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Volumn 378, Issue 2, 2009, Pages 209-212

The formation of argpyrimidine, a methylglyoxal-arginine adduct, in the nucleus of neural cells

Author keywords

Advanced glycation end products; Argpyrimidine; Cerebral cortex; Development; Glyoxalase I; Methylglyoxal; Protein modification

Indexed keywords

ARGININE DERIVATIVE; ARGPYRIMIDINE; LACTOYLGLUTATHIONE LYASE; MESSENGER RNA; METHYLGLYOXAL; UNCLASSIFIED DRUG;

EID: 57049095822     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.11.028     Document Type: Article
Times cited : (24)

References (24)
  • 1
    • 0025298551 scopus 로고
    • The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley P.J. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269 (1990) 1-11
    • (1990) Biochem. J. , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 2
    • 0030176306 scopus 로고    scopus 로고
    • Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification - a role in pathogenesis and antiproliferative chemotherapy
    • Thornalley P.J. Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification - a role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 27 (1996) 565-573
    • (1996) Gen. Pharmacol. , vol.27 , pp. 565-573
    • Thornalley, P.J.1
  • 3
    • 0032703938 scopus 로고    scopus 로고
    • Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications
    • Kalapos M.P. Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications. Toxicol. Lett. 110 (1999) 145-175
    • (1999) Toxicol. Lett. , vol.110 , pp. 145-175
    • Kalapos, M.P.1
  • 4
    • 0029035975 scopus 로고
    • Glyoxalase I in detoxification: studies using a glyoxalase I transfectant cell line
    • Ranganathan S., Walsh E.S., and Tew K.D. Glyoxalase I in detoxification: studies using a glyoxalase I transfectant cell line. Biochem. J. 309 (1995) 127-131
    • (1995) Biochem. J. , vol.309 , pp. 127-131
    • Ranganathan, S.1    Walsh, E.S.2    Tew, K.D.3
  • 5
    • 0028605299 scopus 로고
    • Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin
    • Lo T.W., Westwood M.E., McLellan A.C., Selwood T., and Thornalley P.J. Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin. J. Biol. Chem. 269 (1994) 32299-32305
    • (1994) J. Biol. Chem. , vol.269 , pp. 32299-32305
    • Lo, T.W.1    Westwood, M.E.2    McLellan, A.C.3    Selwood, T.4    Thornalley, P.J.5
  • 7
    • 0037150265 scopus 로고    scopus 로고
    • Rate of formation of AGEs during ascorbate glycation and during aging in human lens tissue
    • Cheng R., Lin B., and Ortwerth B.J. Rate of formation of AGEs during ascorbate glycation and during aging in human lens tissue. Biochim. Biophys. Acta 1587 (2002) 65-74
    • (2002) Biochim. Biophys. Acta , vol.1587 , pp. 65-74
    • Cheng, R.1    Lin, B.2    Ortwerth, B.J.3
  • 8
    • 0033603599 scopus 로고    scopus 로고
    • Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts
    • Oya T., Hattori N., Mizuno Y., Miyata S., Maeda S., Osawa T., and Uchida K. Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J. Biol. Chem. 274 (1999) 18492-18502
    • (1999) J. Biol. Chem. , vol.274 , pp. 18492-18502
    • Oya, T.1    Hattori, N.2    Mizuno, Y.3    Miyata, S.4    Maeda, S.5    Osawa, T.6    Uchida, K.7
  • 10
    • 0031214523 scopus 로고    scopus 로고
    • Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct
    • Shipanova I.N., Glomb M.A., and Nagaraj R.H. Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct. Arch. Biochem. Biophys. 344 (1997) 29-36
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 29-36
    • Shipanova, I.N.1    Glomb, M.A.2    Nagaraj, R.H.3
  • 11
    • 0029165873 scopus 로고
    • Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation end product-modified serum albumins
    • Westwood M.E., and Thornalley P.J. Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation end product-modified serum albumins. J. Protein Chem. 14 (1995) 359-372
    • (1995) J. Protein Chem. , vol.14 , pp. 359-372
    • Westwood, M.E.1    Thornalley, P.J.2
  • 12
    • 23744454602 scopus 로고    scopus 로고
    • Advanced glycation end products in human cancer tissues: detection of N epsilon-(carboxymethyl)lysine and argpyrimidine
    • Van Heijst J.W., Niessen H.W., Hoekman K., and Schalkwijk C.G. Advanced glycation end products in human cancer tissues: detection of N epsilon-(carboxymethyl)lysine and argpyrimidine. Ann. N Y Acad. Sci. 1043 (2005) 725-733
    • (2005) Ann. N Y Acad. Sci. , vol.1043 , pp. 725-733
    • Van Heijst, J.W.1    Niessen, H.W.2    Hoekman, K.3    Schalkwijk, C.G.4
  • 13
    • 0037195845 scopus 로고    scopus 로고
    • Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification
    • Sakamoto H., Mashima T., Yamamoto K., and Tsuruo T. Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification. J. Biol. Chem. 277 (2002) 45770-45775
    • (2002) J. Biol. Chem. , vol.277 , pp. 45770-45775
    • Sakamoto, H.1    Mashima, T.2    Yamamoto, K.3    Tsuruo, T.4
  • 15
    • 7244261872 scopus 로고    scopus 로고
    • Proteomic studies identified a single nucleotide polymorphism in glyoxalase I as autism susceptibility factor
    • Junaid M.A., Kowal D., Barua M., Pullarkat P.S., Sklower B.S., and Pullarkat R.K. Proteomic studies identified a single nucleotide polymorphism in glyoxalase I as autism susceptibility factor. Am. J. Med. Genet. A 131 (2004) 11-17
    • (2004) Am. J. Med. Genet. A , vol.131 , pp. 11-17
    • Junaid, M.A.1    Kowal, D.2    Barua, M.3    Pullarkat, P.S.4    Sklower, B.S.5    Pullarkat, R.K.6
  • 18
    • 12744279337 scopus 로고    scopus 로고
    • Systematic screening and identification of antigens recognized by monoclonal antibodies raised against the developing lateral olfactory tract
    • Kawasaki T., Takagi Y., Yamatani H., and Hirata T. Systematic screening and identification of antigens recognized by monoclonal antibodies raised against the developing lateral olfactory tract. J. Neurobiol. 62 (2005) 330-340
    • (2005) J. Neurobiol. , vol.62 , pp. 330-340
    • Kawasaki, T.1    Takagi, Y.2    Yamatani, H.3    Hirata, T.4
  • 19
    • 0032032578 scopus 로고    scopus 로고
    • Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation end product formation and prevents hyperglycemia-induced increases in macromolecular endocytosis
    • Shinohara M., Thornalley P.J., Giardino I., Beisswenger P., Thorpe S.R., Onorato J., and Brownlee M. Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation end product formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. J. Clin. Invest. 10 (1998) 1142-1147
    • (1998) J. Clin. Invest. , vol.10 , pp. 1142-1147
    • Shinohara, M.1    Thornalley, P.J.2    Giardino, I.3    Beisswenger, P.4    Thorpe, S.R.5    Onorato, J.6    Brownlee, M.7
  • 20
    • 0020549863 scopus 로고
    • Activity changes of glyoxalases I-II and glutathione reductase in regenerating rat liver
    • Principato G.B., Locci P., Rosi G., Talesa V., and Giovannini E. Activity changes of glyoxalases I-II and glutathione reductase in regenerating rat liver. Biochem. Int. 6 (1983) 249-255
    • (1983) Biochem. Int. , vol.6 , pp. 249-255
    • Principato, G.B.1    Locci, P.2    Rosi, G.3    Talesa, V.4    Giovannini, E.5
  • 21
    • 0842305078 scopus 로고    scopus 로고
    • Age-related changes in the glycation of human aortic elastin
    • Konova E., Baydanoff S., Atanasova M., and Velkova A. Age-related changes in the glycation of human aortic elastin. Exp. Gerontol. 39 (2004) 249-254
    • (2004) Exp. Gerontol. , vol.39 , pp. 249-254
    • Konova, E.1    Baydanoff, S.2    Atanasova, M.3    Velkova, A.4
  • 22
    • 0031910005 scopus 로고    scopus 로고
    • The relationship of glycaemic level to advanced glycation end-product (AGE) accumulation and retinal pathology in the spontaneous diabetic hamster
    • Hammes H.P., Wellensiek B., Kloting I., Sickel E., Bretzel R.G., and Brownlee M. The relationship of glycaemic level to advanced glycation end-product (AGE) accumulation and retinal pathology in the spontaneous diabetic hamster. Diabetologia 41 (1998) 165-170
    • (1998) Diabetologia , vol.41 , pp. 165-170
    • Hammes, H.P.1    Wellensiek, B.2    Kloting, I.3    Sickel, E.4    Bretzel, R.G.5    Brownlee, M.6
  • 24
    • 4544374631 scopus 로고    scopus 로고
    • Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis
    • Maeta K., Izawa S., Okazaki S., Kuge S., and Inoue Y. Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis. Mol. Cell Biol. 24 (2004) 8753-8764
    • (2004) Mol. Cell Biol. , vol.24 , pp. 8753-8764
    • Maeta, K.1    Izawa, S.2    Okazaki, S.3    Kuge, S.4    Inoue, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.