PMID- 28155619
OWN - NLM
STAT- MEDLINE
DCOM- 20190115
LR  - 20240109
IS  - 1875-5305 (Electronic)
IS  - 0929-8665 (Linking)
VI  - 24
IP  - 10
DP  - 2017
TI  - Quantification of Specific Glycation Sites in Human Serum Albumin as Prospective 
      Type 2 Diabetes Mellitus Biomarkers.
PG  - 887-896
LID - 10.2174/0929866524666170202124120 [doi]
AB  - BACKGROUND: Type 2 diabetes mellitus (T2DM) is the most common lifestyle disease 
      affecting all countries. Due to its asymptomatic onset, it is often diagnosed 
      after irreversible vascular complications have been initiated. Therefore, 
      specific markers characteristic for very early disease stages and suitable for 
      early diagnostics are required. Glycation of plasma proteins, such as human serum 
      albumin (HSA), has been often suggested as marker. However, the total glycation 
      degree of HSA does not provide sufficient information about short-term 
      fluctuations of blood glucose concentrations due to the large number of glycation 
      sites. Analysis of individual modification sites might be more informative, but 
      methods for reliable quantifications are still missing. OBJECTIVE: The main 
      objective of this study was to establish and qualify a method of analysis 
      applicable to sensitive and precise quantification of glycations sites in plasma 
      proteins. METHODS: Plasma samples obtained from diabetic patients and 
      non-diseased individuals were separated from low-molecular weight compounds, 
      digested with trypsin, enriched for glycated peptides by boronic acid affinity 
      chromatography (BAC), desalted by solid phase extraction (SPE), and separated by 
      RP-HPLC coupled online to ESI-QqQ-MS. Quantification relied on multiple reaction 
      monitoring (MRM) of multiple glycation sites identified in plasma proteins using 
      a stable isotope dilution approach or internal standardization. RESULTS: The data 
      presented here suggests high selectivity and precision (relative standard 
      deviations below 10%) of the overall approach appearing to be well suited for the 
      identification of prospective biomarkers. Six glycated peptides corresponding to 
      different glycation sites of HSA were present in plasma samples obtained from 
      T2DM patients at significantly higher levels than in non-diabetic men matched for 
      age. Additionally, each of the studied glycation site of HSA appeared to be 
      affected at different degrees. CONCLUSION: The presented approach enables the 
      sensitive and robust quantification of prospective T2D biomarkers promising for 
      clinical diagnostics.
CI  - Copyright(c) Bentham Science Publishers; For any queries, please email at 
      epub@benthamscience.org.
FAU - Spiller, Sandro
AU  - Spiller S
AD  - Institute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, 
      Leipzig University, Leipzig. Germany.
FAU - Frolov, Andrej
AU  - Frolov A
AD  - Institute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, 
      Leipzig University, Leipzig. Germany.
FAU - Hoffmann, Ralf
AU  - Hoffmann R
AD  - Institute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, 
      Leipzig University, Leipzig. Germany.
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Protein Pept Lett
JT  - Protein and peptide letters
JID - 9441434
RN  - 0 (Biomarkers)
RN  - 0 (Boronic Acids)
RN  - 0 (Peptides)
RN  - ZIF514RVZR (Serum Albumin, Human)
SB  - IM
MH  - Binding Sites
MH  - Biomarkers/analysis/metabolism
MH  - Boronic Acids/chemistry
MH  - Diabetes Mellitus, Type 2/*drug therapy/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Peptides/*analysis/chemistry/metabolism
MH  - Prospective Studies
MH  - Protein Binding
MH  - Serum Albumin, Human/*analysis/metabolism
OTO - NOTNLM
OT  - Quantification
OT  - biomarker
OT  - glycation
OT  - multiple reaction monitoring (MRM)
OT  - stable isotope dilution
OT  - type 2 diabetes mellitus (T2DM)
EDAT- 2017/02/06 06:00
MHDA- 2019/01/16 06:00
CRDT- 2017/02/04 06:00
PHST- 2016/11/30 00:00 [received]
PHST- 2017/01/29 00:00 [revised]
PHST- 2017/01/30 00:00 [accepted]
PHST- 2017/02/06 06:00 [pubmed]
PHST- 2019/01/16 06:00 [medline]
PHST- 2017/02/04 06:00 [entrez]
AID - PPL-EPUB-81450 [pii]
AID - 10.2174/0929866524666170202124120 [doi]
PST - ppublish
SO  - Protein Pept Lett. 2017;24(10):887-896. doi: 10.2174/0929866524666170202124120.