Analysis and Quantitation of Glycated Hemoglobin by Matrix Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry

Hattan, Stephen J.; Parker, Kenneth C.; Vestal, Marvin L.; Yang, Jianping; Herold, David A.; Duncan, Mark W.

doi:10.1007/s13361-015-1316-6

Cited by 24 publications

(3 citation statements)

References 44 publications

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“…In the next logical step, the described analytical strategy was successfully transferred to in vivo glycation systems [ 72 , 79 , 80 , 81 , 82 , 83 ]. Apparently, the changes in overall protein glycation status can be potentially used as diagnostically valuable markers.…”

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

“…Thus, Lapolla and co-workers compared well- and bad-controlled type 2 diabetes mellitus (T2DM) patients with normoglycemic controls in terms of the number of fructosamine residues attached to HSA [ 66 ] and hemoglobin [ 84 ] in blood samples. Remarkably, for analysis of glycated hemoglobin, MALDI-TOF-MS provided a much higher sample throughput in comparison to conventional high-performance liquid chromatography (HPLC)-based protocols [ 79 , 85 ]. Recently, this diagnostic approach was extended to mitochondrial proteins from peripheral blood mononuclear cells [ 86 ].…”

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

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Maillard Proteomics: Opening New Pages

Soboleva

Schmidt

Vikhnina

et al. 2017

IJMS

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Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer’s disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation. It makes characterization of individual glycation sites a critical pre-requisite for understanding in vivo mechanisms of AGE formation and developing adequate nutritional and therapeutic approaches to reduce it in humans. In this context, proteomics is the methodology of choice to address site-specific molecular changes related to protein glycation. Therefore, here we summarize the methods of Maillard proteomics, specifically focusing on the techniques providing comprehensive structural and quantitative characterization of glycated proteome. Further, we address the novel break-through areas, recently established in the field of Maillard research, i.e., in vitro models based on synthetic peptides, site-based diagnostics of metabolism-related diseases (e.g., diabetes mellitus), proteomics of anti-glycative defense, and dynamics of plant glycated proteome during ageing and response to environmental stress.

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Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

Maillard Proteomics: Opening New Pages

Soboleva

Schmidt

Vikhnina

et al. 2017

IJMS

View full text Add to dashboard Cite

show abstract

“…MALDI-ToF MS has also recently been in development for qualitative and quantitative peptide and protein assays. Examples include monoclonal immunoglobulins and serum free light chains,29 42 44 haemoglobin A1c,45 insulin-like growth factor-1,46 multiplex biomarker panel of C reactive protein, serum amyloid A, faecal calprotectin and cystatin C 47…”

Section: Current Clinical Applications Of Ms In Clinical Laboratoriesmentioning

confidence: 99%

Emerging role of clinical mass spectrometry in pathology

et al. 2019

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Mass spectrometry-based assays have been increasingly implemented in various disciplines in clinical diagnostic laboratories for their combined advantages in multiplexing capacity and high analytical specificity and sensitivity. It is now routinely used in areas including reference methods development, therapeutic drug monitoring, toxicology, endocrinology, paediatrics, immunology and microbiology to identify and quantify biomolecules in a variety of biological specimens. As new ionisation methods, instrumentation and techniques are continuously being improved and developed, novel mass spectrometry-based clinical applications will emerge for areas such as proteomics, metabolomics, haematology and anatomical pathology. This review will summarise the general principles of mass spectrometry and specifically highlight current and future clinical applications in anatomical pathology.

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Analysis of Carbohydrates and Glycoconjugates by Matrix‐assisted Laser Desorption/Ionization Mass Spectrometry: An Update for 2015–2016

Harvey

2021

Mass Spectrometry Reviews

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This review is the ninth update of the original article published in 1999 on the application of matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2016. Also included are papers that describe methods appropriate to analysis by MALDI, such as sample preparation techniques, even though the ionization method is not MALDI. Topics covered in the first part of the review include general aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, fragmentation and arrays. The second part of the review is devoted to applications to various structural types such as oligo‐ and poly‐saccharides, glycoproteins, glycolipids, glycosides and biopharmaceuticals. Much of this material is presented in tabular form. The third part of the review covers medical and industrial applications of the technique, studies of enzyme reactions and applications to chemical synthesis. The reported work shows increasing use of combined new techniques such as ion mobility and the enormous impact that MALDI imaging is having. MALDI, although invented over 30 years ago is still an ideal technique for carbohydrate analysis and advancements in the technique and range of applications show no sign of deminishing. © 2020 Wiley Periodicals, Inc.

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Analysis and Quantitation of Glycated Hemoglobin by Matrix Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry

Cited by 24 publications

References 44 publications

Maillard Proteomics: Opening New Pages

Maillard Proteomics: Opening New Pages

Emerging role of clinical mass spectrometry in pathology

Analysis of Carbohydrates and Glycoconjugates by Matrix‐assisted Laser Desorption/Ionization Mass Spectrometry: An Update for 2015–2016

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