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Volumn 22, Issue 6, 1997, Pages 939-946

Antioxidant functions of inositol 1,2,3-trisphosphate and inositol 1,2,3,6-tetrakisphosphate

Author keywords

Antioxidants; Free radicals; Inositol phosphates; Iron; Phosphatase; Phytase

Indexed keywords

FREE RADICAL; INOSITOL TETRAKISPHOSPHATE; INOSITOL TRISPHOSPHATE; IRON; PHOSPHATASE; PHYTASE;

EID: 0031050089     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(96)00342-5     Document Type: Article
Times cited : (81)

References (52)
  • 1
    • 0027396903 scopus 로고
    • Suppression of colonic cancer by dietary phytic acid
    • Graf E., Eaton J. W. Suppression of colonic cancer by dietary phytic acid. Nutr. Cancer. 19:1993;11-19.
    • (1993) Nutr. Cancer , vol.19 , pp. 11-19
    • Graf, E.1    Eaton, J.W.2
  • 2
    • 0028809234 scopus 로고
    • Inositol phosphates have novel anticancer function
    • Shamsuddin A. M. Inositol phosphates have novel anticancer function. J. Nutr. 125:1995;725S-732S.
    • (1995) J. Nutr. , vol.125
    • Shamsuddin, A.M.1
  • 3
    • 0025021262 scopus 로고
    • Antioxidant functions of phytic acid
    • Graf E., Eaton J. W. Antioxidant functions of phytic acid. Free Radic. Biol. Med. 8:1990;61-69.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 61-69
    • Graf, E.1    Eaton, J.W.2
  • 4
    • 0027484499 scopus 로고
    • Inhibition of iron-catalyzed hydroxyl radical formation by inositol polyphosphates: A possible physiological function for myo-inositol hexakisphosphate
    • Hawkins P. T., Poyner D. R., Jackson T. R., Letcher A. J., Lander D. A., Irvine R. F. Inhibition of iron-catalyzed hydroxyl radical formation by inositol polyphosphates: A possible physiological function for myo-inositol hexakisphosphate. Biochem. J. 294:1993;929-934.
    • (1993) Biochem. J. , vol.294 , pp. 929-934
    • Hawkins, P.T.1    Poyner, D.R.2    Jackson, T.R.3    Letcher, A.J.4    Lander, D.A.5    Irvine, R.F.6
  • 6
    • 0028114818 scopus 로고
    • Purification and some properties of inositol 1,3,4,5,6-pentakisphosphate 2-kinase from immature soybean seeds
    • Phillippy B. Q., Ullah A. H. J., Ehrlich K. C. Purification and some properties of inositol 1,3,4,5,6-pentakisphosphate 2-kinase from immature soybean seeds. J. Biol. Chem. 269:1994;28393-28399.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28393-28399
    • Phillippy, B.Q.1    Ullah, A.H.J.2    Ehrlich, K.C.3
  • 7
    • 0026730329 scopus 로고
    • Inositol polyphosphate receptor and clathrin assembly protein AP-2 are related proteins that form potassium-selective ion channels in planar lipid bilayers
    • Timerman A. P., Mayrleitner M. M., Lukas T. J., Chadwick C. C., Saito A., Watterson D. M., Schindler H., Fleischer S. Inositol polyphosphate receptor and clathrin assembly protein AP-2 are related proteins that form potassium-selective ion channels in planar lipid bilayers. Proc. Natl. Acad. Sci. USA. 89:1992;8976-8980.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8976-8980
    • Timerman, A.P.1    Mayrleitner, M.M.2    Lukas, T.J.3    Chadwick, C.C.4    Saito, A.5    Watterson, D.M.6    Schindler, H.7    Fleischer, S.8
  • 10
    • 0027986795 scopus 로고
    • Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II
    • Fukuda M., Aruga J., Niinobe M., Aimoto S., Mikoshiba K. Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J. Biol. Chem. 269:1994;29206-29211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29206-29211
    • Fukuda, M.1    Aruga, J.2    Niinobe, M.3    Aimoto, S.4    Mikoshiba, K.5
  • 11
    • 0028586130 scopus 로고
    • The inositol high-polyphosphate series blocks synaptic transmission by preventing vesicular fusion: A squid giant synapse study
    • Llinas R., Sugimori M., Lang E. J., Morita M., Fukuda M., Niinobe M, Mikoshiba K. The inositol high-polyphosphate series blocks synaptic transmission by preventing vesicular fusion: A squid giant synapse study. Proc. Natl. Acad. Sci. USA. 91:1994;12990-12993.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12990-12993
    • Llinas, R.1    Sugimori, M.2    Lang, E.J.3    Morita, M.4    Fukuda, M.5    Niinobe, M.6    Mikoshiba, K.7
  • 12
    • 0028842364 scopus 로고
    • Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP-3/AP180) and inhibits clathrin cage assembly in vitro
    • Norris F. A., Ungewickell E., Majerus P. W. Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP-3/AP180) and inhibits clathrin cage assembly in vitro. J. Biol. Chem. 270:1995;214-217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 214-217
    • Norris, F.A.1    Ungewickell, E.2    Majerus, P.W.3
  • 13
    • 0028925007 scopus 로고
    • Inhibition of clathrin assembly by high affinity binding of specific inositol polyphosphates to the synapse-specific clathrin assembly protein AP-3
    • Ye W., Ali N., Bembenek M. E., Shears S. B., Lafer E. M. Inhibition of clathrin assembly by high affinity binding of specific inositol polyphosphates to the synapse-specific clathrin assembly protein AP-3. J. Biol. Chem. 270:1995;1564-1568.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1564-1568
    • Ye, W.1    Ali, N.2    Bembenek, M.E.3    Shears, S.B.4    Lafer, E.M.5
  • 14
    • 0021337104 scopus 로고
    • Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site
    • Graf E., Mahoney J. R., Bryant R. G., Eaton J. W. Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site. J. Biol. Chem. 259:1984;3620-3624.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3620-3624
    • Graf, E.1    Mahoney, J.R.2    Bryant, R.G.3    Eaton, J.W.4
  • 15
    • 0023664866 scopus 로고
    • Phytic acid. A natural antioxidant
    • Graf E., Empson K. L., Eaton J. W. Phytic acid. A natural antioxidant. J. Biol. Chem. 262:1987;11647-11650.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11647-11650
    • Graf, E.1    Empson, K.L.2    Eaton, J.W.3
  • 16
    • 0028966358 scopus 로고
    • The first synthesis and iron binding studies of the natural product, myo-inositol 1,2,3-trisphosphate
    • Spiers I. D., Freeman S., Poyner D. R., Schwalbe C. H. The first synthesis and iron binding studies of the natural product, myo-inositol 1,2,3-trisphosphate. Tetrahedron Lett. 36:1995;2125-2128.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 2125-2128
    • Spiers, I.D.1    Freeman, S.2    Poyner, D.R.3    Schwalbe, C.H.4
  • 17
    • 0000018449 scopus 로고
    • Myoinositol polyphosphate intermediates in the dephosphorylation of phytic acid by phytase
    • Tomlinson R. V., Ballou C. E. Myoinositol polyphosphate intermediates in the dephosphorylation of phytic acid by phytase. Biochemistry. 1:1962;166-171.
    • (1962) Biochemistry , vol.1 , pp. 166-171
    • Tomlinson, R.V.1    Ballou, C.E.2
  • 18
    • 0000994881 scopus 로고
    • Identification by two-dimensional NMR of inositol tris- and tetrakis (phosphates) formed from phytic acid by wheat phytase
    • Phillippy B. Q. Identification by two-dimensional NMR of inositol tris- and tetrakis (phosphates) formed from phytic acid by wheat phytase. J. Agric. Food Chem. 37:1989;1261-1265.
    • (1989) J. Agric. Food Chem. , vol.37 , pp. 1261-1265
    • Phillippy, B.Q.1
  • 19
    • 84954882595 scopus 로고
    • Myo-inositol polyphosphate intermediates in the dephosphorylation of phytic acid by acid phosphatase with phytase activity from rice bran
    • Hayakawa T., Suzuki K., Miura H., Ohno T., Igaue I. Myo-inositol polyphosphate intermediates in the dephosphorylation of phytic acid by acid phosphatase with phytase activity from rice bran. Agric. Biol. Chem. 54:1990;279-286.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 279-286
    • Hayakawa, T.1    Suzuki, K.2    Miura, H.3    Ohno, T.4    Igaue, I.5
  • 20
    • 0028675620 scopus 로고
    • Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen
    • Barrientos L., Scott J. J., Murthy P. P. N. Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen. Plant Physiol. 106:1994;1489-1495.
    • (1994) Plant Physiol. , vol.106 , pp. 1489-1495
    • Barrientos, L.1    Scott, J.J.2    Murthy, P.P.N.3
  • 22
    • 0024273151 scopus 로고
    • Gradient ion chromatography of inositol phosphates
    • Phillippy B. Q., Bland J. M. Gradient ion chromatography of inositol phosphates. Anal. Biochem. 175:1988;162-166.
    • (1988) Anal. Biochem. , vol.175 , pp. 162-166
    • Phillippy, B.Q.1    Bland, J.M.2
  • 23
    • 0019830545 scopus 로고
    • A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase
    • Heinonen J. K., Lahti R. J. A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal. Biochem. 113:1981;313-317.
    • (1981) Anal. Biochem. , vol.113 , pp. 313-317
    • Heinonen, J.K.1    Lahti, R.J.2
  • 24
    • 0019587427 scopus 로고
    • Determination of TBA number by high performance liquid chromatography
    • Kakuda Y., Stanley D. W., van de Voort F. R. Determination of TBA number by high performance liquid chromatography. J. Am. Oil Chem. Soc. 58:1981;773-775.
    • (1981) J. Am. Oil Chem. Soc. , vol.58 , pp. 773-775
    • Kakuda, Y.1    Stanley, D.W.2    Van de Voort, F.R.3
  • 25
    • 0001426346 scopus 로고
    • 31P NMR, and Raman spectroscopic investigation
    • 31P NMR, and Raman spectroscopic investigation. J. Am. Chem. Soc. 102:1980;3144-3148.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 3144-3148
    • Isbrandt, L.R.1    Oertel, R.P.2
  • 26
    • 0026578540 scopus 로고
    • Iron-induced ascorbate oxidation in plasma as monitored by ascorbate free radical formation
    • Minetti M., Forte T., Soriani M., Quaresima V., Menditto A., Ferrari M. Iron-induced ascorbate oxidation in plasma as monitored by ascorbate free radical formation. Biochem. J. 282:1992;459-465.
    • (1992) Biochem. J. , vol.282 , pp. 459-465
    • Minetti, M.1    Forte, T.2    Soriani, M.3    Quaresima, V.4    Menditto, A.5    Ferrari, M.6
  • 27
    • 0027208581 scopus 로고
    • Purification and characterization of two phytases from Escherichia coli
    • Greiner R., Konietzny U., Jany Kl.-D. Purification and characterization of two phytases from Escherichia coli. Arch. Biochem. Biophys. 303:1993;107-113.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 107-113
    • Greiner, R.1    Konietzny, U.2    Jany, Kl.-D.3
  • 28
    • 0026597915 scopus 로고
    • Redox cycling of iron and lipid peroxidation
    • Minotti G., Aust S. D. Redox cycling of iron and lipid peroxidation. Lipids. 27:1992;219-226.
    • (1992) Lipids , vol.27 , pp. 219-226
    • Minotti, G.1    Aust, S.D.2
  • 29
    • 0029866604 scopus 로고    scopus 로고
    • Iron regulatory proteins 1 and 2 bind distinct sets of RNA target sequences
    • Henderson B. R., Menotti E., Kuhn L. C. Iron regulatory proteins 1 and 2 bind distinct sets of RNA target sequences. J. Biol. Chem. 271:1996;4900-4908.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4900-4908
    • Henderson, B.R.1    Menotti, E.2    Kuhn, L.C.3
  • 32
    • 0029610551 scopus 로고
    • Stereospecificity of inositol hexakisphosphate dephosphorylation by Paramecium phytase
    • Van der Kaay J, Van Haastert P. J. M. Stereospecificity of inositol hexakisphosphate dephosphorylation by Paramecium phytase. Biochem. J. 312:1995;907-910.
    • (1995) Biochem. J. , vol.312 , pp. 907-910
    • Van der Kaay, J.1    Van Haastert, P.J.M.2
  • 33
    • 0002449661 scopus 로고
    • Metabolism of inositol phosphates I. Phytase synthesis during germination in cotyledons of mung beans, Phaseolus aureus
    • Mandal N. C., Biswas B. B. Metabolism of inositol phosphates I. Phytase synthesis during germination in cotyledons of mung beans, Phaseolus aureus. Plant Physiol. 45:1970;4-7.
    • (1970) Plant Physiol. , vol.45 , pp. 4-7
    • Mandal, N.C.1    Biswas, B.B.2
  • 34
    • 0015503884 scopus 로고
    • Phytase and alkaline phosphatase activities in intestinal mucosae of rat, chicken, calf, and man
    • Bitar K., Reinhold J. G. Phytase and alkaline phosphatase activities in intestinal mucosae of rat, chicken, calf, and man. Biochim. Biophys. Acta. 268:1972;442-452.
    • (1972) Biochim. Biophys. Acta , vol.268 , pp. 442-452
    • Bitar, K.1    Reinhold, J.G.2
  • 36
    • 0026080005 scopus 로고
    • Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase activity from rat liver and the evaluation of its substrate specificity
    • Nogimori K., Hughes P. J., Glennon M. C., Hodgson M. E., Putney J. W. Jr, Shears S. B. Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase activity from rat liver and the evaluation of its substrate specificity. J. Biol. Chem. 266:1991;16499-16506.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16499-16506
    • Nogimori, K.1    Hughes, P.J.2    Glennon, M.C.3    Hodgson, M.E.4    Putney J.W., Jr.5    Shears, S.B.6
  • 37
    • 0020458827 scopus 로고
    • Purification and properties of phytate-specific phosphatase from Bacillus subtilis
    • Powar V. K., Jagannathan V. Purification and properties of phytate-specific phosphatase from Bacillus subtilis. J. Bacteriol. 151:1982;1102-1108.
    • (1982) J. Bacteriol. , vol.151 , pp. 1102-1108
    • Powar, V.K.1    Jagannathan, V.2
  • 38
    • 0028795109 scopus 로고
    • Effects of aluminum on the hepatic inositol polyphosphate phosphatase
    • Ali N., Craxton A., Sumner M., Shears S. B. Effects of aluminum on the hepatic inositol polyphosphate phosphatase. Biochem. J. 305:1995;557-561.
    • (1995) Biochem. J. , vol.305 , pp. 557-561
    • Ali, N.1    Craxton, A.2    Sumner, M.3    Shears, S.B.4
  • 39
    • 0027463032 scopus 로고
    • Butyrate production from dietary fiber and protection against large bowel cancer in a rat model
    • McIntyre A., Gibson P. R., Young G. P. Butyrate production from dietary fiber and protection against large bowel cancer in a rat model. Gut. 34:1993;386-391.
    • (1993) Gut , vol.34 , pp. 386-391
    • McIntyre, A.1    Gibson, P.R.2    Young, G.P.3
  • 40
    • 0019230294 scopus 로고
    • 14C-phytate in rats: Effect of low and high dietary intakes
    • 14C-phytate in rats: Effect of low and high dietary intakes. J. Nutr. 110:1980;1458-1472.
    • (1980) J. Nutr. , vol.110 , pp. 1458-1472
    • Nahapetian, A.1    Young, V.R.2
  • 41
    • 0027340038 scopus 로고
    • 3H]Phytic acid (inositol hexaphosphate) is absorbed and distributed to various tissues in rats
    • 3H]Phytic acid (inositol hexaphosphate) is absorbed and distributed to various tissues in rats. J. Nutr. 123:1993;713-720.
    • (1993) J. Nutr. , vol.123 , pp. 713-720
    • Sakamoto, K.1    Vucenik, I.2    Shamsuddin, A.M.3
  • 42
    • 0028182572 scopus 로고
    • 3H]-Inositol hexaphosphate (phytic acid) is rapidly absorbed and metabolized by murine and human malignant cells in vitro
    • 3H]-Inositol hexaphosphate (phytic acid) is rapidly absorbed and metabolized by murine and human malignant cells in vitro. J. Nutr. 124:1994;861-868.
    • (1994) J. Nutr. , vol.124 , pp. 861-868
    • Vucenik, I.1    Shamsuddin, A.M.2
  • 43
    • 0023894713 scopus 로고
    • Effect of dietary phytase on the digestion of phytate in the stomach and small intestine of humans
    • Sandberg A.-S., Andersson H. Effect of dietary phytase on the digestion of phytate in the stomach and small intestine of humans. J. Nutr. 118:1988;469-473.
    • (1988) J. Nutr. , vol.118 , pp. 469-473
    • Sandberg, A.-S.1    Andersson, H.2
  • 45
    • 0020808417 scopus 로고
    • Direct demonstration that ferrous ion complexes of di- and triphosphate nucleotides catalyze hydroxyl free radical formation from hydrogen peroxide
    • Floyd R. A. Direct demonstration that ferrous ion complexes of di- and triphosphate nucleotides catalyze hydroxyl free radical formation from hydrogen peroxide. Arch. Biochem. Biophys. 225:1983;263-270.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 263-270
    • Floyd, R.A.1
  • 47
    • 0015045898 scopus 로고
    • Effect of pH on calcium binding by phytic acid and its inositol phosphoric acid derivatives and on the solubility of their calcium salts
    • Kaufman H. W., Kleinberg I. Effect of pH on calcium binding by phytic acid and its inositol phosphoric acid derivatives and on the solubility of their calcium salts. Arch. Oral Biol. 16:1971;445-460.
    • (1971) Arch. Oral Biol. , vol.16 , pp. 445-460
    • Kaufman, H.W.1    Kleinberg, I.2
  • 48
    • 84985287409 scopus 로고
    • Effects of inositol tri-, tetra-, penta-, and hexaphosphates on in vitro estimation of iron availability
    • Sandberg A.-S., Carlsson N.-G., Svanberg U. Effects of inositol tri-, tetra-, penta-, and hexaphosphates on in vitro estimation of iron availability. J. Food Sci. 54:1989;159-161 and 186.
    • (1989) J. Food Sci. , vol.54
    • Sandberg, A.-S.1    Carlsson, N.-G.2    Svanberg, U.3
  • 49
    • 0025082525 scopus 로고
    • Binding of zinc and calcium to inositol phosphates (phytate) in vitro
    • Simpson C. J., Wise A. Binding of zinc and calcium to inositol phosphates (phytate) in vitro. Br. J. Nutr. 64:1990;225-232.
    • (1990) Br. J. Nutr. , vol.64 , pp. 225-232
    • Simpson, C.J.1    Wise, A.2
  • 51
    • 0024598658 scopus 로고
    • Inhibitory effects of phytic acid and other inositol phosphates on zinc and calcium absorption in suckling rats
    • Lonnerdal B., Sandberg A.-S., Sandstrom B., Kunz C. Inhibitory effects of phytic acid and other inositol phosphates on zinc and calcium absorption in suckling rats. J. Nutr. 119:1989;211-214.
    • (1989) J. Nutr. , vol.119 , pp. 211-214
    • Lonnerdal, B.1    Sandberg, A.-S.2    Sandstrom, B.3    Kunz, C.4
  • 52
    • 84986522900 scopus 로고
    • Phytic acid protective effect against beef round muscle lipid peroxidation
    • Lee B. J., Hendricks D. G. Phytic acid protective effect against beef round muscle lipid peroxidation. J. Food Sci. 60:1995;241-244.
    • (1995) J. Food Sci. , vol.60 , pp. 241-244
    • Lee, B.J.1    Hendricks, D.G.2


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