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Volumn 52, Issue 8, 1996, Pages 1187-1194

Direct measurement and regulation of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) generation in vitro

Author keywords

direct assay; HPLC radiometry; PAPS; regulation

Indexed keywords

4 NITROPHENOL; ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CYTIDINE TRIPHOSPHATE; DOPAMINE; GUANOSINE DIPHOSPHATE; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATE; HARMOL; HYMECROMONE; MINOXIDIL; N ACETYLDOPAMINE; SULFATE; SULFUR 35; URIDINE DIPHOSPHATE;

EID: 0030601836     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(96)00461-3     Document Type: Article
Times cited : (9)

References (46)
  • 2
    • 0024293480 scopus 로고
    • Phosphorylation of an 85-kd membrane protein by a novel mechanism
    • 2. Seydel U and Huttner WB, Phosphorylation of an 85-kd membrane protein by a novel mechanism. EMBO J 7: 4163-4167, 1988.
    • (1988) EMBO J , vol.7 , pp. 4163-4167
    • Seydel, U.1    Huttner, W.B.2
  • 3
    • 0017082713 scopus 로고
    • The importance of PAPS in determining sulfation in gastrointestinal mucosa
    • 3. Liau YH and Horowitz MI, The importance of PAPS in determining sulfation in gastrointestinal mucosa. Digestion 14: 372-375, 1976.
    • (1976) Digestion , vol.14 , pp. 372-375
    • Liau, Y.H.1    Horowitz, M.I.2
  • 4
    • 0018849427 scopus 로고
    • Synthesis of 3′-phosphoadenosine-5′-phosphosulfate (PAPS) increases during corneal development
    • 4. Conrad GW and Woo M-L, Synthesis of 3′-phosphoadenosine-5′-phosphosulfate (PAPS) increases during corneal development. J Biol Chem 255: 3086-3091, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 3086-3091
    • Conrad, G.W.1    Woo, M.-L.2
  • 5
    • 0023904313 scopus 로고
    • Does PAPS generation determine the overall sulfate conjugation in human platelets?
    • 5. Khoo BY, Sit KH and Wong KP, Does PAPS generation determine the overall sulfate conjugation in human platelets? Life Sci 42: 2389-2395, 1988.
    • (1988) Life Sci , vol.42 , pp. 2389-2395
    • Khoo, B.Y.1    Sit, K.H.2    Wong, K.P.3
  • 6
    • 0028030298 scopus 로고
    • A defect in the metabolic activation of sulfate in a patient with achondrogenesis type IB
    • 6. Superti-Furga A, A defect in the metabolic activation of sulfate in a patient with achondrogenesis type IB. Am J Hum Genet 55: 1137-1145, 1994.
    • (1994) Am J Hum Genet , vol.55 , pp. 1137-1145
    • Superti-Furga, A.1
  • 7
    • 0028899388 scopus 로고
    • Sulfate-activating enzymes in normal and brachymorphic mice: Evidence for a channeling defect
    • 7. Lyle S, Stanczak JD, Westley J and Schwartz NB, Sulfate-activating enzymes in normal and brachymorphic mice: Evidence for a channeling defect. Biochemistry 34: 940-945, 1995.
    • (1995) Biochemistry , vol.34 , pp. 940-945
    • Lyle, S.1    Stanczak, J.D.2    Westley, J.3    Schwartz, N.B.4
  • 8
    • 37049051839 scopus 로고
    • Synthesis of "active sulphate" (adenosine 3′-phosphate 5′-sulphatophosphate)
    • 8. Baddiley J, Buchanan JG, Letters R and Sanderson AR, Synthesis of "active sulphate" (adenosine 3′-phosphate 5′-sulphatophosphate). J Chem Soc 10: 1731-1734, 1959.
    • (1959) J Chem Soc , vol.10 , pp. 1731-1734
    • Baddiley, J.1    Buchanan, J.G.2    Letters, R.3    Sanderson, A.R.4
  • 9
    • 0011948167 scopus 로고
    • Enzymatic sulfation of mucopolysaccharides in hen oviduct. I. Transfer of sulfate from 3′-phosphoadenosine 5′ -phosphosulfate to mucopolysaccharides
    • 9. Suzuki S and Strominger JL, Enzymatic sulfation of mucopolysaccharides in hen oviduct. I. Transfer of sulfate from 3′-phosphoadenosine 5′ -phosphosulfate to mucopolysaccharides. J Biol Chem 235: 257-266, 1960.
    • (1960) J Biol Chem , vol.235 , pp. 257-266
    • Suzuki, S.1    Strominger, J.L.2
  • 10
    • 0016538005 scopus 로고
    • A bioluminescence method for determining adenosine 3′-phosphate 5′-phosphate (PAP) and adenosine 3′-phosphate 5′-sulfatophosphate (PAPS) in biological materials
    • 10. Stanley PE, Kelley BC, Tuovinen OH and Nicholas DJD, A bioluminescence method for determining adenosine 3′-phosphate 5′-phosphate (PAP) and adenosine 3′-phosphate 5′-sulfatophosphate (PAPS) in biological materials. Anal Biochem 67: 540-551, 1975.
    • (1975) Anal Biochem , vol.67 , pp. 540-551
    • Stanley, P.E.1    Kelley, B.C.2    Tuovinen, O.H.3    Nicholas, D.J.D.4
  • 11
    • 0000304328 scopus 로고
    • The transfer of sulfate among phenolic compounds with 3′,5′-diphosphoadenosine as coenzyme
    • 11. Gregory JD and Lipmann F, The transfer of sulfate among phenolic compounds with 3′,5′-diphosphoadenosine as coenzyme. J Biol Chem 229: 1081-1090, 1957.
    • (1957) J Biol Chem , vol.229 , pp. 1081-1090
    • Gregory, J.D.1    Lipmann, F.2
  • 12
    • 0018743435 scopus 로고
    • Assay of adenosine 3′-phosphate 5′-sulphatophosphate in hepatic tissues
    • 12. Wong KP and Yeo T, Assay of adenosine 3′-phosphate 5′-sulphatophosphate in hepatic tissues. Biochem J 181: 107-110, 1979.
    • (1979) Biochem J , vol.181 , pp. 107-110
    • Wong, K.P.1    Yeo, T.2
  • 13
    • 0021925443 scopus 로고
    • A radiometric method for the measurement of adenosine 3′-phosphate 5′-phosphosulfate in rat and mouse liver
    • 13. Hazelton GA, Hjelle JJ, Dills RL and Klaassen CD, A radiometric method for the measurement of adenosine 3′-phosphate 5′-phosphosulfate in rat and mouse liver. Drug Metab Dispos 13: 30-34, 1985.
    • (1985) Drug Metab Dispos , vol.13 , pp. 30-34
    • Hazelton, G.A.1    Hjelle, J.J.2    Dills, R.L.3    Klaassen, C.D.4
  • 14
    • 0025122204 scopus 로고
    • A simple sensitive fluorimetric assay of APS-kinase activity
    • 14. Wong KP, A simple sensitive fluorimetric assay of APS-kinase activity. Biochem Pharmacol 39: 173-179, 1990.
    • (1990) Biochem Pharmacol , vol.39 , pp. 173-179
    • Wong, K.P.1
  • 15
    • 0026086018 scopus 로고
    • Biosynthesis of PAPS in vitro by human liver. Measurement by two independent assay procedures
    • 15. Wong KP, Khoo BY and Sit KH, Biosynthesis of PAPS in vitro by human liver. Measurement by two independent assay procedures. Biochem Pharmacol 41: 63-69, 1991.
    • (1991) Biochem Pharmacol , vol.41 , pp. 63-69
    • Wong, K.P.1    Khoo, B.Y.2    Sit, K.H.3
  • 16
    • 0028261720 scopus 로고
    • Biosynthesis of 3′-phosphoadenosine-5′-phosphosulfate (PAPS) in rat skin
    • 16. Wong KO and Wong KP, Biosynthesis of 3′-phosphoadenosine-5′-phosphosulfate (PAPS) in rat skin. Biochem Pharmacol 47: 477-483, 1994.
    • (1994) Biochem Pharmacol , vol.47 , pp. 477-483
    • Wong, K.O.1    Wong, K.P.2
  • 17
    • 0023226070 scopus 로고
    • Inhibition of M and P phenol sulfotransferase by analogues of 3′-phosphoadenosine-5′-phosphosulfate
    • 17. Rens-Domiano SS and Roth JA, Inhibition of M and P phenol sulfotransferase by analogues of 3′-phosphoadenosine-5′-phosphosulfate. J Neurochem 48: 1411-1415, 1987.
    • (1987) J Neurochem , vol.48 , pp. 1411-1415
    • Rens-Domiano, S.S.1    Roth, J.A.2
  • 18
    • 0011950624 scopus 로고
    • Direct measurement of PAPS generation
    • 18. Wong KP, Wong KO and Sit KH, Direct measurement of PAPS generation. Can J Physiol Pharmacol 72(Suppl 1): 312, 1994.
    • (1994) Can J Physiol Pharmacol , vol.72 , Issue.SUPPL. 1 , pp. 312
    • Wong, K.P.1    Wong, K.O.2    Sit, K.H.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 20. Bradford MM, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0002854151 scopus 로고
    • Analysis of 3′-phosphoadenylylsulphate and related compounds by pairedion high-performance liquid chromatography
    • 21. Pennings EJM and van Kempen GMJ, Analysis of 3′-phosphoadenylylsulphate and related compounds by pairedion high-performance liquid chromatography. J Chromatogr 176: 478-479, 1979.
    • (1979) J Chromatogr , vol.176 , pp. 478-479
    • Pennings, E.J.M.1    Van Kempen, G.M.J.2
  • 22
    • 0024561266 scopus 로고
    • Rat liver ATP-sulfurylase: Purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions
    • 22. Yu M, Martin RL, Jain S, Chen LJ and Segel IH, Rat liver ATP-sulfurylase: Purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions. Arch Biochem Biophys 269: 156-174, 1989.
    • (1989) Arch Biochem Biophys , vol.269 , pp. 156-174
    • Yu, M.1    Martin, R.L.2    Jain, S.3    Chen, L.J.4    Segel, I.H.5
  • 23
    • 0017181859 scopus 로고
    • The conjugation of tyramine with sulphate by liver and intestine of different animals
    • 23. Wong KP, The conjugation of tyramine with sulphate by liver and intestine of different animals. Biochem J 160: 491-493, 1976.
    • (1976) Biochem J , vol.160 , pp. 491-493
    • Wong, K.P.1
  • 24
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • 24. Lineweaver H and Burk D, The determination of enzyme dissociation constants. J Am Chem Soc 56: 658-666, 1934.
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 26
    • 0014504441 scopus 로고
    • Kinetics of enzyme reactions with interaction between a substrate and a (metal) modifier
    • 26. London WP and Steck TL, Kinetics of enzyme reactions with interaction between a substrate and a (metal) modifier. Biochemistry 8: 1767-1779, 1969.
    • (1969) Biochemistry , vol.8 , pp. 1767-1779
    • London, W.P.1    Steck, T.L.2
  • 27
    • 0016198219 scopus 로고
    • The concentration and control of cytoplasmic free inorganic pyrophosphate in rat liver in vivo
    • 27. Guynn RW, Veloso D, Lawson JWR and Veech RL, The concentration and control of cytoplasmic free inorganic pyrophosphate in rat liver in vivo. Biochem J 140: 369-375, 1974.
    • (1974) Biochem J , vol.140 , pp. 369-375
    • Guynn, R.W.1    Veloso, D.2    Lawson, J.W.R.3    Veech, R.L.4
  • 28
    • 0011321084 scopus 로고
    • Phenol sulphotransferase in human platelet and other tissues: Endogenous inhibitors, assay conditions, tissue and substrate correlations
    • (Eds. Sandler M and Usdin E), Macmillari, London
    • 28. Weinshilboum RM and Anderson RJ, Phenol sulphotransferase in human platelet and other tissues: Endogenous inhibitors, assay conditions, tissue and substrate correlations. In: Phenolsulfotransferase in Mental Health Research (Eds. Sandler M and Usdin E), pp. 8-28. Macmillari, London, 1981.
    • (1981) Phenolsulfotransferase in Mental Health Research , pp. 8-28
    • Weinshilboum, R.M.1    Anderson, R.J.2
  • 29
    • 0003162251 scopus 로고
    • Sulfate conjugation of amines and their metabolites
    • (Eds. Mulder GJ, Caldwell J, van Kempen GMJ and Vonk RJ), Taylor & Francis, London
    • 29. Wong KP, Sulfate conjugation of amines and their metabolites. In: Sulfate Metabolism and Sulfate Conjugation (Eds. Mulder GJ, Caldwell J, van Kempen GMJ and Vonk RJ), pp. 85-92. Taylor & Francis, London, 1982.
    • (1982) Sulfate Metabolism and Sulfate Conjugation , pp. 85-92
    • Wong, K.P.1
  • 30
    • 0019407087 scopus 로고
    • Aberrant pharmacokinetics of harmol in the perfused rat liver preparation: Sulfate and glucuronide conjugations
    • 30. Pang KS, Koster H, Halsema ICM, Scholtens E and Mulder GJ, Aberrant pharmacokinetics of harmol in the perfused rat liver preparation: Sulfate and glucuronide conjugations. J Pharmacol Exp Ther 219: 134-140, 1981.
    • (1981) J Pharmacol Exp Ther , vol.219 , pp. 134-140
    • Pang, K.S.1    Koster, H.2    Halsema, I.C.M.3    Scholtens, E.4    Mulder, G.J.5
  • 31
    • 0026649746 scopus 로고
    • Homeostasis of sulfate and 3′-phosphoadenosine 5′-phosphosulfate in rats after acetaminophen administration
    • 31. Kim HJ, Rozman P, Madhu C and Klaassen CD, Homeostasis of sulfate and 3′-phosphoadenosine 5′-phosphosulfate in rats after acetaminophen administration. J Pharmacol Exp Ther 261: 1015-1021, 1992.
    • (1992) J Pharmacol Exp Ther , vol.261 , pp. 1015-1021
    • Kim, H.J.1    Rozman, P.2    Madhu, C.3    Klaassen, C.D.4
  • 32
    • 0015239426 scopus 로고
    • Adenosine triphosphate sulfurylase from Penicillium chrysogenum. II. Physical, kinetic, and regulatory properties
    • 32. Tweedie JW and Segel IH, Adenosine triphosphate sulfurylase from Penicillium chrysogenum. II. Physical, kinetic, and regulatory properties. J Biol Chem 246: 2438-2446, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 2438-2446
    • Tweedie, J.W.1    Segel, I.H.2
  • 33
    • 0021361418 scopus 로고
    • Adenosine 5′-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization
    • 33. Renosto F, Seubert PA and Segel IH, Adenosine 5′-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization. J Biol Chem 259: 2113-2123, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 2113-2123
    • Renosto, F.1    Seubert, P.A.2    Segel, I.H.3
  • 34
    • 0015784007 scopus 로고
    • Adenosine 5′-triphosphate sulphurylase from Saccharomyces cerevisiae
    • 34. Hawes CS and Nicholas DJD, Adenosine 5′-triphosphate sulphurylase from Saccharomyces cerevisiae. Biochem J 133: 541-550, 1973.
    • (1973) Biochem J , vol.133 , pp. 541-550
    • Hawes, C.S.1    Nicholas, D.J.D.2
  • 35
    • 0015516477 scopus 로고
    • Enzyme-substrate complexes of ATP-sulfurylase from mouse mastocytoma
    • 35. Shoyab M and Marx W, Enzyme-substrate complexes of ATP-sulfurylase from mouse mastocytoma. Biochim Biophys Acta 258: 125-132, 1972.
    • (1972) Biochim Biophys Acta , vol.258 , pp. 125-132
    • Shoyab, M.1    Marx, W.2
  • 36
    • 0015311856 scopus 로고
    • Purification, properties and substrate specificity of adenosine triphosphate sulphurylase from spinach leaf tissue
    • 36. Shaw WH and Anderson JW, Purification, properties and substrate specificity of adenosine triphosphate sulphurylase from spinach leaf tissue. Biochem J 127: 237-247, 1972.
    • (1972) Biochem J , vol.127 , pp. 237-247
    • Shaw, W.H.1    Anderson, J.W.2
  • 37
    • 0011917382 scopus 로고
    • Nucleotide and nucleic acid synthesis, cellular organization
    • (Ed. Dulbecco R), Academic Press, San Diego
    • 37. Mathews CK, Nucleotide and nucleic acid synthesis, cellular organization. In: Encyclopedia of Human Biology (Ed. Dulbecco R), Vol. 5, pp. 461-470. Academic Press, San Diego, 1991.
    • (1991) Encyclopedia of Human Biology , vol.5 , pp. 461-470
    • Mathews, C.K.1
  • 38
    • 0017614106 scopus 로고
    • Studies on bovine adrenal estrogen sulfotransferase. III. Facile synthesis of 3′-phospho-and 2′-phosphoadenosine 5′-phosphosulfate
    • 38. Horwitz JP, Neenan JP, Misra RS, Rozhin J, Huo A and Philips KD, Studies on bovine adrenal estrogen sulfotransferase. III. Facile synthesis of 3′-phospho-and 2′-phosphoadenosine 5′-phosphosulfate. Biochim Biophys Acta 480: 376-381, 1977.
    • (1977) Biochim Biophys Acta , vol.480 , pp. 376-381
    • Horwitz, J.P.1    Neenan, J.P.2    Misra, R.S.3    Rozhin, J.4    Huo, A.5    Philips, K.D.6
  • 39
    • 0019308831 scopus 로고
    • Studies on bovine adrenal estrogen sulfotransferase. V. Synthesis and assay of analogs of 3′-phosphoadenosine 5′-phosphosulfate as cosubstrates for estrogen sulfurylation
    • 39. Horwitz JP, Misra RS, Rozhin J, Helmer S, Bhuta A and Brooks SC, Studies on bovine adrenal estrogen sulfotransferase. V. Synthesis and assay of analogs of 3′-phosphoadenosine 5′-phosphosulfate as cosubstrates for estrogen sulfurylation. Biochim Biophys Acta 613: 85-94, 1980.
    • (1980) Biochim Biophys Acta , vol.613 , pp. 85-94
    • Horwitz, J.P.1    Misra, R.S.2    Rozhin, J.3    Helmer, S.4    Bhuta, A.5    Brooks, S.C.6
  • 40
    • 0014687578 scopus 로고
    • Purification and properties of the enzyme ATP-sulfurylase and its relation to vitamin A
    • 40. Levi AS and Wolf G, Purification and properties of the enzyme ATP-sulfurylase and its relation to vitamin A. Biochim Biophys Acta 178: 262-282, 1969.
    • (1969) Biochim Biophys Acta , vol.178 , pp. 262-282
    • Levi, A.S.1    Wolf, G.2
  • 41
    • 0028357714 scopus 로고
    • Rat chondrosarcoma ATP sulfurylase and adenosine 5′ -phosphosulfate kinase reside on a single bifunctional protein
    • 41. Lyle S, Stanczak J, Ng K and Schwartz NB, Rat chondrosarcoma ATP sulfurylase and adenosine 5′ -phosphosulfate kinase reside on a single bifunctional protein. Biochemistry 33: 5920-5925, 1994.
    • (1994) Biochemistry , vol.33 , pp. 5920-5925
    • Lyle, S.1    Stanczak, J.2    Ng, K.3    Schwartz, N.B.4
  • 42
    • 0028130514 scopus 로고
    • Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating complex requiring GTP for activity
    • 42. Schwedock JS, Liu C, Leyh TS and Long SR, Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating complex requiring GTP for activity. J Bacteriol 176: 7055-7064, 1994.
    • (1994) J Bacteriol , vol.176 , pp. 7055-7064
    • Schwedock, J.S.1    Liu, C.2    Leyh, T.S.3    Long, S.R.4
  • 43
    • 0028017799 scopus 로고
    • Sulfation of acetaminophen and acetaminophen-induced alterations in sulfate and 3′-phosphoadenosine 5′-phosphosulfate homeostasis in rats with deficient dietary intake of sulfur
    • 43. Gregus Z, Kim HJ, Madhu C, Liu Y, Rozman P and Klaassen CD, Sulfation of acetaminophen and acetaminophen-induced alterations in sulfate and 3′-phosphoadenosine 5′-phosphosulfate homeostasis in rats with deficient dietary intake of sulfur. Drug Metab Dispos 22: 725-730, 1994.
    • (1994) Drug Metab Dispos , vol.22 , pp. 725-730
    • Gregus, Z.1    Kim, H.J.2    Madhu, C.3    Liu, Y.4    Rozman, P.5    Klaassen, C.D.6
  • 44
    • 0028363648 scopus 로고
    • The energetic linkage of GTP hydrolysis and the synthesis of activated sulfate
    • 44. Liu C, Suo Y and Leyh TS, The energetic linkage of GTP hydrolysis and the synthesis of activated sulfate. Biochemistry 33: 7309-7314, 1994.
    • (1994) Biochemistry , vol.33 , pp. 7309-7314
    • Liu, C.1    Suo, Y.2    Leyh, T.S.3
  • 45
    • 0028050646 scopus 로고
    • Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain
    • 45. Foster BA, Thomas SM, Mahr JA, Renosto F, Patel HC and Segel IH, Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain. J Biol Chem 269: 19777-19786, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 19777-19786
    • Foster, B.A.1    Thomas, S.M.2    Mahr, J.A.3    Renosto, F.4    Patel, H.C.5    Segel, I.H.6
  • 46
    • 0027138759 scopus 로고
    • ATP sulfurylase from higher plants: Kinetic and structural characterization of the chloroplast and cytosol enzymes from spinach leaf
    • 46. Renosto F, Patel HC, Martin RL, Thomassian C, Zimmerman G and Segel IH, ATP sulfurylase from higher plants: Kinetic and structural characterization of the chloroplast and cytosol enzymes from spinach leaf. Arch Biochem Biophys 307: 272-285, 1993.
    • (1993) Arch Biochem Biophys , vol.307 , pp. 272-285
    • Renosto, F.1    Patel, H.C.2    Martin, R.L.3    Thomassian, C.4    Zimmerman, G.5    Segel, I.H.6


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