메뉴 건너뛰기




Volumn 34, Issue 6, 2007, Pages 1313-1322

Inhibition of alkaline phosphatase by cysteine: Implications for calcium pyrophosphate dihydrate crystal deposition disease

Author keywords

Alkaline phosphatase; Amino acids; Arthritis; Calcium pyrophosphate; Cartilage; Cysteine

Indexed keywords

ALKALINE PHOSPHATASE; AMINO ACID; CALCIUM ION; CALCIUM PYROPHOSPHATE; CYSTEINE; INORGANIC PYROPHOSPHATASE; MAGNESIUM ION;

EID: 34250175521     PISSN: 0315162X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (65)
  • 1
    • 0002271168 scopus 로고    scopus 로고
    • Pathology of osteoarthritis
    • Brandt KD, Lohmander S, Doherty M, editors, Oxford: Oxford University Press;
    • Pritzker KPH. Pathology of osteoarthritis. In: Brandt KD, Lohmander S, Doherty M, editors. Osteoarthritis. Oxford: Oxford University Press; 1998:106-30.
    • (1998) Osteoarthritis , pp. 106-130
    • Pritzker, K.P.H.1
  • 2
    • 0025159260 scopus 로고
    • Spontaneous osteoarthritis in rhesus macaques. 11. Characterization of disease and inorphometric studies
    • Chateauvert JMD, Grynpas MD, Kessler MJ, Pritzker KPH. Spontaneous osteoarthritis in rhesus macaques. 11. Characterization of disease and inorphometric studies. J Rheumatol 1990;17:73-83.
    • (1990) J Rheumatol , vol.17 , pp. 73-83
    • Chateauvert, J.M.D.1    Grynpas, M.D.2    Kessler, M.J.3    Pritzker, K.P.H.4
  • 3
    • 0020569260 scopus 로고
    • Calcium pyrophosphate dihydrate crystal deposition disease with concurrent vertebral hyperostosis in a Barbary ape
    • Kandel RA, Renlund RC, Cheng PT, Rapley WA, Mehren KG, Pritzker KPH. Calcium pyrophosphate dihydrate crystal deposition disease with concurrent vertebral hyperostosis in a Barbary ape. Arthritis Rheum 1983;26:682-7.
    • (1983) Arthritis Rheum , vol.26 , pp. 682-687
    • Kandel, R.A.1    Renlund, R.C.2    Cheng, P.T.3    Rapley, W.A.4    Mehren, K.G.5    Pritzker, K.P.H.6
  • 4
    • 0018636053 scopus 로고
    • Clearance of calcium pyrophosphate dihydrate crystals in vivo
    • McCarty DJ, Palmer DW, James C. Clearance of calcium pyrophosphate dihydrate crystals in vivo. Arthritis Rheum 1979;22:1122-31.
    • (1979) Arthritis Rheum , vol.22 , pp. 1122-1131
    • McCarty, D.J.1    Palmer, D.W.2    James, C.3
  • 5
    • 14944358653 scopus 로고    scopus 로고
    • Preparation and comprehensive characterization of a calcium hydroxyapatite reference material
    • Markovic M, Fowler BO, Tung MS. Preparation and comprehensive characterization of a calcium hydroxyapatite reference material. J Res Natl Inst Stand Technol 2004;109:553-68.
    • (2004) J Res Natl Inst Stand Technol , vol.109 , pp. 553-568
    • Markovic, M.1    Fowler, B.O.2    Tung, M.S.3
  • 6
    • 0026343175 scopus 로고
    • Alkaline phosphatase dissolves calcium pyrophosphatase dihydrate crystals
    • Xu Y, Cruz TF, Pritzker KPH. Alkaline phosphatase dissolves calcium pyrophosphatase dihydrate crystals. J Rheumatol 1991;18:1606-10.
    • (1991) J Rheumatol , vol.18 , pp. 1606-1610
    • Xu, Y.1    Cruz, T.F.2    Pritzker, K.P.H.3
  • 7
    • 0028243631 scopus 로고
    • Characterization of chondrocyte alkaline phosphatase as a mediator in the dissolution of calcium pyrophosphate dihydrate crystals
    • Xu Y, Pritzker KPH, Cruz TF. Characterization of chondrocyte alkaline phosphatase as a mediator in the dissolution of calcium pyrophosphate dihydrate crystals. J Rheumatol 1994;21:912-9.
    • (1994) J Rheumatol , vol.21 , pp. 912-919
    • Xu, Y.1    Pritzker, K.P.H.2    Cruz, T.F.3
  • 8
    • 0034813884 scopus 로고    scopus 로고
    • Inorganic pyrophosphate generation and disposition in pathophysiology
    • Terkeltaub RA. Inorganic pyrophosphate generation and disposition in pathophysiology. Am J Physiol Cell Physiol 2001;281:C1-C11.
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Terkeltaub, R.A.1
  • 9
    • 0021020015 scopus 로고
    • Pyrophosphate, phosphate ion interaction: Effects on calcium pyrophosphate and calcium hydroxyapatite crystal formation in aqueous solutions
    • Cheng P-T, Pritzker KPH, Pyrophosphate, phosphate ion interaction: Effects on calcium pyrophosphate and calcium hydroxyapatite crystal formation in aqueous solutions. J Rheumatol 1983;10:769-77.
    • (1983) J Rheumatol , vol.10 , pp. 769-777
    • Cheng, P.-T.1    Pritzker, K.P.H.2
  • 10
    • 0038664247 scopus 로고    scopus 로고
    • Physiological and pathophysiological functions of the ectonucleotide pyrophosphatase/phosphodiesterase family
    • Goding JW, Grobben B, Slegers H. Physiological and pathophysiological functions of the ectonucleotide pyrophosphatase/phosphodiesterase family. Biochim Biophys Acta 2003;1638:1-19.
    • (2003) Biochim Biophys Acta , vol.1638 , pp. 1-19
    • Goding, J.W.1    Grobben, B.2    Slegers, H.3
  • 11
    • 0038746715 scopus 로고    scopus 로고
    • Metabolism of extracellular pyrophosphate
    • Ryan LM, Rosenthal AK. Metabolism of extracellular pyrophosphate. Curr Opin Rheumatol 2003;15:311-4.
    • (2003) Curr Opin Rheumatol , vol.15 , pp. 311-314
    • Ryan, L.M.1    Rosenthal, A.K.2
  • 12
    • 0038070145 scopus 로고    scopus 로고
    • Extracellular nucleotides, cartilage stress, and calcium crystal formation
    • Graff RD, Picher M, Lee GM. Extracellular nucleotides, cartilage stress, and calcium crystal formation. Curr Opin Rheumatol 2003;15:315-20.
    • (2003) Curr Opin Rheumatol , vol.15 , pp. 315-320
    • Graff, R.D.1    Picher, M.2    Lee, G.M.3
  • 13
    • 0142135854 scopus 로고    scopus 로고
    • Extracellular nucleotide metabolism and signaling in the pathophysiology of articular cartilage
    • Picher M, Graff RD, Lee GM. Extracellular nucleotide metabolism and signaling in the pathophysiology of articular cartilage. Arthritis Rheum 2003;48:2722-36.
    • (2003) Arthritis Rheum , vol.48 , pp. 2722-2736
    • Picher, M.1    Graff, R.D.2    Lee, G.M.3
  • 14
    • 0019432024 scopus 로고
    • Comparison of phosphohydrolase activities from articular cartilage in calcium pyrophosphate deposition disease and primary osteoarthritis
    • Tenenbaum J, Muniz O, Schumacher HR, Good AE, Howell DS. Comparison of phosphohydrolase activities from articular cartilage in calcium pyrophosphate deposition disease and primary osteoarthritis. Arthritis Rheum 1981;24:492-500.
    • (1981) Arthritis Rheum , vol.24 , pp. 492-500
    • Tenenbaum, J.1    Muniz, O.2    Schumacher, H.R.3    Good, A.E.4    Howell, D.S.5
  • 15
    • 1242316272 scopus 로고    scopus 로고
    • Impaired calcification around matrix vesicles of growth plate and bone in alkaline phosphatase-deficient mice
    • Anderson HC, Sipe JB, Hessle L, et al. Impaired calcification around matrix vesicles of growth plate and bone in alkaline phosphatase-deficient mice. Am J Pathol 2004;164:841-7.
    • (2004) Am J Pathol , vol.164 , pp. 841-847
    • Anderson, H.C.1    Sipe, J.B.2    Hessle, L.3
  • 16
    • 0015860385 scopus 로고
    • Measurement of inorganic pyrophosphate in biological fluids. Elevated levels in some patients with osteoarthritis, pseudogout, acromegaly and uremia
    • Silcox DC, McCarty DJ. Measurement of inorganic pyrophosphate in biological fluids. Elevated levels in some patients with osteoarthritis, pseudogout, acromegaly and uremia. J Clin Invest 1973;53:1863-70.
    • (1973) J Clin Invest , vol.53 , pp. 1863-1870
    • Silcox, D.C.1    McCarty, D.J.2
  • 17
    • 0003591643 scopus 로고    scopus 로고
    • Calcium pyrophosphate crystal formation and dissolution
    • Amjad Z, editor, Boston: Kluwer Academic Publishers;
    • Pritzker KPH. Calcium pyrophosphate crystal formation and dissolution. In: Amjad Z, editor. Calcium phosphates in biological and industrial systems. Boston: Kluwer Academic Publishers; 1998:277-301.
    • (1998) Calcium phosphates in biological and industrial systems , pp. 277-301
    • Pritzker, K.P.H.1
  • 18
    • 0023713647 scopus 로고
    • Chemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase
    • Ogata S, Hayashi Y, Takami N, Ikehara Y. Chemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase. J Biol Chem 1988;263:10489-94.
    • (1988) J Biol Chem , vol.263 , pp. 10489-10494
    • Ogata, S.1    Hayashi, Y.2    Takami, N.3    Ikehara, Y.4
  • 20
    • 0029558381 scopus 로고
    • Characterization of the phosphatidylinositol-specific phospholipase C-released form of rat osseous plate alkaline phosphatase and its possible significance on endochondral ossification
    • Pizauro JM, Ciancaglini P, Leone FA. Characterization of the phosphatidylinositol-specific phospholipase C-released form of rat osseous plate alkaline phosphatase and its possible significance on endochondral ossification. Mol Cell Biochem 1995;152:121-9.
    • (1995) Mol Cell Biochem , vol.152 , pp. 121-129
    • Pizauro, J.M.1    Ciancaglini, P.2    Leone, F.A.3
  • 21
    • 34250160114 scopus 로고    scopus 로고
    • Review. Alkaline phosphatases. Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
    • Millan JL. Review. Alkaline phosphatases. Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes. Purinergic Signalling 2006;2:335-41.
    • (2006) Purinergic Signalling , vol.2 , pp. 335-341
    • Millan, J.L.1
  • 22
    • 0035903096 scopus 로고    scopus 로고
    • Structural evidence for a functional role of human tissue nonspecific alkaline phosphatase in bone mineralization
    • Mornet E, Stura E, Lia-Baldini AS, Stigbrand T, Menez A, Le Du MH. Structural evidence for a functional role of human tissue nonspecific alkaline phosphatase in bone mineralization. J Biol Chem 2001;276:31171-8.
    • (2001) J Biol Chem , vol.276 , pp. 31171-31178
    • Mornet, E.1    Stura, E.2    Lia-Baldini, A.S.3    Stigbrand, T.4    Menez, A.5    Le Du, M.H.6
  • 23
    • 0026660288 scopus 로고
    • Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase
    • Hoylaerts MF, Manes T, Millan JL. Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase. Biochem J 1992;286:23-30.
    • (1992) Biochem J , vol.286 , pp. 23-30
    • Hoylaerts, M.F.1    Manes, T.2    Millan, J.L.3
  • 24
    • 16644375200 scopus 로고    scopus 로고
    • Residues determining the binding specificity of uncompetitive inhibitors to tissue-nonspecific alkaline phosphatase
    • Kozlenkov A, Le Du MH, Cuniasse P, Ny T, Hoylaerts MF, Millan JL. Residues determining the binding specificity of uncompetitive inhibitors to tissue-nonspecific alkaline phosphatase. J Bone Miner Res 2004;19:1862-72.
    • (2004) J Bone Miner Res , vol.19 , pp. 1862-1872
    • Kozlenkov, A.1    Le Du, M.H.2    Cuniasse, P.3    Ny, T.4    Hoylaerts, M.F.5    Millan, J.L.6
  • 25
    • 0030928122 scopus 로고    scopus 로고
    • Mammalian alkaline phosphatases are allosteric enzymes
    • Hoylaerts MF, Manes T, Millán JL. Mammalian alkaline phosphatases are allosteric enzymes. J Biol Chem 1997;272:22781-7.
    • (1997) J Biol Chem , vol.272 , pp. 22781-22787
    • Hoylaerts, M.F.1    Manes, T.2    Millán, J.L.3
  • 26
    • 0030959696 scopus 로고    scopus 로고
    • Collagen phagocytosis and apoptosis are induced by high level alkaline phosphatase expression in rat fibroblasts
    • Hui MZ, Tenenbaum HC, McCulloch CA. Collagen phagocytosis and apoptosis are induced by high level alkaline phosphatase expression in rat fibroblasts. J Cell Physiol 1997;172:323-33.
    • (1997) J Cell Physiol , vol.172 , pp. 323-333
    • Hui, M.Z.1    Tenenbaum, H.C.2    McCulloch, C.A.3
  • 27
    • 0034113511 scopus 로고    scopus 로고
    • Hypophosphatasia: The mutations in the tissue-nonspecific alkaline phosphatase gene
    • Mornet E. Hypophosphatasia: the mutations in the tissue-nonspecific alkaline phosphatase gene. Hum Mutat 2000;15:309-15.
    • (2000) Hum Mutat , vol.15 , pp. 309-315
    • Mornet, E.1
  • 28
    • 34250217698 scopus 로고
    • Mechanism of inhibition of phosphatase activity by glycine
    • Bodansky O. Mechanism of inhibition of phosphatase activity by glycine. J Biol Chem 1946;165:605-13.
    • (1946) J Biol Chem , vol.165 , pp. 605-613
    • Bodansky, O.1
  • 29
    • 34250185642 scopus 로고
    • The inhibitory effects of DL-alanine, L-glutamic acid, L-lysine, and L-histidine on the activity of intestinal, bone and kidney phosphatases
    • Bodansky O. The inhibitory effects of DL-alanine, L-glutamic acid, L-lysine, and L-histidine on the activity of intestinal, bone and kidney phosphatases. J Biol Chem 1948;174:465-76.
    • (1948) J Biol Chem , vol.174 , pp. 465-476
    • Bodansky, O.1
  • 30
    • 0014829144 scopus 로고
    • L-homoarginine; an inhibitor of serum "bone and liver" alkaline phosphatase
    • Fishman W, Sie HG. L-homoarginine; an inhibitor of serum "bone and liver" alkaline phosphatase. Clin Chim Acta 1970;29:339-41.
    • (1970) Clin Chim Acta , vol.29 , pp. 339-341
    • Fishman, W.1    Sie, H.G.2
  • 31
    • 0015523082 scopus 로고    scopus 로고
    • Lin CW, Fishman WH. L-Homoarginine. An organ-specific, uncompetitive inhibitor of human liver and bone alkaline phosphohydrolases. J Biol Chem 1972;247:3082-7.
    • Lin CW, Fishman WH. L-Homoarginine. An organ-specific, uncompetitive inhibitor of human liver and bone alkaline phosphohydrolases. J Biol Chem 1972;247:3082-7.
  • 32
    • 0015245862 scopus 로고
    • Organ-specific inhibition of human alkaline phosphatase isoenzymes of liver, bone, intestine and placenta; L-phenylalanine, L-tryptophan and L-homoarginine
    • Fishman WH, Sie HG. Organ-specific inhibition of human alkaline phosphatase isoenzymes of liver, bone, intestine and placenta; L-phenylalanine, L-tryptophan and L-homoarginine. Enzymologia 1971;41:141-67.
    • (1971) Enzymologia , vol.41 , pp. 141-167
    • Fishman, W.H.1    Sie, H.G.2
  • 33
    • 0345631170 scopus 로고
    • L-Phenylalanine: An organ-specific, stereo-specific inhibitor of human intestinal alkaline phosphatase
    • Fishman WH, Green S, Inglis NR. L-Phenylalanine: An organ-specific, stereo-specific inhibitor of human intestinal alkaline phosphatase. Nature 1963;465:685-6.
    • (1963) Nature , vol.465 , pp. 685-686
    • Fishman, W.H.1    Green, S.2    Inglis, N.R.3
  • 34
    • 0015114282 scopus 로고
    • L-tryptophan. A non-allosteric organ-specific uncompetitive inhibitor of human placental alkaline phosphatase
    • Lin CW, Fishman WH. L-tryptophan. A non-allosteric organ-specific uncompetitive inhibitor of human placental alkaline phosphatase. Biochem J 1981;124:509-16.
    • (1981) Biochem J , vol.124 , pp. 509-516
    • Lin, C.W.1    Fishman, W.H.2
  • 35
    • 0022655518 scopus 로고
    • Calcium pyrophosphate crystal arthropathy. A biomineralization disorder
    • Pritzker KPH. Calcium pyrophosphate crystal arthropathy. A biomineralization disorder. Hum Pathol 1986;17:543-5.
    • (1986) Hum Pathol , vol.17 , pp. 543-545
    • Pritzker, K.P.H.1
  • 36
    • 34250202788 scopus 로고
    • Repression of alkaline phosphatase in human cell cultures by cystine and cysteine
    • Cox RP, Macleod CM, Repression of alkaline phosphatase in human cell cultures by cystine and cysteine. Proc Nat Acad Sci USA 1963;49:504-10.
    • (1963) Proc Nat Acad Sci USA , vol.49 , pp. 504-510
    • Cox, R.P.1    Macleod, C.M.2
  • 37
    • 0014006561 scopus 로고
    • Inhibition of alkaline phosphatase by cysteine and its analogues
    • Agus SG, Cox RP, Griffin MJ. Inhibition of alkaline phosphatase by cysteine and its analogues. Biochim Biophys Acta 1966;118:363-70.
    • (1966) Biochim Biophys Acta , vol.118 , pp. 363-370
    • Agus, S.G.1    Cox, R.P.2    Griffin, M.J.3
  • 38
    • 0032873672 scopus 로고    scopus 로고
    • Kinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by L-cysteine
    • Zhu CM, Chen QC, Lin HN, et al. Kinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by L-cysteine. J Protein Chem 1999;18:603-7.
    • (1999) J Protein Chem , vol.18 , pp. 603-607
    • Zhu, C.M.1    Chen, Q.C.2    Lin, H.N.3
  • 39
    • 1442277849 scopus 로고    scopus 로고
    • Kinetics and mechanism of interaction of L-cysteine with calf intestine alkaline phosphatase [Russian]
    • Vovk AI, Muzychka OV, Kharchenko OV. Kinetics and mechanism of interaction of L-cysteine with calf intestine alkaline phosphatase [Russian]. Ukr Biokhim Zh 2003;75:35-9.
    • (2003) Ukr Biokhim Zh , vol.75 , pp. 35-39
    • Vovk, A.I.1    Muzychka, O.V.2    Kharchenko, O.V.3
  • 40
    • 0037339424 scopus 로고    scopus 로고
    • Chondroitin sulfate and other sulfate containing chondroprotective agents may exhibit their effects by overcoming a deficiency of sulfur amino acids
    • Cordoba F, Nimni ME. Chondroitin sulfate and other sulfate containing chondroprotective agents may exhibit their effects by overcoming a deficiency of sulfur amino acids. Osteoarthritis Cartilage 2003;11:228-30.
    • (2003) Osteoarthritis Cartilage , vol.11 , pp. 228-230
    • Cordoba, F.1    Nimni, M.E.2
  • 42
    • 2642544983 scopus 로고    scopus 로고
    • Advancing age and other factors influencing the balance between amino acid requirements and toxicity
    • Fukagawa NK, Galbraith RA. Advancing age and other factors influencing the balance between amino acid requirements and toxicity. J Nutr 2004;134:1569S-74S.
    • (2004) J Nutr , vol.134
    • Fukagawa, N.K.1    Galbraith, R.A.2
  • 43
    • 34250166060 scopus 로고    scopus 로고
    • Jacobs DS, DeMott WR, Oxley DK. Laboratory test handbook. 5th ed. Hudson. OH: Lexi-Comp Inc.; 2001.
    • Jacobs DS, DeMott WR, Oxley DK. Laboratory test handbook. 5th ed. Hudson. OH: Lexi-Comp Inc.; 2001.
  • 45
    • 34250183006 scopus 로고    scopus 로고
    • Hase M. KaleidaGraph 3.0.5. for Macintosh and Windows. Computer software reviews. J Am Chem Soc 1997;119:4323.
    • Hase M. KaleidaGraph 3.0.5. for Macintosh and Windows. Computer software reviews. J Am Chem Soc 1997;119:4323.
  • 46
    • 34250164542 scopus 로고    scopus 로고
    • Kirsch PD, Ekerdt JG. KaleidaGraph: Graphing and data analysis. Version 3.5 for Windows. Computer software reviews. J Am Chem Soc 2000;122:11755
    • Kirsch PD, Ekerdt JG. KaleidaGraph: Graphing and data analysis. Version 3.5 for Windows. Computer software reviews. J Am Chem Soc 2000;122:11755.
  • 47
    • 0021881191 scopus 로고
    • A statistical comparison of parameter estimation for the Michaelis-Menten kinetics of human placental hexosaminidiase
    • Tommasini R, Endrenyi L, Taylor PA, Mahuran DJ, Lowden JA. A statistical comparison of parameter estimation for the Michaelis-Menten kinetics of human placental hexosaminidiase. Can J Biochem Cell Biol 1985;63:225-30.
    • (1985) Can J Biochem Cell Biol , vol.63 , pp. 225-230
    • Tommasini, R.1    Endrenyi, L.2    Taylor, P.A.3    Mahuran, D.J.4    Lowden, J.A.5
  • 48
    • 5844225066 scopus 로고
    • m in enzyme reactions
    • m in enzyme reactions. Science 1952;116:329-31.
    • (1952) Science , vol.116 , pp. 329-331
    • Hofstee, B.H.J.1
  • 49
    • 0035397393 scopus 로고    scopus 로고
    • Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: New ways of analysing data
    • Cortes A, Cascante M, Cardenas ML, Cornish-Bowden A. Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: new ways of analysing data. Biochem J 2001;357:263-8.
    • (2001) Biochem J , vol.357 , pp. 263-268
    • Cortes, A.1    Cascante, M.2    Cardenas, M.L.3    Cornish-Bowden, A.4
  • 50
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden A. A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem J 1974;137:143-4.
    • (1974) Biochem J , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 51
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon M. The determination of enzyme inhibitor constants. Biochem J 1953;55:170-1.
    • (1953) Biochem J , vol.55 , pp. 170-171
    • Dixon, M.1
  • 52
    • 0014045713 scopus 로고
    • Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations
    • Moss DW, Eaton RH, Smith JK, Whitby LG. Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations. Biochem J 1967;102:53-7.
    • (1967) Biochem J , vol.102 , pp. 53-57
    • Moss, D.W.1    Eaton, R.H.2    Smith, J.K.3    Whitby, L.G.4
  • 53
    • 0014138883 scopus 로고
    • Alkaline inorganic pyrophosphatase activity of mammalian-cell alkaline phosphatase
    • Cox RP, Gilbert P Jr, Griffin MJ. Alkaline inorganic pyrophosphatase activity of mammalian-cell alkaline phosphatase. Biochem J 1967;105:155-61.
    • (1967) Biochem J , vol.105 , pp. 155-161
    • Cox, R.P.1    Gilbert Jr, P.2    Griffin, M.J.3
  • 54
    • 0026030288 scopus 로고
    • Effects of pyrophosphatase on dissolution of calcium pyrophosphate dihydrate crystals
    • Xu Y, Cruz TF, Cheng P-T, Pritzker KPH. Effects of pyrophosphatase on dissolution of calcium pyrophosphate dihydrate crystals. J Rheumatol 1991;18:66-71.
    • (1991) J Rheumatol , vol.18 , pp. 66-71
    • Xu, Y.1    Cruz, T.F.2    Cheng, P.-T.3    Pritzker, K.P.H.4
  • 55
    • 0028801440 scopus 로고
    • Calcium pyrophosphate dihydrate (CPPD) crystal dissolution by alkaline phosphatase: Interaction of alkaline phosphatase on CPPD crystals
    • Shinozaki T, Xu Y, Cruz TF, Pritzker KPH. Calcium pyrophosphate dihydrate (CPPD) crystal dissolution by alkaline phosphatase: interaction of alkaline phosphatase on CPPD crystals. J Rheumatol 1995;22:117-23.
    • (1995) J Rheumatol , vol.22 , pp. 117-123
    • Shinozaki, T.1    Xu, Y.2    Cruz, T.F.3    Pritzker, K.P.H.4
  • 56
    • 0034194887 scopus 로고    scopus 로고
    • Amino acid release into the knee joint: Key role in nociception and inflammation
    • Lawand NB, McNearney T, Westlund KN. Amino acid release into the knee joint: key role in nociception and inflammation. Pain 2000;86:69-74.
    • (2000) Pain , vol.86 , pp. 69-74
    • Lawand, N.B.1    McNearney, T.2    Westlund, K.N.3
  • 58
    • 0037151014 scopus 로고    scopus 로고
    • Function assignment to conserved residues in mammalian alkaline phosphatases
    • Kozlenkov A, Manes T, Hoylaerts MF, Millán JL. Function assignment to conserved residues in mammalian alkaline phosphatases. J Biol Chem 2002;277:22992-9.
    • (2002) J Biol Chem , vol.277 , pp. 22992-22999
    • Kozlenkov, A.1    Manes, T.2    Hoylaerts, M.F.3    Millán, J.L.4
  • 59
    • 0032521155 scopus 로고    scopus 로고
    • Glutathione in human plasma: Decline in association with aging, age-related macular degeneration, and diabetes
    • Samiec PS, Drews-Botsch C, Flagg EW, et al. Glutathione in human plasma: decline in association with aging, age-related macular degeneration, and diabetes. Free Radical Biol Med 1998;24:699-704.
    • (1998) Free Radical Biol Med , vol.24 , pp. 699-704
    • Samiec, P.S.1    Drews-Botsch, C.2    Flagg, E.W.3
  • 61
    • 0023633601 scopus 로고
    • Effect of glycosaminoglycans on calcium pyrophosphate crystal formation in collagen gels
    • Hunter GK, Grynpas MD, Cheng P-T, Pritzker KPH. Effect of glycosaminoglycans on calcium pyrophosphate crystal formation in collagen gels. Calcif Tissue Int 1987;41:164-70.
    • (1987) Calcif Tissue Int , vol.41 , pp. 164-170
    • Hunter, G.K.1    Grynpas, M.D.2    Cheng, P.-T.3    Pritzker, K.P.H.4
  • 62
    • 0015550164 scopus 로고
    • The glycosaminoglycans of articular cartilage in calcium pyrophosphate dihydrate (CPPD) crystal deposition disease (chondrocalcinosis articularis or pyrophosphate arthropathy)
    • Bjelle AO. The glycosaminoglycans of articular cartilage in calcium pyrophosphate dihydrate (CPPD) crystal deposition disease (chondrocalcinosis articularis or pyrophosphate arthropathy). Calcif Tissue Int 1973;12:37-46.
    • (1973) Calcif Tissue Int , vol.12 , pp. 37-46
    • Bjelle, A.O.1
  • 63
    • 0032461412 scopus 로고    scopus 로고
    • A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • Galperin MY, Bairoch A, Koonin EV. A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci 1998;7:1829-35.
    • (1998) Protein Sci , vol.7 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 64
    • 0035847049 scopus 로고    scopus 로고
    • Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases
    • Gijsbers R, Ceulemans H, Stalmans W, Bollen M. Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases. J Biol Chem 2001;276:1361-8.
    • (2001) J Biol Chem , vol.276 , pp. 1361-1368
    • Gijsbers, R.1    Ceulemans, H.2    Stalmans, W.3    Bollen, M.4
  • 65
    • 0032477286 scopus 로고    scopus 로고
    • Sulfatase activity of E. coli alkaline phosphatase demonstrates a functional link to arysulfatases, an evolutionarily related enzyme family
    • O'Brien PJ, Herschlag D. Sulfatase activity of E. coli alkaline phosphatase demonstrates a functional link to arysulfatases, an evolutionarily related enzyme family. J Am Chem Soc 1998;120:12369-70.
    • (1998) J Am Chem Soc , vol.120 , pp. 12369-12370
    • O'Brien, P.J.1    Herschlag, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.