Journal article
(Review article)


Analysis of Protein Glycation Products by Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry


Publication Details
Author(s): Kislinger T, Humeny A, Pischetsrieder M
Publisher: Bentham Science Publishers
Publication year: 2004
Volume: 11
Journal issue: 16
Pages range: 2185-2193
ISSN: 0929-8673

Abstract

The term protein glycation summarizes non-enzymatic reactions between amino groups of proteins and sugars or sugar degradation products, leading to early glycation products (intact sugar attached) and advanced glycation end-products (AGEs). Protein glycation is involved in the progression of several diseases, such as diabetes, uremia, and atherosclerosis. However, qualitative and quantitative analysis of in vitro or in vivo glycated proteins is still a challenging task. The introduction of matrix-assisted laser desorption ionization time-of-flight technique (MALDI-TOF) changed mass spectrometry (MS) into a valuable tool for biomedical analysis, because the soft ionization procedure allows the measurement of proteins up to 100 kDa. In the last few years, MALDI-TOF-MS was applied to the investigation of glycation processes: the analyses of plasma proteins from diabetic or uremic patients allowed a precise determination of the average number of sugar residues attached to serum albumin or immunoglobulins of each patient. Thus, a more individualized diagnosis of each patient was achieved by MALDI-TOF-MS than by other diagnostic tools. In a similar way, the glycation rate of hemoglobin, isolated from diabetic blood and of β-2-microglobulin isolated from amyloid plaques from uremic patients was determined. The application of MALDI-TOF-MS for in vitro studies revealed important new insights into glycation mechanisms. Whereas the measurement of the intact proteins allows the determination of the average glycation rate, peptide mapping prior to MALDI-TOF-MS can reveal the exact structures of the glycation products and the glycation site. Furthermore, when the unmodified peptide is used as internal standard, MALDI-TOF-MS can also be used for reliable, site specific relative quantification of defined glycation products. © 2004 Bentham Science Publishers Ltd.



How to cite
APA: Kislinger, T., Humeny, A., & Pischetsrieder, M. (2004). Analysis of Protein Glycation Products by Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry. Current Medicinal Chemistry, 11(16), 2185-2193. https://dx.doi.org/10.2174/0929867043364649

MLA: Kislinger, Thomas, Andreas Humeny, and Monika Pischetsrieder. "Analysis of Protein Glycation Products by Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry." Current Medicinal Chemistry 11.16 (2004): 2185-2193.

BibTeX: Download
Share link
Last updated on 2017-11-20 at 01:32
PDF downloaded successfully