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 inBiotechnology and bioprocess engineering Vol. 19; no. 1; pp. 83 - 92
Main Authors Kim, Mi-Ryung, Yu, Shin-Ae, Kim, Mi-Yeon, Choi, Kyung Mook, Kim, Chan-Wha
Format Journal Article
LanguageEnglish
Published 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.
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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SSID ssj0047888
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Snippet 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....
The aim of this study was to screen for proteinsthat are susceptible to glycation under hyperglycemicconditions in patients with type 2 diabetic nephropathy....
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StartPage 83
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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Volume 19
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