptors for ATP are classified into two groups: a ligand-gated ion channel P2X receptor family and a G protein-coupled P2Y receptor family (5). We previously reported that extracellular ATP stimulated glucocorticoid production (steroidogenesis) in bovine adrenocortical fasciculata cells (BAFC) via P2Y receptors at micromolar concentrations (6).Recently, the importance of cross-talk between two biological active substances on the functions in several kinds of cells and organs has been mentioned. In the case of extracellular ATP, the nucleotide potentiates the insulin secretion stimulated by acetylcholine in isolated perfused rat pancreas (7), and the cytosolic Ca 2+ response to parathyroid hormone in rat osteoblastic cells (8). In steroidogenic organs, the cross-talk between serotonin and angiotensin II (9), interleukin-6 and adrenocorticotropic hormone (ACTH) (10) in rat adrenal steroidogenesis and angiotensin II and ACTH on cyclic AMP formation in bovine adrenal glomerulosa cells (11, 12) had been reported. From these observations, there might be possible cross-talk between extracellular ATP and ACTH (and/ or another steroidogenic substances) on glucocorticoid production in BAFC. Therefore, we investigated the effect of ATP on ACTH-and angiotensin II-induced steroidogenesis in BAFC. MATERIALS AND METHODS Primary culture of BAFCIsolated bovine adrenocortical fasciculata cells were prepared aseptically using collagenase and deoxyribonuclease I as previously described (13). The isolated cells were cultured in Ham's F-10 medium supplemented with 5% fetal calf serum, 10% newborn calf serum, 2.5% horse serum and antibiotics in a 24-well-type dish (10 -15 10 5 cells / well) in a CO2 incubator (humidified atmosphere of 5% CO 2 in air) at 37°C as repor...

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“…Ecto-nucleotidases metabolize ATP to adenosine (16,25). Adenosine combines with A2 receptors that are linked to Gs protein (26) and may cross-talk with Gs proteincoupled ACTH receptor.…”

Section: Discussionmentioning

confidence: 99%

Extracellular ATP Potentiates Steroidogenic Effect of Adrenocorticotropic Hormone in Bovine Adrenocortical Fasciculata Cells

Kawamura

Niitsu

Nishi

et al. 2001

Japanese Journal of Pharmacology

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“…3,13,14) Meanwhile, Ado released from cells including normal cells, necrotic cells, or apoptotic cells might act not only as an intercellular signaling molecule in paracrine/autocrine fashion but also as a substrate for the salvage pathway of intracellular adenine nucleotides. Our results demonstrated for the first time that the enhancement of cellular ATP levels by extracellular Ado is mediated by the salvage pathway of adenine nucleotides but not by the P1 receptor-mediated signaling pathway in PC12 cells.…”

Section: Metabolism Of Extracellular Ado and Atp By Pc12mentioning

confidence: 99%

“…3,13,14) Extracellular ATP was rapidly degraded to adenosine 5Ј-monophosphate (AMP) by PC12 cells, but the formation of Ado from AMP was slow, 4,15) despite having ecto-5Ј-nucleotidase, which catalyzes the conversion of AMP to Ado.…”

mentioning

confidence: 99%

Enhancement of Cellular Adenosine Triphosphate Levels in PC12 Cells by Extracellular Adenosine.

Fujimori

Yasuda

Pan-Hou

2002

Biological & Pharmaceutical Bulletin

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Extracellular adenosine (Ado), a metabolite of adenosine triphosphate (ATP), has been shown to function as an intercellular signaling molecule by interacting with specific P1 receptors.1,2) Extracellular ATP released from nerve cells, endothelial cells, chromaffin cells, or platelets can act as a transmitter or modulator via P2 receptors. 1,3) A number of cellular responses induced by Ado [4][5][6] and ATP [7][8][9][10][11] in rat pheochromocytoma PC12 cells, a neuronal model, have been demonstrated to be mediated mainly through P1 and P2 receptors. PC12 cells are known to have A2a and A2b but not A1 or A3 receptors among the P1 receptor subtypes, and P2X 2 , P2Y 1 , and P2Y 2 among the P2 receptor subtypes.2)The common responses induced by Ado and ATP in PC12 cells are to increase the cellular levels of cAMP and the activity of cAMP-regulated tyrosine hydroxylase, a rate-limiting enzyme of catecholamine biosynthesis. 4,12) It is of interest to determine whether cellular levels of ATP in PC12 cells would be affected by the addition of Ado, ATP, and related compounds.In general, extracellular ATP is known to be metabolized rapidly to Ado, and then converted to inosine and other metabolites by ecto-enyzmes on cell surfaces or soluble enzymes in extracellular fluids. 3,13,14) Extracellular ATP was rapidly degraded to adenosine 5Ј-monophosphate (AMP) by PC12 cells, but the formation of Ado from AMP was slow, 4,15) despite having ecto-5Ј-nucleotidase, which catalyzes the conversion of AMP to Ado.16) It is of interest to examine whether PC12 cells have the ability to metabolize Ado, and to know whether extracellular Ado influences the cellular contents of adenine compounds, especially ATP.In this investigation, we examined the effects of Ado and adenine nucleotides on cellular levels of adenine compounds, especially ATP, in PC12 cells. We showed that extracellular Ado enhanced the cellular ATP level, probably via the salvage pathway of adenine nucleotides, but not P1 and P2 receptors of Ado and ATP, respectively. MATERIALS AND METHODSMaterials Ado, AMP, adenosine 5Ј-diphosphate (ADP), and ATP were purchased from Yamasa Shouyu (Japan). 2-Chloro-N 6 -cyclopentyladenosine (CCPA), N 6 -cyclohexyladenosine (CHA), 5Ј-N-ethylcarboxaminoadenosine (NECA), dipyridamole, and reactive blue 2 were obtained from Sigma Chemical (U.S.A.). 2[p-(2-Carboxyethyl)phenethylamino]-5Ј-N-ethylcarboxamidoadenosine (CGS 21680) and coformycin were from Funakoshi Chemical (Japan) and Nakarai Tesque (Japan), respectively. Theophylline and chloroacetaldehyde were from Wako Chemicals (Japan). Fetal calf serum and inactivated horse serum were from IS Japan (Japan) and Gibco BRL (U.S.A.), respectively. Other chemicals of reagent grade were commercially obtained.Cell Culture Rat pheochromocytoma PC12 cells were kindly supplied by Professor K. Miura (Wako University, Tokyo, Japan). Cells were grown at 37°C in Dulbecco's modified Eagle's medium supplemented with 10% fetal calf serum, 5% heat-inactivated horse serum, glutamine 30 mg/ ml, and kanamycin 60 ...

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“…Ecto-ATPases have been purified from a range of tissues (see Ziganshin et at., 1994) and in some cases cDNA sequences isolated. The ecto-ATPases were found to be identical to previously identified cell adhesion molecules (Lin & Guidotti, 1989;Culic et al, 1992;Dzhandzhugazyan & Bock, 1993;Edlund et al, 1993;McCuaig et al, 1993;Najjar et al, 1993).…”

Section: Concentration-effect Relationship For Arl 67156mentioning

confidence: 99%

Enhancement of sympathetic purinergic neurotransmission in the guinea‐pig isolated vas deferens by the novel ecto‐ATPase inhibitor ARL 67156

Westfall

Kennedy

Sneddon

1996

British J Pharmacology

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1 Field stimulation of the sympathetic nerves of the guinea-pig isolated vas deferens with trains of pulses for 20 s at 1-8 Hz produced characteristic biphasic contractions. The effect of the novel ectoATPase inhibitor, 6-N,N-diethyl-D-13,y-dibromomethyleneATP (ARL 67156, formerly known as FPL 67156), on the magnitude of the initial, predominantly purinergic peak of this response was studied in order to determine the influence of enzymatic degradation of adenosine 5'-triphosphate (ATP) on its action as a neurotransmitter. 2 The peak magnitude of the response to nerve stimulation was significantly increased in a concentration-dependent manner by ARL 67156 (5-100 rM) and the size of the neurogenic response at 4 Hz was approximately doubled in the presence of ARL 67156 (100 gM). 3 ARL 67156 (100 gM) has a rapid onset of action. The enhancing effect on neurogenic contractions was maximal after 10 min, was well maintained for at least 30 min and was rapidly reversed, with responses returning to control levels 10 min after washout.4 The neurogenic contraction in the presence of prazosin (0.1 gM) was purely purinergic, as it was abolished by the P2-purinoceptor antagonist, PPADS (100 /M). ARL 67156 (100 /M) produced a similar degree of enhancement of neurogenic responses in the absence and presence of prazosin, supporting the view that the enhancing effects of ARL 67156 on neurogenic contractions result from potentiation of the action of ATP.5 Exogenous ATP and a,,B-methyleneATP produced rapid transient contractions. Responses to ATP were increased in magnitude and duration in the presence of ARL 67156 (100 gM), whereas those to the stable analogue, cx,fl-methyleneATP were not significantly affected.6 Contractions to exogenous noradrenaline (10 gM) and KCl (40 mM) were significantly enhanced by ARL 67156 (100 gM), but this potentiation was abolished by PPADS (100 pM). Therefore, this effect of the ecto-ATPase inhibitor may be due to a build up of endogenous ATP, increasing the sensitivity of the smooth muscle to other agonists. 7 It is concluded that ARL 67156 potentiates the action of ATP, and that when ATP acts as a neurotransmitter its postjunctional actions are greatly attenuated by enzymatic degradation.

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Ecto‐enzymes and metabolism of extracellular ATP

Cited by 99 publications

References 151 publications

Extracellular ATP Potentiates Steroidogenic Effect of Adrenocorticotropic Hormone in Bovine Adrenocortical Fasciculata Cells

Extracellular ATP Potentiates Steroidogenic Effect of Adrenocorticotropic Hormone in Bovine Adrenocortical Fasciculata Cells

Enhancement of Cellular Adenosine Triphosphate Levels in PC12 Cells by Extracellular Adenosine.

Enhancement of sympathetic purinergic neurotransmission in the guinea‐pig isolated vas deferens by the novel ecto‐ATPase inhibitor ARL 67156

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