메뉴 건너뛰기




Volumn 251, Issue 2, 2011, Pages 104-109

Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3

Author keywords

Chlorotyrosine; Nitrotyrosine; Sulfation; Sulfotransferase; SULT1A3

Indexed keywords

CHLOROTYROSINE SULFATE; NITROTYROSINE SULFATE; SULFOTRANSFERASE; SULFOTRANSFERASE 1A3; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79851511094     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2010.12.006     Document Type: Article
Times cited : (9)

References (44)
  • 1
    • 19644372377 scopus 로고    scopus 로고
    • Cardiovascular effects of secondhand smoke: nearly as large as smoking
    • Barnoya J., Glantz S.A. Cardiovascular effects of secondhand smoke: nearly as large as smoking. Circulation 2005, 111:2684-2698.
    • (2005) Circulation , vol.111 , pp. 2684-2698
    • Barnoya, J.1    Glantz, S.A.2
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0346731060 scopus 로고    scopus 로고
    • Amino acid and protein oxidation in cardiovascular disease
    • Brennan M.L., Hazen S.L. Amino acid and protein oxidation in cardiovascular disease. Amino Acids 2003, 25:365-374.
    • (2003) Amino Acids , vol.25 , pp. 365-374
    • Brennan, M.L.1    Hazen, S.L.2
  • 4
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan M.L., Wu W., Fu X., Shen Z., Song W., Frost H., et al. A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J. Biol. Chem. 2002, 277:17415-17427.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17415-17427
    • Brennan, M.L.1    Wu, W.2    Fu, X.3    Shen, Z.4    Song, W.5    Frost, H.6
  • 5
    • 0037372157 scopus 로고    scopus 로고
    • 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome
    • Buss I.H., Senthilmohan R., Darlow B.A., Mogridge N., Kettle A.J., Winterboum C.C. 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome. Pediatr. Res. 2003, 53:455-462.
    • (2003) Pediatr. Res. , vol.53 , pp. 455-462
    • Buss, I.H.1    Senthilmohan, R.2    Darlow, B.A.3    Mogridge, N.4    Kettle, A.J.5    Winterboum, C.C.6
  • 6
    • 79851508753 scopus 로고    scopus 로고
    • Chlorotyrosine induces endothelial dysfunction in human coronary artery endothelial cells and porcine coronary arteries
    • Chai H., Mohiuddin I., Lin P., Lumsden A., Yao Q., Chen C. Chlorotyrosine induces endothelial dysfunction in human coronary artery endothelial cells and porcine coronary arteries. J. Surg. Res. 2007, 137:174.
    • (2007) J. Surg. Res. , vol.137 , pp. 174
    • Chai, H.1    Mohiuddin, I.2    Lin, P.3    Lumsden, A.4    Yao, Q.5    Chen, C.6
  • 8
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 2002, 82:47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 10
    • 0030996250 scopus 로고    scopus 로고
    • Enzymology of human cytosolic sulfotransferases
    • Falany C.N. Enzymology of human cytosolic sulfotransferases. FASEB J. 1997, 11:206-216.
    • (1997) FASEB J. , vol.11 , pp. 206-216
    • Falany, C.N.1
  • 11
    • 0001853622 scopus 로고
    • Properties of human cytosolic sulfotransferases involved in drug metabolism
    • CRC Press, Boca Raton, FL, E.H. Jeffery (Ed.) Human Drug Metabolism
    • Falany C., Roth J.A. Properties of human cytosolic sulfotransferases involved in drug metabolism. From Molecular Biology to Man 1993, 101-115. CRC Press, Boca Raton, FL. E.H. Jeffery (Ed.).
    • (1993) From Molecular Biology to Man , pp. 101-115
    • Falany, C.1    Roth, J.A.2
  • 15
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos H. Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch. Biochem. Biophys. 1998, 356:1-11.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 16
    • 13244284790 scopus 로고    scopus 로고
    • Pathophysiological functions of nitric oxide-mediated protein modifications
    • Ischiropoulos H., Gow A. Pathophysiological functions of nitric oxide-mediated protein modifications. Toxicology 2005, 208:299-303.
    • (2005) Toxicology , vol.208 , pp. 299-303
    • Ischiropoulos, H.1    Gow, A.2
  • 18
    • 0036146786 scopus 로고    scopus 로고
    • Biomarkers of some pulmonary diseases in exhaled breath
    • Kharitonov S.A., Barnes P.J. Biomarkers of some pulmonary diseases in exhaled breath. Biomarkers 2002, 7:1-32.
    • (2002) Biomarkers , vol.7 , pp. 1-32
    • Kharitonov, S.A.1    Barnes, P.J.2
  • 19
    • 26944469650 scopus 로고    scopus 로고
    • Effects of corticosteroids on noninvasive biomarkers of inflammation in asthma and chronic obstructive pulmonary disease
    • Kharitonov S.A., Barnes P.J. Effects of corticosteroids on noninvasive biomarkers of inflammation in asthma and chronic obstructive pulmonary disease. Proc. Am. Thorac. Soc. 2004, 1:191-199.
    • (2004) Proc. Am. Thorac. Soc. , vol.1 , pp. 191-199
    • Kharitonov, S.A.1    Barnes, P.J.2
  • 20
    • 0001072567 scopus 로고
    • Biological sulfate activation and transfer
    • Lipmann F. Biological sulfate activation and transfer. Science 1958, 128:575-580.
    • (1958) Science , vol.128 , pp. 575-580
    • Lipmann, F.1
  • 21
    • 0021186097 scopus 로고
    • Decrease of tyrosine-O-sulfate-containing proteins found in rat fibroblasts infected with Rous sarcoma virus or Fujinami sarcoma virus
    • Liu M.C., Lipmann F. Decrease of tyrosine-O-sulfate-containing proteins found in rat fibroblasts infected with Rous sarcoma virus or Fujinami sarcoma virus. Proc. Natl Acad. Sci. USA 1984, 81:3695-3698.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3695-3698
    • Liu, M.C.1    Lipmann, F.2
  • 23
    • 3042675247 scopus 로고    scopus 로고
    • Urinary 3-bromotyrosine and 3-chlorotyrosine concentrations in asthmatic patients: lack of increase in 3-bromotyrosine concentration in urine and plasma proteins in aspirin-induced asthma after intravenous aspirin challenge
    • Mita H., Higashi N., Taniguchi M., Higashi A., Kawagishi Y., Akiyama K. Urinary 3-bromotyrosine and 3-chlorotyrosine concentrations in asthmatic patients: lack of increase in 3-bromotyrosine concentration in urine and plasma proteins in aspirin-induced asthma after intravenous aspirin challenge. Clin. Exp. Allergy 2004, 34:931-938.
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 931-938
    • Mita, H.1    Higashi, N.2    Taniguchi, M.3    Higashi, A.4    Kawagishi, Y.5    Akiyama, K.6
  • 24
    • 33646788424 scopus 로고    scopus 로고
    • Nitrotyrosine and chlorotyrosine: clinical significance and biological functions in the vascular system
    • Mohiuddin I., Chai H., Lin P.H., Lumsden A.B., Yao Q., Chen C. Nitrotyrosine and chlorotyrosine: clinical significance and biological functions in the vascular system. J. Surg. Res. 2006, 133:143-149.
    • (2006) J. Surg. Res. , vol.133 , pp. 143-149
    • Mohiuddin, I.1    Chai, H.2    Lin, P.H.3    Lumsden, A.B.4    Yao, Q.5    Chen, C.6
  • 25
    • 0344743071 scopus 로고
    • Sulfation in conjugation reactions
    • Taylor and Francis, London, G.J. Mulder, W.B. Jakoby (Eds.)
    • Mulder G.J., Jakoby W.B. Sulfation in conjugation reactions. Drug Metabolism 1990, 107-161. Taylor and Francis, London. G.J. Mulder, W.B. Jakoby (Eds.).
    • (1990) Drug Metabolism , pp. 107-161
    • Mulder, G.J.1    Jakoby, W.B.2
  • 26
    • 1542345762 scopus 로고    scopus 로고
    • Oxidative DNA damage induced by nitrotyrosine, a biomarker of inflammation
    • Murata M., Kawanishi S. Oxidative DNA damage induced by nitrotyrosine, a biomarker of inflammation. Biochem. Biophys. Res. Commun. 2004, 316:123-128.
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 123-128
    • Murata, M.1    Kawanishi, S.2
  • 27
    • 0037078917 scopus 로고    scopus 로고
    • Differential xenoestrogen-sulfating activities of the human cytosolic sulfotransferases: molecular cloning, expression, and purification of human SULT2B1a and SULT2B1b sulfotransferases
    • Pai T.G., Sugahara T., Suiko M., Sakakibara Y., Xu F., Liu M.C. Differential xenoestrogen-sulfating activities of the human cytosolic sulfotransferases: molecular cloning, expression, and purification of human SULT2B1a and SULT2B1b sulfotransferases. Biochim. Biophys. Acta 2002, 1573:165-170.
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 165-170
    • Pai, T.G.1    Sugahara, T.2    Suiko, M.3    Sakakibara, Y.4    Xu, F.5    Liu, M.C.6
  • 31
    • 70350319524 scopus 로고    scopus 로고
    • Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: the SULT "pie"
    • Riches Z., Stanley E.L., Bloomer J.C., Coughtrie M.W. Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: the SULT "pie". Drug Metab. Dispos. 2009, 37:2255-2261.
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 2255-2261
    • Riches, Z.1    Stanley, E.L.2    Bloomer, J.C.3    Coughtrie, M.W.4
  • 32
    • 0027960877 scopus 로고
    • De novo sulfation of l-tyrosine in HepG2 human hepatoma cells and its possible functional implication
    • Sakakibara Y., Suiko M., Liu M.C. De novo sulfation of l-tyrosine in HepG2 human hepatoma cells and its possible functional implication. Eur. J. Biochem. 1994, 226:293-301.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 293-301
    • Sakakibara, Y.1    Suiko, M.2    Liu, M.C.3
  • 33
    • 0028909149 scopus 로고
    • Sulphation of l-tyrosine in mammalian cells: a comparative study
    • Sakakibara Y., Suiko M., Nakajima H., Liu M.C. Sulphation of l-tyrosine in mammalian cells: a comparative study. Biochem. J. 1995, 305:993-998.
    • (1995) Biochem. J. , vol.305 , pp. 993-998
    • Sakakibara, Y.1    Suiko, M.2    Nakajima, H.3    Liu, M.C.4
  • 34
    • 0031041499 scopus 로고    scopus 로고
    • Manganese-dependent Dopa/tyrosine sulfation in HepG2 human hepatoma cells: novel Dopa/tyrosine sulfotransferase activities associated with the human monoamine-form phenol sulfotransferase
    • Sakakibara Y., Katafuchi J., Takami Y., Nakayama T., Suiko M., Nakajima H., et al. Manganese-dependent Dopa/tyrosine sulfation in HepG2 human hepatoma cells: novel Dopa/tyrosine sulfotransferase activities associated with the human monoamine-form phenol sulfotransferase. Biochim. Biophys. Acta 1997, 1355:102-106.
    • (1997) Biochim. Biophys. Acta , vol.1355 , pp. 102-106
    • Sakakibara, Y.1    Katafuchi, J.2    Takami, Y.3    Nakayama, T.4    Suiko, M.5    Nakajima, H.6
  • 35
    • 0032513046 scopus 로고    scopus 로고
    • Localization and functional analysis of the substrate specificity/catalytic domains of human M-form and P-form phenol sulfotransferases
    • Sakakibara Y., Takami Y., Nakayama T., Suiko M., Liu M.C. Localization and functional analysis of the substrate specificity/catalytic domains of human M-form and P-form phenol sulfotransferases. J. Biol. Chem. 1998, 273:6242-6247.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6242-6247
    • Sakakibara, Y.1    Takami, Y.2    Nakayama, T.3    Suiko, M.4    Liu, M.C.5
  • 36
    • 0032545405 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene
    • Sakakibara Y., Yanagisawa K., Katafuchi J., Ringer D.P., Takami Y., Nakayama T., et al. Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene. J. Biol. Chem. 1998, 273:33929-33935.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33929-33935
    • Sakakibara, Y.1    Yanagisawa, K.2    Katafuchi, J.3    Ringer, D.P.4    Takami, Y.5    Nakayama, T.6
  • 38
    • 0036796816 scopus 로고    scopus 로고
    • Sulfonation and molecular action
    • Strott C.A. Sulfonation and molecular action. Endocr. Rev. 2002, 23:703-732.
    • (2002) Endocr. Rev. , vol.23 , pp. 703-732
    • Strott, C.A.1
  • 39
    • 0030047645 scopus 로고    scopus 로고
    • Enzymic sulphation of dopa and tyrosine isomers by HepG2 human hepatoma cells: stereoselectivity and stimulation by Mn2+
    • Suiko M., Sakakibara Y., Nakajima H., Sakaida H., Liu M.C. Enzymic sulphation of dopa and tyrosine isomers by HepG2 human hepatoma cells: stereoselectivity and stimulation by Mn2+. Biochem. J. 1996, 314:151-158.
    • (1996) Biochem. J. , vol.314 , pp. 151-158
    • Suiko, M.1    Sakakibara, Y.2    Nakajima, H.3    Sakaida, H.4    Liu, M.C.5
  • 40
    • 0343851132 scopus 로고    scopus 로고
    • Sulfation of environmental estrogen-like chemicals by human cytosolic sulfotransferases
    • Suiko M., Sakakibara Y., Liu M.C. Sulfation of environmental estrogen-like chemicals by human cytosolic sulfotransferases. Biochem. Biophys. Res. Commun. 2000, 267:80-84.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 80-84
    • Suiko, M.1    Sakakibara, Y.2    Liu, M.C.3
  • 42
    • 0032062223 scopus 로고    scopus 로고
    • CDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme
    • Yanagisawa K., Sakakibara Y., Suiko M., Takami Y., Nakayama T., Nakajima H., et al. cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci. Biotechnol. Biochem. 1998, 62:1037-1040.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1037-1040
    • Yanagisawa, K.1    Sakakibara, Y.2    Suiko, M.3    Takami, Y.4    Nakayama, T.5    Nakajima, H.6
  • 43
    • 33846540783 scopus 로고    scopus 로고
    • Nitrotyrosine generation and release of nitrotyrosine O-sulfate by HepG2 human hepatoma cells upon SIN-1 stimulation: identification of SULT1A3 as the enzyme responsible
    • Yasuda S., Idell S., Liu M.C. Nitrotyrosine generation and release of nitrotyrosine O-sulfate by HepG2 human hepatoma cells upon SIN-1 stimulation: identification of SULT1A3 as the enzyme responsible. Biochem. J. 2007, 401:497-503.
    • (2007) Biochem. J. , vol.401 , pp. 497-503
    • Yasuda, S.1    Idell, S.2    Liu, M.C.3
  • 44
    • 63849300219 scopus 로고    scopus 로고
    • Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3
    • Yasuda S., Liu M.Y., Suiko M., Sakakibara Y., Liu M.C Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3. J. Neurochem. 2007, 103:2679-2689.
    • (2007) J. Neurochem. , vol.103 , pp. 2679-2689
    • Yasuda, S.1    Liu, M.Y.2    Suiko, M.3    Sakakibara, Y.4    Liu, M.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.