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Volumn 25, Issue 5, 2006, Pages 713-723

Mass spectrometry for the study of protein glycation in disease
[No Author Info available]

Author keywords

Cataract; Diabetes; Glycation; Liver cirrhosis; Mass spectrometry; Uremia

Indexed keywords

DESORPTION; DISEASES; HYDROLYSIS; LASER APPLICATIONS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PATIENT TREATMENT; TISSUE;

EID: 33748302108     PISSN: 02777037     EISSN: None     Source Type: Journal    
DOI: 10.1002/mas.20089     Document Type: Article
Times cited : (50)

References (61)
  • 1
    • 22444445653 scopus 로고    scopus 로고
    • Profound mishandling of protein glycation degradation products in uremia and dialysis
    • Agalou S, Ahmed N, Babaei-Jadidi R, Dawnay A, Thornalley PJ. 2005. Profound mishandling of protein glycation degradation products in uremia and dialysis. J Am Soc Nephrol 16:1471-1485.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 1471-1485
    • Agalou, S.1    Ahmed, N.2    Babaei-Jadidi, R.3    Dawnay, A.4    Thornalley, P.J.5
  • 2
    • 0022931516 scopus 로고
    • ε-carboxymethyllysine as a degradation product of fructoselysine in glycated protein
    • ε-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J Biol Chem 261:4889-4894.
    • (1986) J Biol Chem , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 3
    • 0037093522 scopus 로고    scopus 로고
    • Chromatographic assay of glycation adducts in human serum albumin glycated in vitro by derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl- carbamate and intrinsic fluorescence
    • Ahmed N, Thornalley PJ. 2002. Chromatographic assay of glycation adducts in human serum albumin glycated in vitro by derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and intrinsic fluorescence. Biochem J 364(Pt 1): 15-24.
    • (2002) Biochem J , vol.364 , Issue.1 PART , pp. 15-24
    • Ahmed, N.1    Thornalley, P.J.2
  • 4
    • 0030919275 scopus 로고    scopus 로고
    • ε-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins
    • ε-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem J 324:565-570.
    • (1997) Biochem J , vol.324 , pp. 565-570
    • Ahmed, M.U.1    Brinkmann Frye, E.2    Degenhardt, T.P.3    Thorpe, S.R.4    Baynes, J.W.5
  • 8
    • 22444447985 scopus 로고    scopus 로고
    • Degradation products of proteins damaged by glycation, oxidation and nitration in clinical type 1 diabetes
    • Ahmed N, Babaei-Jadidi R, Howell SK, Beisswenger PJ, Thornalley PJ. 2005b. Degradation products of proteins damaged by glycation, oxidation and nitration in clinical type 1 diabetes. Diabetologia 48: 1590-1603.
    • (2005) Diabetologia , vol.48 , pp. 1590-1603
    • Ahmed, N.1    Babaei-Jadidi, R.2    Howell, S.K.3    Beisswenger, P.J.4    Thornalley, P.J.5
  • 9
    • 0036237275 scopus 로고    scopus 로고
    • The Maillard hypothesis on aging: Time to focus on DNA
    • Baynes JW. 2002. The Maillard hypothesis on aging: Time to focus on DNA. Ann NY Acad Sci 959:360-367.
    • (2002) Ann NY Acad Sci , vol.959 , pp. 360-367
    • Baynes, J.W.1
  • 10
    • 0034659178 scopus 로고    scopus 로고
    • Glycoxidation and lipoxidation in atherogenesis
    • Baynes JW, Thorpe SR. 2000. Glycoxidation and lipoxidation in atherogenesis. Free Radic Biol Med 28:1708-1716.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1708-1716
    • Baynes, J.W.1    Thorpe, S.R.2
  • 11
    • 0037067723 scopus 로고    scopus 로고
    • Identification and quantification of major Maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound
    • Biemel KM, Friedl DA, Lederer MO. 2002. Identification and quantification of major Maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound. J Biol Chem 277: 24907-24915.
    • (2002) J Biol Chem , vol.277 , pp. 24907-24915
    • Biemel, K.M.1    Friedl, D.A.2    Lederer, M.O.3
  • 12
    • 0000571086 scopus 로고
    • Modification of DNA by reducing sugars: A possible mechanism for nucleic acid aging and age-related dysfunction in gene expression
    • Bucala R, Model P, Cerami A. 1984. Modification of DNA by reducing sugars: A possible mechanism for nucleic acid aging and age-related dysfunction in gene expression. Proc Natl Acad Sci USA 81:105-109.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 105-109
    • Bucala, R.1    Model, P.2    Cerami, A.3
  • 15
    • 0032563120 scopus 로고    scopus 로고
    • Role of the Maillard reaction in aging of tissue proteins. Advanced glycation end product-dependent increase in imidazolium cross-links in human lens proteins
    • Frye EB, Degenhardt TP, Thorpe SR, Baynes JW. 1998. Role of the Maillard reaction in aging of tissue proteins. Advanced glycation end product-dependent increase in imidazolium cross-links in human lens proteins. J Biol Chem 273:18714-18719.
    • (1998) J Biol Chem , vol.273 , pp. 18714-18719
    • Frye, E.B.1    Degenhardt, T.P.2    Thorpe, S.R.3    Baynes, J.W.4
  • 16
    • 0037174437 scopus 로고    scopus 로고
    • Analysis of glycated and ascorbylated proteins by gas chromatography-mass spectrometry
    • Hasenkopf K, Ronner B, Hiller H, Pischetsrieder M. 2002. Analysis of glycated and ascorbylated proteins by gas chromatography-mass spectrometry. J Agric Food Chem 50:5697-5703.
    • (2002) J Agric Food Chem , vol.50 , pp. 5697-5703
    • Hasenkopf, K.1    Ronner, B.2    Hiller, H.3    Pischetsrieder, M.4
  • 17
    • 0024511940 scopus 로고
    • Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo
    • Hayase F, Nagaraj RH, Miyata S, Njoroge FG, Monnier VM. 1989. Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo. J Biol Chem 264:3758-3764.
    • (1989) J Biol Chem , vol.264 , pp. 3758-3764
    • Hayase, F.1    Nagaraj, R.H.2    Miyata, S.3    Njoroge, F.G.4    Monnier, V.M.5
  • 18
    • 0037181327 scopus 로고    scopus 로고
    • Qualitative determination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry Peptide mapping
    • Humeny A, Kislinger T, Becker CM, Pischetsrieder M. 2002. Qualitative determination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry Peptide mapping. J Agric Food Chem 50:2153-2160.
    • (2002) J Agric Food Chem , vol.50 , pp. 2153-2160
    • Humeny, A.1    Kislinger, T.2    Becker, C.M.3    Pischetsrieder, M.4
  • 20
    • 0034176220 scopus 로고    scopus 로고
    • ω-carboxymethylarginine as a novel acid-labileadvanced glycation end product in collagen
    • ω-carboxymethylarginine as a novel acid-labileadvanced glycation end product in collagen. Biochem J 347:23-27.
    • (2000) Biochem J , vol.347 , pp. 23-27
    • Iijima, K.1    Murata, M.2    Takahara, H.3    Irie, S.4    Fujimoto, D.5
  • 21
    • 0348049805 scopus 로고    scopus 로고
    • Accumulation of fructosyl-lysine and advanced glycation end products in the kidney, retina and peripheral nerve of streptozotocin-induced diabetic rats
    • Karachalias N, Babaei-Jadidi R, Ahmed N, Thornalley PJ. 2003. Accumulation of fructosyl-lysine and advanced glycation end products in the kidney, retina and peripheral nerve of streptozotocin-induced diabetic rats. Biochem Soc Trans 31:1423-1425.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1423-1425
    • Karachalias, N.1    Babaei-Jadidi, R.2    Ahmed, N.3    Thornalley, P.J.4
  • 22
    • 3242770754 scopus 로고    scopus 로고
    • Analysis of protein glycation products by matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • Kislinger T, Humeny A, Pischetsrieder M. 2004. Analysis of protein glycation products by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Curr Med Chem 11:2185-2193.
    • (2004) Curr Med Chem , vol.11 , pp. 2185-2193
    • Kislinger, T.1    Humeny, A.2    Pischetsrieder, M.3
  • 28
    • 0034582197 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry, enzymatic digestion, and molecular modeling in the study of nonenzymatic glycation of IgG
    • Lapolla A, Fedele D, Garbeglio M, Martano L, Tonani R, Seraglia R, Favretto D, Fedrigo MA, Traldi P. 2000. Matrix-assisted laser desorption/ionization mass spectrometry, enzymatic digestion, and molecular modeling in the study of nonenzymatic glycation of IgG. J Am Soc Mass Spectrom 11:153-159.
    • (2000) J Am Soc Mass Spectrom , vol.11 , pp. 153-159
    • Lapolla, A.1    Fedele, D.2    Garbeglio, M.3    Martano, L.4    Tonani, R.5    Seraglia, R.6    Favretto, D.7    Fedrigo, M.A.8    Traldi, P.9
  • 37
    • 0037295407 scopus 로고    scopus 로고
    • Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides
    • Marotta E, Lapolla A, Fedele D, Senesi A, Reitano R, Witt M, Seraglia R, Traldi P. 2003. Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides. J Mass Spectrom 38:196-205.
    • (2003) J Mass Spectrom , vol.38 , pp. 196-205
    • Marotta, E.1    Lapolla, A.2    Fedele, D.3    Senesi, A.4    Reitano, R.5    Witt, M.6    Seraglia, R.7    Traldi, P.8
  • 39
    • 0347065359 scopus 로고    scopus 로고
    • Glycation and post-translational processing of human interferon-γ expressed in Escherichia coli
    • Mironova R, Niwa T, Dimitrova R, Boyanova M, Ivanov I. 2003. Glycation and post-translational processing of human interferon-γ expressed in Escherichia coli. J Biol Chem 278:51068-51074.
    • (2003) J Biol Chem , vol.278 , pp. 51068-51074
    • Mironova, R.1    Niwa, T.2    Dimitrova, R.3    Boyanova, M.4    Ivanov, I.5
  • 40
    • 0037073688 scopus 로고    scopus 로고
    • Identification in human atherosclerotic lesions of GA-pyridine, a novel structure derived from glycolaldehyde-modified proteins
    • Nagai R, Hayashi CM, Xia L, Takeya M, Horiuchi S. 2002. Identification in human atherosclerotic lesions of GA-pyridine, a novel structure derived from glycolaldehyde-modified proteins. J Biol Chem 277:48905-48912.
    • (2002) J Biol Chem , vol.277 , pp. 48905-48912
    • Nagai, R.1    Hayashi, C.M.2    Xia, L.3    Takeya, M.4    Horiuchi, S.5
  • 41
    • 0031555853 scopus 로고    scopus 로고
    • Acid-stable fluorescent advanced glycation end products: Vesperlysines A, B, and C are formed as crosslinked products in the Maillard reaction between lysine or proteins with glucose
    • Nakamura K, Nakazawa Y, Ienaga K. 1997. Acid-stable fluorescent advanced glycation end products: Vesperlysines A, B, and C are formed as crosslinked products in the Maillard reaction between lysine or proteins with glucose. Biochem Biophys Res Commun 232:227-230.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 227-230
    • Nakamura, K.1    Nakazawa, Y.2    Ienaga, K.3
  • 42
    • 21644441968 scopus 로고    scopus 로고
    • Pyridoxal phosphate and hepatocyte growth factor prevent dialysate-induced peritoneal damage
    • Nakamura S, Niwa T. 2005. Pyridoxal phosphate and hepatocyte growth factor prevent dialysate-induced peritoneal damage. J Am Soc Nephrol 16:144-150.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 144-150
    • Nakamura, S.1    Niwa, T.2
  • 43
    • 0031265505 scopus 로고    scopus 로고
    • Mass spectrometry in the search for uremic toxins
    • Niwa T. 1997c. Mass spectrometry in the search for uremic toxins. Mass Spectrom Rev 16:307-332.
    • (1997) Mass Spectrom Rev , vol.16 , pp. 307-332
    • Niwa, T.1
  • 44
    • 0032808026 scopus 로고    scopus 로고
    • 3-Deoxyglucosone: Metabolism, analysis, biological activity and clinical implication
    • Niwa T. 1999. 3-Deoxyglucosone: Metabolism, analysis, biological activity and clinical implication. J Chromatogr 731:23-36.
    • (1999) J Chromatogr , vol.731 , pp. 23-36
    • Niwa, T.1
  • 45
    • 0035122180 scopus 로고    scopus 로고
    • 3-deoxyglucosone and AGEs in uremic complications: Inactivation of glutathione peroxidase by 3-deoxyglucosone
    • Niwa T, Tsukushi S. 2001. 3-deoxyglucosone and AGEs in uremic complications: Inactivation of glutathione peroxidase by 3-deoxyglucosone. Kidney Int 59(Suppl 78):S37-S41.
    • (2001) Kidney Int , vol.59 , Issue.78 SUPPL.
    • Niwa, T.1    Tsukushi, S.2
  • 48
    • 0030901310 scopus 로고    scopus 로고
    • Immunohistochemical detection of imidazolone, a novel advanced glycation end product, in kidneys and aortas of diabetic patients
    • Niwa T, Katsuzaki T, Miyazaki S, Miyazaki T, Ishizaki Y, Hayase F, Tatemichi N, Takei Y. 1997a. Immunohistochemical detection of imidazolone, a novel advanced glycation end product, in kidneys and aortas of diabetic patients. J Clin Invest 99:1272-1280.
    • (1997) J Clin Invest , vol.99 , pp. 1272-1280
    • Niwa, T.1    Katsuzaki, T.2    Miyazaki, S.3    Miyazaki, T.4    Ishizaki, Y.5    Hayase, F.6    Tatemichi, N.7    Takei, Y.8
  • 49
    • 0030987873 scopus 로고    scopus 로고
    • Imidazolone, a novel advanced glycation end product, is present at high levels in kidneys of rats with streptozotocin-induced diabetes
    • Niwa T, Katsuzaki T, Ishizaki Y, Hayase F, Miyazaki T, Uematsu T, Tatemichi N, Takei Y. 1997b. Imidazolone, a novel advanced glycation end product, is present at high levels in kidneys of rats with streptozotocin- induced diabetes. FEBS Lett 407:297-302.
    • (1997) FEBS Lett , vol.407 , pp. 297-302
    • Niwa, T.1    Katsuzaki, T.2    Ishizaki, Y.3    Hayase, F.4    Miyazaki, T.5    Uematsu, T.6    Tatemichi, N.7    Takei, Y.8
  • 50
    • 0032523822 scopus 로고    scopus 로고
    • Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: Evidence for increased oxidative stress in uremia
    • Odani H, Shinzato T, Usami J, Matsumoto Y, Brinkmann Frye E, Baynes JW, Maeda K. 1998. Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: Evidence for increased oxidative stress in uremia. FEBS Lett 427:381-385.
    • (1998) FEBS Lett , vol.427 , pp. 381-385
    • Odani, H.1    Shinzato, T.2    Usami, J.3    Matsumoto, Y.4    Brinkmann Frye, E.5    Baynes, J.W.6    Maeda, K.7
  • 52
    • 0028310848 scopus 로고
    • Immunological quantification of advanced glycosylation end-products in the serum of patients on hemodialysis or CAPD
    • Papanastasiou P, Grass L, Rodela H, Patrikarea A, Oreopoulos D, Diamandis EP. 1994. Immunological quantification of advanced glycosylation end-products in the serum of patients on hemodialysis or CAPD. Kidney Int 46:216-222.
    • (1994) Kidney Int , vol.46 , pp. 216-222
    • Papanastasiou, P.1    Grass, L.2    Rodela, H.3    Patrikarea, A.4    Oreopoulos, D.5    Diamandis, E.P.6
  • 54
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process
    • Sell DR, Monnier VM. 1989. Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. J Biol Chem 264:21597-21602.
    • (1989) J Biol Chem , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 55
    • 0031214523 scopus 로고    scopus 로고
    • Protein modification by methylglyoxal: Chemical nature and synthetic mechanism of a major fluorescent adduct
    • Shipanova IN, Glomb MA, Nagaraj RH. 1997. Protein modification by methylglyoxal: Chemical nature and synthetic mechanism of a major fluorescent adduct. Arch Biochem Biophys 344:29-36.
    • (1997) Arch Biochem Biophys , vol.344 , pp. 29-36
    • Shipanova, I.N.1    Glomb, M.A.2    Nagaraj, R.H.3
  • 56
    • 0032197143 scopus 로고    scopus 로고
    • Characterisation of a novel AGE-compound derived from lysine and 3-deoxyglucosone
    • Skovsted IC, Christensen M, Breinholt J, Mortensen SB. 1998. Characterisation of a novel AGE-compound derived from lysine and 3-deoxyglucosone. Cell Mol Biol 44:1159-1163.
    • (1998) Cell Mol Biol , vol.44 , pp. 1159-1163
    • Skovsted, I.C.1    Christensen, M.2    Breinholt, J.3    Mortensen, S.B.4
  • 57
    • 3042523379 scopus 로고    scopus 로고
    • ε-(carboxyethyl)lysine in human plasma protein by stable-isotope-dilution tandem mass spectrometry
    • ε-(carboxyethyl) lysine in human plasma protein by stable-isotope-dilution tandem mass spectrometry. Clin Chem 50:1222-1228.
    • (2004) Clin Chem , vol.50 , pp. 1222-1228
    • Teerlink, T.1    Barto, R.2    Ten Brink, H.J.3    Schalkwijk, C.G.4
  • 58
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • Thornalley PJ, Langborg A, Minhas HS. 1999. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 344:109-116.
    • (1999) Biochem J , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 60
    • 0242468729 scopus 로고    scopus 로고
    • Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry
    • Thornalley PJ, Battah S, Ahmed N, Karachalias N, Agalou S, Babaei-Jadidi R, Dawnay A. 2003. Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry. Biochem J 375:581-592.
    • (2003) Biochem J , vol.375 , pp. 581-592
    • Thornalley, P.J.1    Battah, S.2    Ahmed, N.3    Karachalias, N.4    Agalou, S.5    Babaei-Jadidi, R.6    Dawnay, A.7
  • 61


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