Analysis of glycated serum proteins in type 2 diabetes patients with nephropathy
The aim of this study was to screen for proteins that are susceptible to glycation under hyperglycemic conditions in patients with type 2 diabetic nephropathy. Serum proteins were analyzed by a proteomic approach using two-dimensional electrophoresis (2-DE) and ESI-Q-TOF MS/MS. Gels were stained wit...
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Published in | Biotechnology and bioprocess engineering Vol. 19; no. 1; pp. 83 - 92 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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Berlin/Heidelberg
Springer-Verlag
01.02.2014
Springer Berlin Heidelberg Springer Nature B.V 한국생물공학회 |
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Abstract | The aim of this study was to screen for proteins that are susceptible to glycation under hyperglycemic conditions in patients with type 2 diabetic nephropathy. Serum proteins were analyzed by a proteomic approach using two-dimensional electrophoresis (2-DE) and ESI-Q-TOF MS/MS. Gels were stained with Pro-Q Emerald 488 to analyze the serum glycoproteome, followed by silver nitrate to examine the total serum proteome. Patient sera were divided into four groups according to their microalbuminuria index: type 2 diabetics with normoalbuminuria, microalbuminuria, and overt nephropathy, and healthy subjects. When the HbA1c levels of the diabetic groups were examined, groups with higher HbA1c exhibited higher fructosamine levels, suggesting that the loss of glycemic control affected the glycation of serum proteins. The proteins that became glycated under poor glycemic control were PEDF, apolipoprotein J precursor, hemopexin, immunoglobulin mu heavy chain, and immunoglobulin kappa chain. As albuminuria increased, a marker of kidney damage, the levels of glycated prekallikrein and complement factor C4B3 also increased. The glycated proteins identified in this study may provide the foundation for the development of novel markers of diabetes, hyperglycemia, and diabetic complications. |
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AbstractList | The aim of this study was to screen for proteins that are susceptible to glycation under hyperglycemic conditions in patients with type 2 diabetic nephropathy. Serum proteins were analyzed by a proteomic approach using two-dimensional electrophoresis (2-DE) and ESI-Q-TOF MS/MS. Gels were stained with Pro-Q Emerald 488 to analyze the serum glycoproteome, followed by silver nitrate to examine the total serum proteome. Patient sera were divided into four groups according to their microalbuminuria index: type 2 diabetics with normoalbuminuria, microalbuminuria, and overt nephropathy, and healthy subjects. When the HbA1c levels of the diabetic groups were examined, groups with higher HbA1c exhibited higher fructosamine levels, suggesting that the loss of glycemic control affected the glycation of serum proteins. The proteins that became glycated under poor glycemic control were PEDF, apolipoprotein J precursor, hemopexin, immunoglobulin mu heavy chain, and immunoglobulin kappa chain. As albuminuria increased, a marker of kidney damage, the levels of glycated prekallikrein and complement factor C4B3 also increased. The glycated proteins identified in this study may provide the foundation for the development of novel markers of diabetes, hyperglycemia, and diabetic complications. The aim of this study was to screen for proteins that are susceptible to glycation under hyperglycemic conditions in patients with type 2 diabetic nephropathy. Serum proteins were analyzed by a proteomic approach using two-dimensional electrophoresis (2-DE) and ESI-Q-TOF MS/MS. Gels were stained with Pro-Q Emerald 488 to analyze the serum glycoproteome, followed by silver nitrate to examine the total serum proteome. Patient sera were divided into four groups according to their microalbuminuria index: type 2 diabetics with normoalbuminuria, microalbuminuria, and overt nephropathy, and healthy subjects. When the HbA1c levels of the diabetic groups were examined, groups with higher HbA1c exhibited higher fructosamine levels, suggesting that the loss of glycemic control affected the glycation of serum proteins. The proteins that became glycated under poor glycemic control were PEDF, apolipoprotein J precursor, hemopexin, immunoglobulin mu heavy chain, and immunoglobulin kappa chain. As albuminuria increased, a marker of kidney damage, the levels of glycated prekallikrein and complement factor C4B3 also increased. The glycated proteins identified in this study may provide the foundation for the development of novel markers of diabetes, hyperglycemia, and diabetic complications. [PUBLICATION ABSTRACT] The aim of this study was to screen for proteinsthat are susceptible to glycation under hyperglycemicconditions in patients with type 2 diabetic nephropathy. Serum proteins were analyzed by a proteomic approachusing two-dimensional electrophoresis (2-DE) and ESI-QTOFMS/MS. Gels were stained with Pro-Q Emerald 488to analyze the serum glycoproteome, followed by silvernitrate to examine the total serum proteome. Patient serawere divided into four groups according to their microalbuminuriaindex: type 2 diabetics with normoalbuminuria,microalbuminuria, and overt nephropathy, and healthysubjects. When the HbA1c levels of the diabetic groupswere examined, groups with higher HbA1c exhibitedhigher fructosamine levels, suggesting that the loss ofglycemic control affected the glycation of serum proteins. The proteins that became glycated under poor glycemiccontrol were PEDF, apolipoprotein J precursor, hemopexin,immunoglobulin mu heavy chain, and immunoglobulinkappa chain. As albuminuria increased, a marker of kidneydamage, the levels of glycated prekallikrein and complementfactor C4B3 also increased. The glycated proteins identifiedin this study may provide the foundation for the developmentof novel markers of diabetes, hyperglycemia, and diabeticcomplications. KCI Citation Count: 5 |
Author | Yu, Shin-Ae Choi, Kyung Mook Kim, Mi-Ryung Kim, Chan-Wha Kim, Mi-Yeon |
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CitedBy_id | crossref_primary_10_1007_s12010_015_1793_x crossref_primary_10_1007_s12257_014_0184_4 crossref_primary_10_1021_acs_analchem_5b00790 crossref_primary_10_1007_s12257_014_0771_4 crossref_primary_10_2152_jmi_68_76 crossref_primary_10_1155_2016_7934504 |
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SubjectTerms | Apolipoproteins Biomarkers Biomedical research Biotechnology Chemistry Chemistry and Materials Science Chronic illnesses complement Diabetes Diabetic nephropathy electrophoresis gels glycation glycemic control Glycoproteins High density lipoprotein Hyperglycemia Immunoglobulins Industrial and Production Engineering Insulin Kidney diseases kidneys Life sciences Metabolism noninsulin-dependent diabetes mellitus Pathogenesis patients Proteins proteome proteomics Research Paper Silver silver nitrate Studies 생물공학 |
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Title | Analysis of glycated serum proteins in type 2 diabetes patients with nephropathy |
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