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Volumn 1373, Issue 1, 1998, Pages 227-236

Steady-state binding of [3H]ATP to rat liver plasma membranes and competition by various purinergic agonists and antagonists

Author keywords

ATP binding; Liver plasma membrane; P2Y purinoceptor; Rat

Indexed keywords

ADENOSINE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CYTIDINE TRIPHOSPHATE; EDETIC ACID; GUANOSINE TRIPHOSPHATE; NUCLEOSIDE TRIPHOSPHATE; NUCLEOTIDE; PURINE P2 RECEPTOR; PURINERGIC RECEPTOR BLOCKING AGENT; PURINERGIC RECEPTOR STIMULATING AGENT; URIDINE TRIPHOSPHATE;

EID: 0032516730     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(98)00108-4     Document Type: Article
Times cited : (11)

References (40)
  • 3
    • 0030669521 scopus 로고    scopus 로고
    • The past, present and future of purine nucleotides as signalling molecules
    • G. Burnstock, The past, present and future of purine nucleotides as signalling molecules, Neuropharmacology 36 (1997) 1127-1139.
    • (1997) Neuropharmacology , vol.36 , pp. 1127-1139
    • Burnstock, G.1
  • 4
    • 0000179693 scopus 로고
    • A basis for distinguishing two types of purinergic receptors
    • R.W. Straub, L. Bolis (Eds.) Raven Press, New York
    • G. Burnstock, A basis for distinguishing two types of purinergic receptors, in: R.W. Straub, L. Bolis (Eds.), Cell Membrane Receptors for Drugs and Hormones, a Multidisciplinary Approach, Raven Press, New York, 1978, pp. 107-118.
    • (1978) Cell Membrane Receptors for Drugs and Hormones, a Multidisciplinary Approach , pp. 107-118
    • Burnstock, G.1
  • 7
    • 0027962545 scopus 로고
    • Purinoreceptors: Are there families of P2X and P2Y purinoceptors?
    • M.P. Abbracchio, G. Burnstock, Purinoreceptors: are there families of P2X and P2Y purinoceptors?, Pharmacol. Ther. 64 (1994) 445-475.
    • (1994) Pharmacol. Ther. , vol.64 , pp. 445-475
    • Abbracchio, M.P.1    Burnstock, G.2
  • 8
    • 0000612708 scopus 로고
    • Ectonucleotidases: Measurement of activities and use of inhibitors
    • D.M. Paton (Ed.) Plenum Press, New York
    • J.D. Pearson, Ectonucleotidases: measurement of activities and use of inhibitors, in: D.M. Paton (Ed.), Methods in Pharmacology, Plenum Press, New York, 1985, pp. 83-105.
    • (1985) Methods in Pharmacology , pp. 83-105
    • Pearson, J.D.1
  • 9
    • 0030221465 scopus 로고    scopus 로고
    • Biochemistry, localization and functional roles of ecto-nucleotidases in the nervous system
    • H. Zimmermann, Biochemistry, localization and functional roles of ecto-nucleotidases in the nervous system, Prog. Neurobiol. 49 (1996) 589-618.
    • (1996) Prog. Neurobiol. , vol.49 , pp. 589-618
    • Zimmermann, H.1
  • 11
    • 0029150609 scopus 로고
    • 3H]α,β-methylene adenosine 5′-triphosphate binding sites in human urinary bladder
    • 3H]α,β-methylene adenosine 5′-triphosphate binding sites in human urinary bladder, Br. J. Urol. 76 (1995) 297-302.
    • (1995) Br. J. Urol. , vol.76 , pp. 297-302
    • Bo, X.1    Burnstock, G.2
  • 13
    • 0029143893 scopus 로고
    • Purinergic agonist and G protein stimulation of phospholipase D in rat liver plasma membranes. Independence from phospholipase C activation
    • K.C. Malcolm, S.E. Trammell, J.H. Exton, Purinergic agonist and G protein stimulation of phospholipase D in rat liver plasma membranes. Independence from phospholipase C activation, Biochim. Biophys. Acta 1268 (1995) 152-158.
    • (1995) Biochim. Biophys. Acta , vol.1268 , pp. 152-158
    • Malcolm, K.C.1    Trammell, S.E.2    Exton, J.H.3
  • 17
    • 0022923888 scopus 로고
    • 2-purinoceptor involved in the activation of glycogen phosphorylase
    • 2-purinoceptor involved in the activation of glycogen phosphorylase, Biochem. J. 240 (1986) 367-371.
    • (1986) Biochem. J. , vol.240 , pp. 367-371
    • Keppens, S.1    De Wulf, H.2
  • 18
    • 0027411196 scopus 로고
    • The complex interaction of ATP and UTP with isolated hepatocytes. How many receptors?
    • S. Keppens, The complex interaction of ATP and UTP with isolated hepatocytes. How many receptors?, Gen. Pharmacol. 24 (1993) 283-289.
    • (1993) Gen. Pharmacol. , vol.24 , pp. 283-289
    • Keppens, S.1
  • 19
    • 0024323405 scopus 로고
    • The effects of some possible inhibitors of ectonucleotidases on the breakdown and pharmacological effects of ATP in the guinea-pig urinary bladder
    • S.M.O. Hourani, J.A. Chown, The effects of some possible inhibitors of ectonucleotidases on the breakdown and pharmacological effects of ATP in the guinea-pig urinary bladder, Gen. Pharmacol. 20 (1989) 413-416.
    • (1989) Gen. Pharmacol. , vol.20 , pp. 413-416
    • Hourani, S.M.O.1    Chown, J.A.2
  • 20
    • 0028020202 scopus 로고
    • Effects of cyclopiazonic acid on contractility and ecto-ATPase activity in guinea-pig urinary bladder and vas deferens
    • A.U. Ziganshin, C.H.V. Hoyle, L.E. Ziganshina, G. Burnstock, Effects of cyclopiazonic acid on contractility and ecto-ATPase activity in guinea-pig urinary bladder and vas deferens, Br. J. Pharmacol. 113 (1994) 669-674.
    • (1994) Br. J. Pharmacol. , vol.113 , pp. 669-674
    • Ziganshin, A.U.1    Hoyle, C.H.V.2    Ziganshina, L.E.3    Burnstock, G.4
  • 22
    • 0030937227 scopus 로고    scopus 로고
    • The interaction of diadenosine polyphosphates with P2X-receptors in the guinea-pig isolated vas deferens
    • T.D. Westfall, C.A. McIntyre, S. Obeid, J. Bowes, C. Kennedy, P. Sheddon, The interaction of diadenosine polyphosphates with P2X-receptors in the guinea-pig isolated vas deferens, Br. J. Pharmacol. 121 (1997) 57-62.
    • (1997) Br. J. Pharmacol. , vol.121 , pp. 57-62
    • Westfall, T.D.1    McIntyre, C.A.2    Obeid, S.3    Bowes, J.4    Kennedy, C.5    Sheddon, P.6
  • 23
    • 0029554726 scopus 로고
    • Inhibition of purified chicken gizzard smooth muscle ecto-ATPase by P2 purinoceptor antagonists
    • J.G. Stout, T.L. Kirley, Inhibition of purified chicken gizzard smooth muscle ecto-ATPase by P2 purinoceptor antagonists, Biochem. Mol. Biol. Int. 36 (1995) 927-934.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 927-934
    • Stout, J.G.1    Kirley, T.L.2
  • 24
    • 0023859146 scopus 로고
    • d 7.9 μmol/L) platelet binding sites for ADP and competition by ADP analogues
    • d 7.9 μmol/L) platelet binding sites for ADP and competition by ADP analogues, Blood 71 (1988) 110-116.
    • (1988) Blood , vol.71 , pp. 110-116
    • Jefferson, J.R.1    Harmon, J.T.2    Jamieson, G.A.3
  • 26
    • 0027209037 scopus 로고
    • Alteration of 5′-nucleotidase properties in rat adipose and liver plasma membranes after 1 Gy whole-body γ-irradiation
    • G.G. Yegutkin, S.M. Yakubovskii, G.G. Gatsko, Alteration of 5′-nucleotidase properties in rat adipose and liver plasma membranes after 1 Gy whole-body γ-irradiation, Int. J. Radiat. Biol. 63 (1993) 583-587.
    • (1993) Int. J. Radiat. Biol. , vol.63 , pp. 583-587
    • Yegutkin, G.G.1    Yakubovskii, S.M.2    Gatsko, G.G.3
  • 27
    • 0344828820 scopus 로고
    • Interaction of native 5′-ATP with plasma membranes of rat liver and adipose tissue
    • (Moscow) (Engl. transl.)
    • G.G. Yegutkin, Interaction of native 5′-ATP with plasma membranes of rat liver and adipose tissue, Biochemistry (Moscow) (Engl. transl.) 59 (1994) 1109-1112.
    • (1994) Biochemistry , vol.59 , pp. 1109-1112
    • Yegutkin, G.G.1
  • 28
    • 0015855230 scopus 로고
    • A rapid high yield method for the preparation of rat liver cell plasma membranes
    • P.R. Dorling, R.N. Le Page, A rapid high yield method for the preparation of rat liver cell plasma membranes, Biochim. Biophys. Acta 318 (1973) 33-44.
    • (1973) Biochim. Biophys. Acta , vol.318 , pp. 33-44
    • Dorling, P.R.1    Le Page, R.N.2
  • 29
    • 0015968725 scopus 로고
    • Quantitative thin-layer chromatography of ATP and the products of its degradation in meat tissue
    • G.A. Norman, M.J. Follett, D.A. Hector, Quantitative thin-layer chromatography of ATP and the products of its degradation in meat tissue, J. Chromatogr. 90 (1974) 105-111.
    • (1974) J. Chromatogr. , vol.90 , pp. 105-111
    • Norman, G.A.1    Follett, M.J.2    Hector, D.A.3
  • 30
    • 0014540830 scopus 로고
    • A new sensitive determination of phosphate
    • H. Eibl, W.E.M. Lands, A new sensitive determination of phosphate, Anal. Biochem. 30 (1969) 51-57.
    • (1969) Anal. Biochem. , vol.30 , pp. 51-57
    • Eibl, H.1    Lands, W.E.M.2
  • 31
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • M.A.K. Markwell, S.M. Haas, L.L. Bieber, N.B. Tolbert, A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples, Anal. Biochem. 87 (1978) 206-210.
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.B.4
  • 32
    • 0022393946 scopus 로고
    • Characterization of responses of isolated rat hepatocytes to ATP and ADP
    • R. Charest, P.F. Blackmore, J.H. Exton, Characterization of responses of isolated rat hepatocytes to ATP and ADP, J. Biol. Chem. 260 (1985) 15789-15794.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15789-15794
    • Charest, R.1    Blackmore, P.F.2    Exton, J.H.3
  • 33
    • 0028970635 scopus 로고
    • 2 purinergic agonists increase cytosolic calcium but not inositol 1,4,5-triphosphate in isolated rat hepatocytes
    • 2 purinergic agonists increase cytosolic calcium but not inositol 1,4,5-triphosphate in isolated rat hepatocytes, Biochim. Biophys. Acta 1269 (1995) 316-322.
    • (1995) Biochim. Biophys. Acta , vol.1269 , pp. 316-322
    • Keppens, S.1    De Wulf, H.2
  • 34
    • 0025937071 scopus 로고
    • Characterization of the biological effects of 2-methylthio-ATP on rat hepatocytes: Clear-cut differences with ATP
    • S. Keppens, H. De Wulf, Characterization of the biological effects of 2-methylthio-ATP on rat hepatocytes: clear-cut differences with ATP, Br. J. Pharmacol. 104 (1991) 301-304.
    • (1991) Br. J. Pharmacol. , vol.104 , pp. 301-304
    • Keppens, S.1    De Wulf, H.2
  • 35
    • 0027399066 scopus 로고
    • Adenine dinucleotide-mediated activation of glycogen phosphorylase in isolated liver cells
    • K.M. Craik, A.G. McLennan, M.J. Fisher, Adenine dinucleotide-mediated activation of glycogen phosphorylase in isolated liver cells, Cell. Signal. 5 (1993) 89-96.
    • (1993) Cell. Signal. , vol.5 , pp. 89-96
    • Craik, K.M.1    McLennan, A.G.2    Fisher, M.J.3
  • 36
    • 0030576660 scopus 로고    scopus 로고
    • Effects of diadenosine triphosphate and diadenosine tetraphosphate on rat liver cells. Differences and similarities with ADP and ATP
    • S. Keppens, Effects of diadenosine triphosphate and diadenosine tetraphosphate on rat liver cells. Differences and similarities with ADP and ATP, Biochem. Pharmacol. 52 (1996) 441-445.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 441-445
    • Keppens, S.1
  • 37
    • 0024538083 scopus 로고
    • Regulation of hepatic metabolism by extra-cellular nucleotides and eicosanoids
    • D. Häussinger, Regulation of hepatic metabolism by extra-cellular nucleotides and eicosanoids, J. Hepatol. 8 (1989) 259-266.
    • (1989) J. Hepatol. , vol.8 , pp. 259-266
    • Häussinger, D.1
  • 38
    • 0025566017 scopus 로고
    • Structural and chemical properties of ATP and its metal complexes in solution
    • M. Cohn, Structural and chemical properties of ATP and its metal complexes in solution, Ann. NY Acad. Sci. 603 (1990) 151-164.
    • (1990) Ann. NY Acad. Sci. , vol.603 , pp. 151-164
    • Cohn, M.1
  • 39
    • 0022357078 scopus 로고
    • Investigation of the preferred Mg(II)-adenine-nucleotide complex at the active site of ecto-nucleotidases in intact vascular cells using phosphorothioate analogues of ADP and ATP
    • J. Pearson, N.J. Cusack, Investigation of the preferred Mg(II)-adenine-nucleotide complex at the active site of ecto-nucleotidases in intact vascular cells using phosphorothioate analogues of ADP and ATP, Eur. J. Biochem. 151 (1985) 373-375.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 373-375
    • Pearson, J.1    Cusack, N.J.2


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