메뉴 건너뛰기




Volumn 19, Issue 1, 2014, Pages 83-92

Analysis of glycated serum proteins in type 2 diabetes patients with nephropathy

Author keywords

biomarker; fructosamine; glycation; glycoproteome; type 2 diabetic nephropathy

Indexed keywords

BIOMARKERS; BODY FLUIDS; CHAINS; DISEASES; ELECTROPHORESIS; GLYCOSYLATION;

EID: 84896959576     PISSN: 12268372     EISSN: 19763816     Source Type: Journal    
DOI: 10.1007/s12257-013-0464-4     Document Type: Article
Times cited : (7)

References (43)
  • 1
    • 23744438103 scopus 로고    scopus 로고
    • Diabetes mellitus in the era of proteomics
    • Korc, M. (2003) Diabetes mellitus in the era of proteomics. Mol. Cell Proteomics 2: 399-404.
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 399-404
    • Korc, M.1
  • 2
    • 3142534320 scopus 로고    scopus 로고
    • Evaluation of some biochemical changes in diabetic patients
    • DOI 10.1016/j.cccn.2004.03.030, PII S0009898104001731
    • Abou-Seif, M. A. and A. A. Youssef (2004) Evaluation of some biochemical changes in diabetic patients. Clin. Chim. Acta 346: 161-170. (Pubitemid 38901047)
    • (2004) Clinica Chimica Acta , vol.346 , Issue.2 , pp. 161-170
    • Abou-Seif, M.A.1    Youssef, A.-A.2
  • 3
    • 0029560077 scopus 로고
    • The pathological implications of protein glycation
    • Brownlee, M. (1995) The pathological implications of protein glycation. Clin. Invest. Med. 18: 275-281.
    • (1995) Clin. Invest. Med. , vol.18 , pp. 275-281
    • Brownlee, M.1
  • 4
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. (2001) Biochemistry and molecular cell biology of diabetic complications. Nature 414: 813-820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 5
    • 0032737294 scopus 로고    scopus 로고
    • End-stage renal failure in type 2 diabetes: A medical catastrophe of worldwide dimensions
    • Ritz, E., I. Rychlik, F. Locatelli, and S. Halimi (1999) End-stage renal failure in type 2 diabetes: A medical catastrophe of worldwide dimensions. Am. J. Kidney Dis. 34: 795-808. (Pubitemid 29521694)
    • (1999) American Journal of Kidney Diseases , vol.34 , Issue.5 , pp. 795-808
    • Ritz, E.1    Rychlik, I.2    Locatelli, F.3    Halimi, S.4
  • 7
    • 21344454447 scopus 로고    scopus 로고
    • The early natural history of nephropathy in type 1 diabetes: III. Predictors of 5-year urinary albumin excretion rate patterns in initially normoalbuminuric patients
    • DOI 10.2337/diabetes.54.7.2164
    • Steinke, J. M., A. R. Sinaiko, M. S. Kramer, S. Suissa, B. M. Chavers, M. Mauer and International Diabetic Nephropathy Study Group (2005) The early natural history of nephropathy in Type 1 diabetes: III. Predictors of 5-year urinary albumin excretion rate patterns in initially normoalbuminuric patients. Diabetes 54: 2164-2171. (Pubitemid 40911280)
    • (2005) Diabetes , vol.54 , Issue.7 , pp. 2164-2171
    • Steinke, J.M.1    Sinaiko, A.R.2    Kramer, M.S.3    Suissa, S.4    Chavers, B.M.5    Mauer, M.6
  • 9
    • 11144324314 scopus 로고    scopus 로고
    • Advanced glycation endproducts - Role in pathology of diabetic complications
    • Ahmed, N. (2005) Advanced glycation endproducts - role in pathology of diabetic complications. Diab. Res. Clin. Pract. 67: 3-21.
    • (2005) Diab. Res. Clin. Pract. , vol.67 , pp. 3-21
    • Ahmed, N.1
  • 10
    • 0034003453 scopus 로고    scopus 로고
    • Advanced glycation end products: A Nephrologist's perspective
    • Raj, D. S., D. Choudhury, T. C. Welbourne, and M. Levi (2000) Advanced glycation end products: A Nephrologist's perspective. Am. J. Kidney Dis. 35: 365-380.
    • (2000) Am. J. Kidney Dis. , vol.35 , pp. 365-380
    • Raj, D.S.1    Choudhury, D.2    Welbourne, T.C.3    Levi, M.4
  • 11
    • 0035787070 scopus 로고    scopus 로고
    • Protein glycation, diabetes, and aging
    • Ulrich, P. and A. Cerami (2001) Protein glycation, diabetes, and aging. Recent Prog. Horm. Res. 56: 1-21.
    • (2001) Recent Prog. Horm. Res. , vol.56 , pp. 1-21
    • Ulrich, P.1    Cerami, A.2
  • 12
    • 14644435071 scopus 로고    scopus 로고
    • Identification of amadori-modified plasma proteins in type 2 diabetes and the effect of short-term intensive insulin treatment
    • DOI 10.2337/diacare.28.3.645
    • Jaleel, A., P. Halvatsiotis, B. Williamson, P. Juhasz, S. Martin, and K. S. Nair (2005) Identification of Amadori-modified plasma proteins in type 2 diabetes and the effect of short-term intensive insulin treatment. Diab. Care 28: 645-652. (Pubitemid 40315326)
    • (2005) Diabetes Care , vol.28 , Issue.3 , pp. 645-652
    • Jaleel, A.1    Halvatsiotis, P.2    Willlamson, B.3    Juhasz, P.4    Martin, S.5    Nair, K.S.6
  • 15
    • 26944467179 scopus 로고    scopus 로고
    • New developments in diabetic neuropathy
    • Sullivan, K. A. and E. L. Feldman (2005) New developments in diabetic neuropathy. Curr. Opin. Neurol. 18: 586-590. (Pubitemid 41476148)
    • (2005) Current Opinion in Neurology , vol.18 , Issue.5 , pp. 586-590
    • Sullivan, K.A.1    Feldman, E.L.2
  • 16
    • 0023877704 scopus 로고
    • Fructosamine or glycated haemoglobin as a measure of diabetic control?
    • Allgrove, J. and B. L. Cockrill (1988) Fructosamine or glycated haemoglobin as a measure of diabetic control? Arch. Dis. Child. 63: 418-422.
    • (1988) Arch. Dis. Child. , vol.63 , pp. 418-422
    • Allgrove, J.1    Cockrill, B.L.2
  • 17
    • 52049113492 scopus 로고    scopus 로고
    • Proteomic profiling of nonenzymatically glycated proteins in human plasma and erythrocyte membranes
    • Zhang, Q., N. Tang, A. A. Schepmoes, L. S. Phillips, R. D. Smith, and T. O. Metz (2008) Proteomic profiling of nonenzymatically glycated proteins in human plasma and erythrocyte membranes. J. Proteome Res. 7: 2025-2032.
    • (2008) J. Proteome Res. , vol.7 , pp. 2025-2032
    • Zhang, Q.1    Tang, N.2    Schepmoes, A.A.3    Phillips, L.S.4    Smith, R.D.5    Metz, T.O.6
  • 18
    • 84871196747 scopus 로고    scopus 로고
    • Current status and perspectives of biopharmaceutical drugs
    • Ryu, J. K., H. S. Kim, and D. H. Nam (2012) Current status and perspectives of biopharmaceutical drugs. Biotechnol. Bioproc. Eng. 17: 900-911.
    • (2012) Biotechnol. Bioproc. Eng. , vol.17 , pp. 900-911
    • Ryu, J.K.1    Kim, H.S.2    Nam, D.H.3
  • 19
    • 84871247166 scopus 로고    scopus 로고
    • Investigation of proteomic responses of streptomyces lydicus to pitching ratios for improving streptolydigin production
    • Cheng, J. S., X. M. Lv, and Y. J. Yuan (2012) Investigation of proteomic responses of streptomyces lydicus to pitching ratios for improving streptolydigin production. Biotechnol. Bioproc. Eng. 17: 997-1007.
    • (2012) Biotechnol. Bioproc. Eng. , vol.17 , pp. 997-1007
    • Cheng, J.S.1    Lv, X.M.2    Yuan, Y.J.3
  • 20
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0028061667 scopus 로고
    • Chemistry of the fructosamine assay: D-glucosone is the product of oxidation of Amadori compounds
    • Baker, J. R., D. V. Zyzak, S. R. Thorpe, and J. W. Baynes (1994) Chemistry of the fructosamine assay: D-glucosone is the product of oxidation of Amadori compounds. Clin. Chem. 40: 1950-1955. (Pubitemid 24332701)
    • (1994) Clinical Chemistry , vol.40 , Issue.10 , pp. 1950-1955
    • Baker, J.R.1    Zyzak, D.V.2    Thoroe, S.R.3    Baynes, J.W.4
  • 22
    • 0020655989 scopus 로고
    • Fructosamine: A new approach to the estimation of serum glycosylprotein. An index of diabetic control
    • DOI 10.1016/0009-8981(83)90078-5
    • Johnson, R. N., P. A. Metcalf, and J. R. Baker (1983) Fructosamine: A new approach to the estimation of serum glycosylprotein; An index of diabetic control. Clin. Chim. Acta 127: 87-95. (Pubitemid 13168108)
    • (1983) Clinica Chimica Acta , vol.127 , Issue.1 , pp. 87-95
    • Johnson, R.N.1    Metcalf, P.A.2    Baker, J.R.3
  • 26
    • 84876575266 scopus 로고    scopus 로고
    • Protein glycation in diabetes as determined by mass spectrometry
    • Lapolla, A., L. Molin, and P. Traldi (2013) Protein glycation in diabetes as determined by mass spectrometry. Int. J. Endocrinol. 2013: 11-21.
    • (2013) Int. J. Endocrinol. , vol.2013 , pp. 11-21
    • Lapolla, A.1    Molin, L.2    Traldi, P.3
  • 27
    • 0024394207 scopus 로고
    • Neuronal differentiation of retinoblastoma cells induced by medium conditioned by human RPE cells
    • Tombran-Tink, J. and L. V. Johnson (1989) Neuronal differentiation of retinoblastoma cells induced by medium conditioned by human RPE cells. Invest. Ophthalmol. Vis. Sci. 30: 1700-1707. (Pubitemid 19214990)
    • (1989) Investigative Ophthalmology and Visual Science , vol.30 , Issue.8 , pp. 1700-1707
    • Tombran-Tink, J.1    Johnson, L.V.2
  • 29
    • 77952962984 scopus 로고    scopus 로고
    • Urinary pigment epithelium-derived factor as a marker of diabetic nephropathy
    • Chen, H., Z. Zheng, R. Li, J. Lu, Y. Bao, X. Ying, R. Zeng, and W. Jia (2010) Urinary pigment epithelium-derived factor as a marker of diabetic nephropathy. Am. J. Nephrol. 32: 47-56.
    • (2010) Am. J. Nephrol. , vol.32 , pp. 47-56
    • Chen, H.1    Zheng, Z.2    Li, R.3    Lu, J.4    Bao, Y.5    Ying, X.6    Zeng, R.7    Jia, W.8
  • 31
    • 79959987571 scopus 로고    scopus 로고
    • Comprehensive identification of glycated peptides and their glycation motifs in plasma and erythrocytes of control and diabetic subjects
    • Zhang, Q., M. E. Monroe, A. A. Schepmoes, T. R. W. Clauss, M. A. Gritsenko, D. Meng, V. A. Petyuk, R. D. Smith, and T. O. Metz (2011) Comprehensive identification of glycated peptides and their glycation motifs in plasma and erythrocytes of control and diabetic subjects. J. Proteome Res. 10: 3076-3088.
    • (2011) J. Proteome Res. , vol.10 , pp. 3076-3088
    • Zhang, Q.1    Monroe, M.E.2    Schepmoes, A.A.3    Clauss, T.R.W.4    Gritsenko, M.A.5    Meng, D.6    Petyuk, V.A.7    Smith, R.D.8    Metz, T.O.9
  • 32
    • 0036814405 scopus 로고    scopus 로고
    • Serum levels of the senescence biomarker clusterin/apolipoprotein J increase significantly in diabetes type II and during development of coronary heart disease or at myocardial infarction
    • DOI 10.1016/S0531-5565(02)00139-0, PII S0531556502001390
    • Trougakos, I. P., M. Poulakou, M. Stathatos, A. Chalikia, A. Melidonis, and E. S. Gonos (2002) Serum levels of the senescence biomarker clusterin/apolipoprotein J increase significantly in diabetes type II and during development of coronary heart disease or at myocardial infarction. Exp. Gerontol. 37: 1175-1187. (Pubitemid 35418275)
    • (2002) Experimental Gerontology , vol.37 , Issue.10-11 , pp. 1175-1187
    • Trougakos, I.P.1    Poulakou, M.2    Stathatos, M.3    Chalikia, A.4    Melidonis, A.5    Gonos, E.S.6
  • 33
    • 0242684705 scopus 로고    scopus 로고
    • Plasma prekallikrein: A risk marker for hypertension and nephropathy in type 1 diabetes
    • DOI 10.2337/diabetes.52.5.1215
    • Jaffa, A. A., R. Durazo-Arvizu, D. Zheng, D. T. Lackland, S. Srikanth, W. T. Garvey, and A. H. Schmaier (2003) Plasma prekallikrein: Plasma prekallikrein: A risk marker for hypertension and nephropathy in type 1 diabetes. Diabetes 52: 1215-1221. (Pubitemid 36523359)
    • (2003) Diabetes , vol.52 , Issue.5 , pp. 1215-1221
    • Jaffa, A.A.1    Durazo-Arvizu, R.2    Zheng, D.3    Lackland, D.T.4    Srikanth, S.5    Garvey, W.T.6    Schmaier, A.H.7
  • 34
    • 0029884310 scopus 로고    scopus 로고
    • Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4
    • Herwald, H., T. Renné, J. C. M. Meijers, D. W. Chung, J. D. Page, R. W. Colman, and W. Müller-Esterl (1996) Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4. J. Bio. Chem. 271: 13061-13067.
    • (1996) J. Bio. Chem. , vol.271 , pp. 13061-13067
    • Herwald, H.1    Renné, T.2    Meijers, J.C.M.3    Chung, D.W.4    Page, J.D.5    Colman, R.W.6    Müller-Esterl, W.7
  • 36
    • 0021831741 scopus 로고
    • Relation of gene expression (allotypes) of the fourth component of complement to insulin dependent diabetes and its microangiopathic complications
    • Mijovic, C., J. Fletcher, A. R. Bradwell, T. Harvey, and A. H. Barnett (1985) Relation of gene expression (allotypes) of the fourth component of complement to insulin dependent diabetes and its microangiopathic complications. BMJ 291: 9-10. (Pubitemid 15068792)
    • (1985) British Medical Journal , vol.291 , Issue.6487 , pp. 9-10
    • Mijovic, C.1    Fletcher, J.2    Bradwell, A.R.3
  • 37
    • 73949137622 scopus 로고    scopus 로고
    • Positive association of circulating levels of advanced glycation end products (AGEs) with pigment epithelium-derived factor (PEDF) in a general population
    • Yamagishi, S., T. Matsui, H. Adachi, and M. Takeuchi (2010) Positive association of circulating levels of advanced glycation end products (AGEs) with pigment epithelium-derived factor (PEDF) in a general population. Pharmacol. Res. 61: 103-107.
    • (2010) Pharmacol. Res. , vol.61 , pp. 103-107
    • Yamagishi, S.1    Matsui, T.2    Adachi, H.3    Takeuchi, M.4
  • 38
    • 33746353693 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor (PEDF) prevents diabetes- or advanced glycation end products (AGE)-elicited retinal leukostasis
    • DOI 10.1016/j.mvr.2006.04.002, PII S0026286206000410
    • Yamagishi, S., T. Matsui, K. Nakamura, M. Takeuchi, and T. Imaizumi (2006) Pigment epithelium-derived factor (PEDF) prevents diabetes- or advanced glycation end products (AGE)-elicited retinal leukostasis. Microvasc. Res. 72: 86-90. (Pubitemid 44118388)
    • (2006) Microvascular Research , vol.72 , Issue.1-2 , pp. 86-90
    • Yamagishi, S.-i.1    Matsui, T.2    Nakamura, K.3    Takeuchi, M.4    Imaizumi, T.5
  • 39
    • 0032512650 scopus 로고    scopus 로고
    • Characterization of the human serum trypanosome toxin, haptoglobin- related protein
    • DOI 10.1074/jbc.273.7.3884
    • Muranjan, M., V. Nussenzweig, and S. Tomlinson (1998) Characterization of the human serum Trypanosome toxin, Haptoglobin-related Protein. J. Bio. Chem. 273: 3884-3887. (Pubitemid 28103245)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.7 , pp. 3884-3887
    • Muranjan, M.1    Nussenzweig, V.2    Tomlinson, S.3
  • 41
    • 33947497535 scopus 로고    scopus 로고
    • In vivo and in vitro studies establishing haptoglobin as a major susceptibility gene for diabetic vascular disease
    • Asleh, R. and A. P. Levy (2005) In vivo and in vitro studies establishing haptoglobin as a major susceptibility gene for diabetic vascular disease. Vas Heal. Risk Manag. 1: 19-28.
    • (2005) Vas Heal. Risk Manag. , vol.1 , pp. 19-28
    • Asleh, R.1    Levy, A.P.2
  • 42
    • 54049117269 scopus 로고    scopus 로고
    • Association of haptoglobin phenotypes with markers of diabetic nephropathy in Type 2 diabetes mellitus
    • Samir, M. A., A. S. Suleiman, M. A. S. Qasem, and H. Hisham (2008) Association of haptoglobin phenotypes with markers of diabetic nephropathy in Type 2 diabetes mellitus. J. Diab. Compl. 22: 384-388.
    • (2008) J. Diab. Compl. , vol.22 , pp. 384-388
    • Samir, M.A.1    Suleiman, A.S.2    Qasem, M.A.S.3    Hisham, H.4
  • 43
    • 0032034302 scopus 로고    scopus 로고
    • Non enzymatic glycosylation of Alpha-1-proteinase inhibitor of human plasma
    • Phadke, M., F. R. Billimoria, and V. Ninjoor (1998) Non enzymatic glycosylation of alpha-1-proteinase inhibitor of human plasma. J. Postgrad. Med. 44: 29-34. (Pubitemid 128527755)
    • (1998) Journal of Postgraduate Medicine , vol.44 , Issue.2 , pp. 29-34
    • Phadke, M.1    Billimoria, F.R.2    Ninjoor, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.