메뉴 건너뛰기




Volumn 317, Issue 1-2, 2008, Pages 85-95

Transformation and actions of extracellular NADP+ in the rat liver

Author keywords

2 Phospho ADP ribose; Glycogen catabolism; Hemodynamics; Hepatic action; Oxygen uptake; Purinergic receptors

Indexed keywords

4 BROMOPHENACYL BROMIDE; ADENOSINE DIPHOSPHATE RIBOSE; CALCIUM; GLUCOSE; GLYCOGEN; ICOSANOID; LACTIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PYRUVIC ACID; SURAMIN;

EID: 53149140255     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-008-9834-1     Document Type: Article
Times cited : (1)

References (39)
  • 4
    • 0026014146 scopus 로고
    • Novel mechanism of intracellular calcium release in pituitary cells
    • Koshiyama H, Lee HC, Tashjian AH (1991) Novel mechanism of intracellular calcium release in pituitary cells. J Biol Chem 266:16985-16988
    • (1991) J Biol Chem , vol.266 , pp. 16985-16988
    • Koshiyama, H.1    Lee, H.C.2    Tashjian, A.H.3
  • 5
    • 0028036438 scopus 로고
    • +
    • doi: 10.1007/BF00928466
    • +. Mol Cell Biochem 138:229-235. doi: 10.1007/BF00928466
    • (1994) Mol Cell Biochem , vol.138 , pp. 229-235
    • Lee, H.C.1
  • 9
    • 0035877808 scopus 로고    scopus 로고
    • + and cyclic ADP-ribose in increasing intracellular calcium and enhancing cell proliferation of 3T3 fibroblasts
    • + and cyclic ADP-ribose in increasing intracellular calcium and enhancing cell proliferation of 3T3 fibroblasts. J Biol Chem 276:21642-21648
    • (2001) J Biol Chem , vol.276 , pp. 21642-21648
    • Franco, F.1    Zocchi, E.2    Usai, C.3    Guida, L.4    Bruzzone, S.5    Costa, A.6
  • 12
    • 0027953389 scopus 로고
    • Glycogenolytic effect of adenosine involves ATP from hepatocytes and eicosanoids from Kupffer cells
    • Nukina S, Fusaoka T, Thurmann RG (1994) Glycogenolytic effect of adenosine involves ATP from hepatocytes and eicosanoids from Kupffer cells. Am J Physiol 266:G99-G105
    • (1994) Am J Physiol , vol.266
    • Nukina, S.1    Fusaoka, T.2    Thurmann, R.G.3
  • 14
    • 0029916751 scopus 로고    scopus 로고
    • 2′-Phospho-cyclic ADP-ribose, a calcium-mobilizing agent derived from NADP
    • doi: 10.1074/jbc.271.9.4747
    • Vu CQ, Lu PJ, Chen CS, Jacobson MK (1996) 2′-Phospho-cyclic ADP-ribose, a calcium-mobilizing agent derived from NADP. J Biol Chem 271:4747-4754. doi: 10.1074/jbc.271.9.4747
    • (1996) J Biol Chem , vol.271 , pp. 4747-4754
    • Vu, C.Q.1    Lu, P.J.2    Chen, C.S.3    Jacobson, M.K.4
  • 15
    • 0029616337 scopus 로고
    • ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP
    • doi: 10.1074/jbc.270.51.30327
    • Aarhus R, Graeff RM, Dickey DM, Walseth TF, Lee HC (1995) ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP. J Biol Chem 270:30327-30333. doi: 10.1074/ jbc.270.51.30327
    • (1995) J Biol Chem , vol.270 , pp. 30327-30333
    • Aarhus, R.1    Graeff, R.M.2    Dickey, D.M.3    Walseth, T.F.4    Lee, H.C.5
  • 16
    • 0028963107 scopus 로고
    • 2+-releasing agonist, in rat tissues
    • doi: 10.1006/bbrc.1995.1485
    • 2+-releasing agonist, in rat tissues. Biochem Biophys Res Commun 209:167-174. doi: 10.1006/bbrc.1995.1485
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 167-174
    • Chini, E.N.1    Dousa, T.P.2
  • 17
    • 0033986588 scopus 로고    scopus 로고
    • NAADP: An emerging calcium signalling molecule
    • doi: 10.1007/s002320001001
    • Lee HC (2000) NAADP: An emerging calcium signalling molecule. J Membr Biol 173:1-8. doi: 10.1007/s002320001001
    • (2000) J Membr Biol , vol.173 , pp. 1-8
    • Lee, H.C.1
  • 18
    • 23844497402 scopus 로고    scopus 로고
    • Pyridine nucleotides and calcium signalling in arterial smooth muscle: From cell physiology to pharmacology
    • doi: 10.1016/j.pharmthera.2005.03.003
    • Evans AM, Wyant CH, Kinnear NP, Clakr JH, Blanco EA (2005) Pyridine nucleotides and calcium signalling in arterial smooth muscle: From cell physiology to pharmacology. Pharmacol Ther 107:286-313. doi: 10.1016/ j.pharmthera.2005.03.003
    • (2005) Pharmacol Ther , vol.107 , pp. 286-313
    • Evans, A.M.1    Wyant, C.H.2    Kinnear, N.P.3    Clakr, J.H.4    Blanco, E.A.5
  • 19
    • 0027321317 scopus 로고
    • NAD glyco-hydrolase specifically induced by retinoic acid in human leukemic HL-60 cells. Identification of the NAD glycohydrolase as leukocyte cell surface antigen CD38
    • Kontani K, Nishina H, Ohoka Y, Takahashi K, Katada T (1993) NAD glyco-hydrolase specifically induced by retinoic acid in human leukemic HL-60 cells. Identification of the NAD glycohydrolase as leukocyte cell surface antigen CD38. J Biol Chem 268:16985-16988
    • (1993) J Biol Chem , vol.268 , pp. 16985-16988
    • Kontani, K.1    Nishina, H.2    Ohoka, Y.3    Takahashi, K.4    Katada, T.5
  • 20
    • 15944417442 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-Ribose in the activation of TRPM2 channels
    • doi: 10.1016/j.molcel.2005.02.033
    • Kolisek M, Beck A, Fleig A, Penner R (2005) Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-Ribose in the activation of TRPM2 channels. Mol Cell 18:61-69. doi: 10.1016/j.molcel.2005.02.033
    • (2005) Mol Cell , vol.18 , pp. 61-69
    • Kolisek, M.1    Beck, A.2    Fleig, A.3    Penner, R.4
  • 21
    • 0002232871 scopus 로고
    • Hemoglobin-free perfusion of rat liver
    • In: Chance B, Estabrook RW, Williamson JR (eds) Academic Press, New York
    • Scholz R, Bücher T (1965) Hemoglobin-free perfusion of rat liver. In: Chance B, Estabrook RW, Williamson JR (eds) Control of energy metabolism. Academic Press, New York, pp 393-414
    • (1965) Control of Energy Metabolism , pp. 393-414
    • Scholz, R.1    Bücher, T.2
  • 22
    • 0020300686 scopus 로고
    • Calcium ion fluxes induced by the action of alpha-adrenergic agonists in perfused rat liver
    • Reinhart PH, Taylor WM, Bygrave FL (1982) Calcium ion fluxes induced by the action of alpha-adrenergic agonists in perfused rat liver. Biochem J 208:619-630
    • (1982) Biochem J , vol.208 , pp. 619-630
    • Reinhart, P.H.1    Taylor, W.M.2    Bygrave, F.L.3
  • 23
    • 0000002475 scopus 로고
    • Determination of glucose with glucose oxidase and peroxidase
    • In: Bergmeyer HU (ed) Verlag Chemie-Academic Press, Weinheim-London
    • Bergmeyer HU, Bernt E (1974) Determination of glucose with glucose oxidase and peroxidase. In: Bergmeyer HU (ed) Methods of enzymatic analysis. Verlag Chemie-Academic Press, Weinheim-London, pp 1205-1215
    • (1974) Methods of Enzymatic Analysis , pp. 1205-1215
    • Bergmeyer, H.U.1    Bernt, E.2
  • 24
    • 0000831018 scopus 로고
    • +
    • In: Bergmeyer HU (ed) Verlag Chemie-Academic Press, Weinheim-London
    • +. In: Bergmeyer HU (ed) Methods of enzymatic analysis. Verlag Chemie-Academic Press, Weinheim-London, pp 1464-1468
    • (1974) Methods of Enzymatic Analysis , pp. 1464-1468
    • Gutman, J.1    Wahlefeld, A.W.2
  • 25
    • 0001262581 scopus 로고
    • Pyruvate, phosphoenolpyruvate and D-glycerate-2-phosphate
    • In: Bergmeyer HU (ed) Verlag Chemie-Academic Press, Weinheim-London
    • Czok R, Lamprecht W (1974) Pyruvate, phosphoenolpyruvate and D-glycerate-2-phosphate. In: Bergmeyer HU (ed) Methods of enzymatic analysis. Verlag Chemie-Academic Press, Weinheim-London, pp 1446-1451
    • (1974) Methods of Enzymatic Analysis , pp. 1446-1451
    • Czok, R.1    Lamprecht, W.2
  • 26
    • 0017893011 scopus 로고
    • Subcellular metabolite concentrations. Dependence of mitochondrial and cytosolic ATP systems on the metabolic state of perfused rat liver
    • doi: 10.1111/j.1432-1033.1978.tb12387.x
    • Soboll S, Scholz R, Heldt HW (1978) Subcellular metabolite concentrations. Dependence of mitochondrial and cytosolic ATP systems on the metabolic state of perfused rat liver. Eur J Biochem 87:377-390. doi: 10.1111/j.1432-1033.1978.tb12387.x
    • (1978) Eur J Biochem , vol.87 , pp. 377-390
    • Soboll, S.1    Scholz, R.2    Heldt, H.W.3
  • 27
    • 0015952137 scopus 로고
    • Histidine at the active site of phospholipase A 2
    • doi: 10.1021/bi00704a020
    • Volwerk JJ, Pieterson WA, de Haas GH (1974) Histidine at the active site of phospholipase A 2. Biochemistry 13:1446-1454. doi: 10.1021/bi00704a020
    • (1974) Biochemistry , vol.13 , pp. 1446-1454
    • Volwerk, J.J.1    Pieterson, W.A.2    de Haas, G.H.3
  • 28
    • 0027661421 scopus 로고
    • Signal transduction via P2-purinergic receptors for extracellular ATP and other nucleotides
    • Dubyak GR, El-Moatassim C (1993) Signal transduction via P2-purinergic receptors for extracellular ATP and other nucleotides. Am J Physiol 265:C577-C606
    • (1993) Am J Physiol , vol.265
    • Dubyak, G.R.1    El-Moatassim, C.2
  • 29
    • 0023818369 scopus 로고
    • 2+ fluxes and other physiological responses in rat liver
    • 2+ fluxes and other physiological responses in rat liver. Biochem J 249:677-685
    • (1988) Biochem J , vol.249 , pp. 677-685
    • Altin, J.G.1    Bygrave, F.L.2
  • 30
    • 0023874638 scopus 로고
    • Effects of leukotrienes and the thromboxane A2 analogue U-46619 in isolated perfused rat liver. Metabolic, hemodynamic and ion-flux responses
    • Häussinger D, Stehle T, Gerok W (1988) Effects of leukotrienes and the thromboxane A2 analogue U-46619 in isolated perfused rat liver. Metabolic, hemodynamic and ion-flux responses. Biol Chem Hoppe Seyler 369:97-107
    • (1988) Biol Chem Hoppe Seyler , vol.369 , pp. 97-107
    • Häussinger, D.1    Stehle, T.2    Gerok, W.3
  • 31
    • 0023749543 scopus 로고
    • Potential role for prostaglandin F2 alpha, D2, E2 and thromboxane A2 in mediating the metabolic and hemodynamic actions of sympathetic nerves in perfused rat
    • doi: 10.1111/j.1432-1033.1988.tb14164.x
    • Iwai M, Gardemann A, Püschel G, Jungermann K (1988) Potential role for prostaglandin F2 alpha, D2, E2 and thromboxane A2 in mediating the metabolic and hemodynamic actions of sympathetic nerves in perfused rat liver. Eur J Biochem 175:45-50. doi: 10.1111/j.1432-1033.1988.tb14164.x
    • (1988) Liver Eur J Biochem , vol.175 , pp. 45-50
    • Iwai, M.1    Gardemann, A.2    Püschel, G.3    Jungermann, K.4
  • 32
    • 0035978751 scopus 로고    scopus 로고
    • ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudixmotif homology
    • doi: 10.1038/35079100
    • Perraud AL, Fleig A, Dunn CA, Bagley LA, Launay P, Schmitz C et al (2001) ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudixmotif homology. Nature 411:595-599. doi: 10.1038/ 35079100
    • (2001) Nature , vol.411 , pp. 595-599
    • Perraud, A.L.1    Fleig, A.2    Dunn, C.A.3    Bagley, L.A.4    Launay, P.5    Schmitz, C.6
  • 33
    • 33744509311 scopus 로고    scopus 로고
    • Regulation of intracellular levels of NAD: A novel role for CD38
    • doi: 10.1016/j.bbrc.2006.05.042
    • Aksoy P, White TA, Thompson M, Chini EN (2006) Regulation of intracellular levels of NAD: A novel role for CD38. Biochem Biophys Res Commun 345:1386-1392. doi: 10.1016/j.bbrc.2006.05.042
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 1386-1392
    • Aksoy, P.1    White, T.A.2    Thompson, M.3    Chini, E.N.4
  • 34
    • 0021928360 scopus 로고
    • Analytical study of microsomes and isolated subcellular membranes from rat liver: IX. Nicotinamide adenine dinucleotide glycohydrolase: A plasma membrane enzyme prominently found in Kupffer cells
    • doi: 10.1083/jcb.100.1.189
    • Amar-Costesec A, Prado-Figueroa M, Beaufay H, Nagelkerke JF, van Berkel TJ (1985) Analytical study of microsomes and isolated subcellular membranes from rat liver: IX. Nicotinamide adenine dinucleotide glycohydrolase: A plasma membrane enzyme prominently found in Kupffer cells. J Cell Biol 100:89-97. doi: 10.1083/jcb.100.1.189
    • (1985) J Cell Biol , vol.100 , pp. 89-97
    • Amar-Costesec, A.1    Prado-Figueroa, M.2    Beaufay, H.3    Nagelkerke, J.F.4    van Berkel, T.J.5
  • 35
    • 2442431501 scopus 로고    scopus 로고
    • Regulation of purified and reconstituted connexin 43 hemichannels by protein kinase C-mediated phosphorylation of serine 368*
    • doi: 10.1074/jbc.M311137200
    • Bao X, Reuss L, Altenberg GA (2004) Regulation of purified and reconstituted connexin 43 hemichannels by protein kinase C-mediated phosphorylation of serine 368*. J Biol Chem 279:20058-20066. doi: 10.1074/jbc.M311137200
    • (2004) J Biol Chem , vol.279 , pp. 20058-20066
    • Bao, X.1    Reuss, L.2    Altenberg, G.A.3
  • 36
    • 40249103337 scopus 로고    scopus 로고
    • A novel role for connexin hemichannel in oxidative stress and smoking-induced cell injury
    • doi: 10.1371/journal.pone.0000712
    • Ramachandran S, Xie L-H, John SA, Subramaniam S, Lal R (2007) A novel role for connexin hemichannel in oxidative stress and smoking-induced cell injury. PLoS ONE 2(8):e712. doi: 10.1371/journal.pone.0000712
    • (2007) PLoS ONE , vol.2 , Issue.8
    • Ramachandran, S.1    Xie, L.-H.2    John, S.A.3    Subramaniam, S.4    Lal, R.5
  • 37
    • 0002703923 scopus 로고
    • Nicotinamide nucleotide compartmentation
    • In: Sies H (ed) Academic Press, New York
    • Sies H (1982) Nicotinamide nucleotide compartmentation. In: Sies H (ed) Metabolic compartmentation. Academic Press, New York, pp 205-231
    • (1982) Metabolic Compartmentation , pp. 205-231
    • Sies, H.1
  • 38
    • 36348971843 scopus 로고    scopus 로고
    • NAD kinase levels control the NADPH concentration in human cells
    • doi: 10.1074/jbc.M704442200
    • Pollak N, Niere M, Ziegler M (2007) NAD kinase levels control the NADPH concentration in human cells. J Biol Chem 282:33562-33571. doi: 10.1074/ jbc.M704442200
    • (2007) J Biol Chem , vol.282 , pp. 33562-33571
    • Pollak, N.1    Niere, M.2    Ziegler, M.3
  • 39
    • 37549068090 scopus 로고    scopus 로고
    • +/NADPH in cellular functions and cell death: Regulation and biological consequences
    • doi: 10.1089/ars.2007.1672
    • +/NADPH in cellular functions and cell death: Regulation and biological consequences. Antioxid Redox Signal 10:179-206. doi: 10.1089/ ars.2007.1672
    • (2008) Antioxid Redox Signal , vol.10 , pp. 179-206
    • Ying, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.