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Volumn 25, Issue 1, 2012, Pages 237-245

Enhanced iron availability by protein glycation may explain higher infection rates in diabetics

Author keywords

Diabetes; Glycation; Iron homeostasisAlbumin; QCM; Siderophores

Indexed keywords

APOENTEROCHELIN; BOVINE SERUM ALBUMIN; ENTEROCHELIN; HOLOENTEROCHELIN; SIDEROPHORE; UNCLASSIFIED DRUG; ADVANCED GLYCATION END PRODUCT; IRON; PROTEIN;

EID: 84859484821     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-011-9492-8     Document Type: Article
Times cited : (7)

References (42)
  • 1
    • 0028857589 scopus 로고
    • Glycation of albumin with aging and diabetes in rats: Changes in its renal handling
    • Bakala H, Verbeke P, Périchon M, Corman B, Schaeverbeke J (1995) Glycation of albumin with aging and diabetes in rats: changes in its renal handling. Mech Ageing Dev 78:63-71
    • (1995) Mech Ageing Dev , vol.78 , pp. 63-71
    • Bakala, H.1    Verbeke, P.2    Périchon, M.3    Corman, B.4    Schaeverbeke, J.5
  • 2
    • 78650250717 scopus 로고    scopus 로고
    • Comparison of modification sites formed on human serum albumin at various stages of glycation
    • Barnaby OS, Cerny RL, Clarke W, Hage DS (2011) Comparison of modification sites formed on human serum albumin at various stages of glycation. Clin Chim Acta 412:277-285
    • (2011) Clin Chim Acta , vol.412 , pp. 277-285
    • Barnaby, O.S.1    Cerny, R.L.2    Clarke, W.3    Hage, D.S.4
  • 3
    • 0032029363 scopus 로고    scopus 로고
    • AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus I
    • Bierhaus A, Hofmann MA, Ziegler R, Nawroth PP (1998) AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus. I. The AGE concept. Cardiovasc Res 37:586-600
    • (1998) The AGE Concept. Cardiovasc Res , vol.37 , pp. 586-600
    • Bierhaus, A.1    Hofmann, M.A.2    Ziegler, R.3    Nawroth, P.P.4
  • 4
    • 0030722201 scopus 로고    scopus 로고
    • Massive glycation of protein HC, a low molecular weight lipocalin, in non-diabetic individuals
    • Bonay P, Solis J, de la Calle H, Fresno M, Grubb A, Méndez E (1997) Massive glycation of protein HC, a low molecular weight lipocalin, in non-diabetic individuals. FEBS Lett 416:276-280
    • (1997) FEBS Lett , vol.416 , pp. 276-280
    • Bonay, P.1    Solis, J.2    De La Calle, H.3    Fresno, M.4    Grubb, A.5    Méndez, E.6
  • 5
    • 0002751446 scopus 로고
    • Harris MI, Cowie CC, Stern MP, Boyko EJ, Reiber GE, Bennett PH (eds) Diabetes in America, 2nd edn. U.S. Govt. Printing Office, Washington, DC(NIH publ. no. 495-1468)
    • Boyko EJ, Lipsky BA (1995) Infection and diabetes. In: Harris MI, Cowie CC, Stern MP, Boyko EJ, Reiber GE, Bennett PH (eds) Diabetes in America, 2nd edn. U.S. Govt. Printing Office, Washington, DC, pp 485-499 (NIH publ. no. 495-1468)
    • (1995) Infection and Diabetes , pp. 485-499
    • Boyko, E.J.1    Lipsky, B.A.2
  • 6
    • 33645111877 scopus 로고    scopus 로고
    • Natural resistance, iron and infection: A challenge for clinical medicine
    • Bullen JJ, Rogers HJ, Spalding PB, Ward CG (2006) Natural resistance, iron and infection: a challenge for clinical medicine. J Med Microbiol 55:251-258
    • (2006) J Med Microbiol , vol.55 , pp. 251-258
    • Bullen, J.J.1    Rogers, H.J.2    Spalding, P.B.3    Ward, C.G.4
  • 7
    • 23844528167 scopus 로고    scopus 로고
    • Community acquired infections in type 2 diabetic patients and their non-diabetic partners: The fremantle diabetes study
    • Davis TME, Weerarathna T, Foong Y, Mason C, Davis WA (2005) Community acquired infections in type 2 diabetic patients and their non-diabetic partners: the fremantle diabetes study. J Diabetes Complicat 19:259-263
    • (2005) J Diabetes Complicat , vol.19 , pp. 259-263
    • Davis, T.M.E.1    Weerarathna, T.2    Foong, Y.3    Mason, C.4    Davis, W.A.5
  • 8
    • 0018395653 scopus 로고
    • Nonenzymatically glucosylated albumin
    • Day JF, Thorpe SR, Baynes JW (1979) Nonenzymatically glucosylated albumin. J Biol Chem 254:595-597
    • (1979) J Biol Chem , vol.254 , pp. 595-597
    • Day, J.F.1    Thorpe, S.R.2    Baynes, J.W.3
  • 9
    • 0019251060 scopus 로고
    • Increased glycosylation of serum albumin in diabetes mellitus
    • Dolhofer R, Wieland OH (1980) Increased glycosylation of serum albumin in diabetes mellitus. Diabetes 29:417-422
    • (1980) Diabetes , vol.29 , pp. 417-422
    • Dolhofer, R.1    Wieland, O.H.2
  • 10
    • 65549156402 scopus 로고    scopus 로고
    • Executive summary: standards of medical care in diabetes- 2009 (2009). Diabetes Care 32:S6-S12
    • (2009) Diabetes Care , vol.32
    • Summary, E.1
  • 11
    • 0017053199 scopus 로고
    • In vitro synthesis of hemoglobin AIc
    • Fluckiger R, Winterhalter KH (1976) In vitro synthesis of hemoglobin AIc. FEBS Lett 71:356-360
    • (1976) FEBS Lett , vol.71 , pp. 356-360
    • Fluckiger, R.1    Winterhalter, K.H.2
  • 12
    • 0028987361 scopus 로고
    • Nonenzymatic glycation of transferrin: Decrease of iron-binding capacity and increase of oxygen radical production
    • Fujimoto S, Kawakami N, Ohara A (1995) Nonenzymatic glycation of transferrin: decrease of iron-binding capacity and increase of oxygen radical production. Bio Pharm Bull 18:396-400
    • (1995) Bio Pharm Bull , vol.18 , pp. 396-400
    • Fujimoto, S.1    Kawakami, N.2    Ohara, A.3
  • 13
    • 0020586544 scopus 로고
    • The principal site of nonenzymatic glycosylation of human serum albumin in vivo
    • Garlick RL, Mazer JS (1983) The principal site of nonenzymatic glycosylation of human serum albumin in vivo. J Biol Chem 258:6142-6146
    • (1983) J Biol Chem , vol.258 , pp. 6142-6146
    • Garlick, R.L.1    Mazer, J.S.2
  • 14
    • 0001569222 scopus 로고
    • Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes
    • Harris WR, Carrano CJ, Cooper SR, Sofen SR, Avdeef AE, McArdle JV, Raymond KN (1979) Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes. J Am Chem Soc 101:6097-6104
    • (1979) J Am Chem Soc , vol.101 , pp. 6097-6104
    • Harris, W.R.1    Carrano, C.J.2    Cooper, S.R.3    Sofen, S.R.4    Avdeef, A.E.5    McArdle, J.V.6    Raymond, K.N.7
  • 15
    • 33745061876 scopus 로고    scopus 로고
    • Site specificity of glycation and carboxymethylation of bovine serum albumin by fructose
    • Hinton DJS, Ames JM (2006) Site specificity of glycation and carboxymethylation of bovine serum albumin by fructose. Amino Acids 30:425-433
    • (2006) Amino Acids , vol.30 , pp. 425-433
    • Hinton, D.J.S.1    Ames, J.M.2
  • 17
    • 0032765645 scopus 로고    scopus 로고
    • A kinetic study of protein binding to ecabet sodium using quartz-crystal microbalance
    • Kawakami K, Yasuda M, Ishii K, Kokusenya Y, Sato T (1999) A kinetic study of protein binding to ecabet sodium using quartz-crystal microbalance. Chem Pharm Bull 47: 919-922
    • (1999) Chem Pharm Bull , vol.47 , pp. 919-922
    • Kawakami, K.1    Yasuda, M.2    Ishii, K.3    Kokusenya, Y.4    Sato, T.5
  • 19
    • 0021265129 scopus 로고
    • Effect of serum albumin on siderophore-mediated utilization of transferrin iron
    • Konopka K, Neilands JB (1984) Effect of serum albumin on siderophore-mediated utilization of transferrin iron. Biochemistry 23:2122-2127
    • (1984) Biochemistry , vol.23 , pp. 2122-2127
    • Konopka, K.1    Neilands, J.B.2
  • 20
    • 24644506128 scopus 로고    scopus 로고
    • Glycosylation of bovine serum albumin with D-[14C]-glucose
    • Kublashvili RI, Ugrekhelidze DS (2005) Glycosylation of bovine serum albumin with D-[14C]-glucose. Chem Nat Comp 41:340-343
    • (2005) Chem Nat Comp , vol.41 , pp. 340-343
    • Kublashvili, R.I.1    Ugrekhelidze, D.S.2
  • 21
    • 0001263746 scopus 로고    scopus 로고
    • Molecular identity and cellular distribution of advanced glycation endproduct receptors: Relationship of p60 to OST-48 and p90 to 80 K-H membrane proteins
    • Li YM, Mitsuhashi T, Wojciechowicz D, Shimizu N, Li J, Stitt A, He C, Banerjee D, Vlassara H (1996) Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80 K-H membrane proteins. Proc Nat Acad Sci USA 93:11047-11052
    • (1996) Proc Nat Acad Sci USA , vol.93 , pp. 11047-11052
    • Li, Y.M.1    Mitsuhashi, T.2    Wojciechowicz, D.3    Shimizu, N.4    Li, J.5    Stitt, A.6    He, C.7    Banerjee, D.8    Vlassara, H.9
  • 22
    • 0020073553 scopus 로고
    • Glucosylated albumin and its influence on salicylate binding
    • Mereish KA, Rosenberg H, Cobby J (1982) Glucosylated albumin and its influence on salicylate binding. J Pharm Sci 71:235-238
    • (1982) J Pharm Sci , vol.71 , pp. 235-238
    • Mereish, K.A.1    Rosenberg, H.2    Cobby, J.3
  • 23
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke M, Marahiel MA (2007) Siderophore-based iron acquisition and pathogen control. Microbiol Mol Biol Rev 71:413-451
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 24
    • 0036252023 scopus 로고    scopus 로고
    • Thermodynamic analysis of human serum albumin interactions with glucose: Insights into diabetic range of glucose concentration
    • Mohamadi-Nejad A, Moosavi-Movahedi AA, Hakimelahi GH, Sheibani N (2002) Thermodynamic analysis of human serum albumin interactions with glucose: insights into diabetic range of glucose concentration. Int J Biochem Cell Biol 34:1115-1124
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1115-1124
    • Mohamadi-Nejad, A.1    Moosavi-Movahedi, A.A.2    Hakimelahi, G.H.3    Sheibani, N.4
  • 25
    • 0041778403 scopus 로고
    • Martell AE, Anderson WF, Badman DG (eds). Elsevier North-Holland, New York
    • Neilands JB (1981) Development of iron chelators for clinical use. In: Martell AE, Anderson WF, Badman DG (eds). Elsevier North-Holland, New York, pp 13-31
    • (1981) Development of Iron Chelators for Clinical Use , pp. 13-31
    • Neilands, J.B.1
  • 27
    • 0028287443 scopus 로고
    • Clark VL, Bavoil PM (eds) Methods in enzymology, bacterial pathogenesis, Part A: identification and regulation of virulence factors, vol 235. Academic Press, Oxford
    • Payne SM (1994) Detection, isolation, and characterization of siderophores. In: Clark VL, Bavoil PM (eds) Methods in enzymology, bacterial pathogenesis, Part A: identification and regulation of virulence factors, vol 235. Academic Press, Oxford, pp 329-344
    • (1994) Detection, Isolation, and Characterization of Siderophores , pp. 329-344
    • Payne, S.M.1
  • 28
    • 33846512288 scopus 로고    scopus 로고
    • Common infections in diabetes: Pathogenesis, management and relationship to glycemic control
    • Peleg AY, Weerarathna T, McCarthy JS, Davis TME (2007) Common infections in diabetes: pathogenesis, management and relationship to glycemic control. Diabetes Metab Res Rev 23:3-13
    • (2007) Diabetes Metab Res Rev , vol.23 , pp. 3-13
    • Peleg, A.Y.1    Weerarathna, T.2    McCarthy, J.S.3    Davis, T.M.E.4
  • 29
    • 84862906830 scopus 로고    scopus 로고
    • National diabetes fact sheet: general information and national estimates on diatebetes in the United States, 2007
    • Prevention CfDCa (2008) National diabetes fact sheet: general information and national estimates on diatebetes in the United States, 2007
    • (2008) Prevention CfDCa
  • 31
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: An archetype for microbial iron transport
    • Raymond KN, Dertz EA, Kim SS (2003) Enterobactin: an archetype for microbial iron transport. Proc Nat Acad Sci USA 100:3584-3588
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 32
    • 25844487822 scopus 로고    scopus 로고
    • The pathogenesis of Staphylococcus aureus infection in the diabetic NOD mouse
    • Rich J, Lee JC (2005) The pathogenesis of Staphylococcus aureus infection in the diabetic NOD mouse. Diabetes 54:2904-2910
    • (2005) Diabetes , vol.54 , pp. 2904-2910
    • Rich, J.1    Lee, J.C.2
  • 33
    • 36449001717 scopus 로고
    • Quartz-crystal microbalance setup for frequency and Q-factor measurements in gaseous and liquid environments
    • Rodahl M, Höök F, Krozer A, Brzezinski P, Kasemo B (1995) Quartz-crystal microbalance setup for frequency and Q-factor measurements in gaseous and liquid environments. Rev Sci Instrum 66:3924-3930
    • (1995) Rev Sci Instrum , vol.66 , pp. 3924-3930
    • Rodahl, M.1    Höök, F.2    Krozer, A.3    Brzezinski, P.4    Kasemo, B.5
  • 34
    • 77649133503 scopus 로고    scopus 로고
    • A review of glycated albumin as an intermediate glycation index for controlling diabetes
    • Roohk HV, Zaidi AR (2008) A review of glycated albumin as an intermediate glycation index for controlling diabetes. J Diabetes Sci Technol 2:1114-1121
    • (2008) J Diabetes Sci Technol , vol.2 , pp. 1114-1121
    • Roohk, H.V.1    Zaidi, A.R.2
  • 35
    • 0842302394 scopus 로고    scopus 로고
    • In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress
    • Roy A, Sen S, Chakraborti AS (2004) In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress. Free Radic Res 38:139-146
    • (2004) Free Radic Res , vol.38 , pp. 139-146
    • Roy, A.1    Sen, S.2    Chakraborti, A.S.3
  • 36
    • 84951279351 scopus 로고
    • Verwendung von schwingquarzen zur wägung dünner schichten und zur mikrowägung
    • Sauerbrey G (1959) Verwendung von schwingquarzen zur wägung dünner schichten und zur mikrowägung. Zeitschrift fü r Physik 155:206-222
    • (1959) Zeitschrift Fü R Physik , vol.155 , pp. 206-222
    • Sauerbrey, G.1
  • 37
    • 11144346788 scopus 로고    scopus 로고
    • Effect of nonenzymatic glycation on functional and structural properties of hemoglobin
    • Sen S, Kar M, Roy A, Chakraborti AS (2005) Effect of nonenzymatic glycation on functional and structural properties of hemoglobin. Biophys Chem 113:289-298
    • (2005) Biophys Chem , vol.113 , pp. 289-298
    • Sen, S.1    Kar, M.2    Roy, A.3    Chakraborti, A.S.4
  • 38
    • 0021365056 scopus 로고
    • Nonenzymatic glycosylation of human serum albumin alters its conformation and function
    • Shaklai N, Garlick RL, Bunn HF (1984) Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J Biol Chem 259:3812-3817
    • (1984) J Biol Chem , vol.259 , pp. 3812-3817
    • Shaklai, N.1    Garlick, R.L.2    Bunn, H.F.3
  • 39
    • 45749110943 scopus 로고    scopus 로고
    • Relationship between free iron and glycated hemoglobin in uncontrolled type 2 diabetes patients associated with complications
    • Shetty JK, Prakash M, Ibrahim MS (2008) Relationship between free iron and glycated hemoglobin in uncontrolled type 2 diabetes patients associated with complications. Ind J Clin Biochem 23:67-70
    • (2008) Ind J Clin Biochem , vol.23 , pp. 67-70
    • Shetty, J.K.1    Prakash, M.2    Ibrahim, M.S.3
  • 40
    • 0024514306 scopus 로고
    • Nonenzymatic glycation of bovine serum albumin by fructose (fructation). Comparison with the Maillard reaction initiated by glucose
    • Suárez G, Rajaram R, Oronsky AL, Gawinowicz MA (1989) Nonenzymatic glycation of bovine serum albumin by fructose (fructation). Comparison with the Maillard reaction initiated by glucose. J Biol Chem 264:3674-3679
    • (1989) J Biol Chem , vol.264 , pp. 3674-3679
    • Suárez, G.1    Rajaram, R.2    Oronsky, A.L.3    Gawinowicz, M.A.4
  • 41
    • 77953621114 scopus 로고    scopus 로고
    • The Maillard reaction in the human body. The main discoveries and factors that affect glycation
    • Tessier FJ (2010) The Maillard reaction in the human body. The main discoveries and factors that affect glycation. Pathol Biol 58:214-219
    • (2010) Pathol Biol , vol.58 , pp. 214-219
    • Tessier, F.J.1
  • 42
    • 0031669171 scopus 로고    scopus 로고
    • Evidence for the importance of catechol-type siderophores in the ironlimited growth of a cyanobacterium
    • Wilhelm SW, MacAuley K, Trick CG (1998) Evidence for the importance of catechol-type siderophores in the ironlimited growth of a cyanobacterium. Limnol Oceanogr 43:992-997
    • (1998) Limnol Oceanogr , vol.43 , pp. 992-997
    • Wilhelm, S.W.1    MacAuley, K.2    Trick, C.G.3


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