Non-enzymatic model glycation reactions — a comprehensive study of the reactivity of a modified arginine with aldehydic and diketonic dicarbonyl compounds by electrospray mass spectrometry

2006 ◽  
Vol 41 (6) ◽  
pp. 755-770 ◽  
Author(s):  
Marco A. Saraiva ◽  
Carlos M. Borges ◽  
M. Helena Florêncio
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Dicarbonyl Compounds ◽  
Enzymatic Model ◽  
Comprehensive Study

Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease

2020 ◽  
Vol 64 (1) ◽  
pp. 97-110
Author(s):  
Christian Sibbersen ◽  
Mogens Johannsen
Keyword(s):  
Mass Spectrometry ◽  
Future Research ◽  
Amino Acid Residues ◽  
Post Translational Modification ◽  
Dicarbonyl Compounds ◽  
Protein Targets ◽  
Post Translational Modifications ◽  
Reactive Protein ◽  
Glycation End Products ◽  
Direct Mass Spectrometry

Abstract In living systems, nucleophilic amino acid residues are prone to non-enzymatic post-translational modification by electrophiles. α-Dicarbonyl compounds are a special type of electrophiles that can react irreversibly with lysine, arginine, and cysteine residues via complex mechanisms to form post-translational modifications known as advanced glycation end-products (AGEs). Glyoxal, methylglyoxal, and 3-deoxyglucosone are the major endogenous dicarbonyls, with methylglyoxal being the most well-studied. There are several routes that lead to the formation of dicarbonyl compounds, most originating from glucose and glucose metabolism, such as the non-enzymatic decomposition of glycolytic intermediates and fructosyl amines. Although dicarbonyls are removed continuously mainly via the glyoxalase system, several conditions lead to an increase in dicarbonyl concentration and thereby AGE formation. AGEs have been implicated in diabetes and aging-related diseases, and for this reason the elucidation of their structure as well as protein targets is of great interest. Though the dicarbonyls and reactive protein side chains are of relatively simple nature, the structures of the adducts as well as their mechanism of formation are not that trivial. Furthermore, detection of sites of modification can be demanding and current best practices rely on either direct mass spectrometry or various methods of enrichment based on antibodies or click chemistry followed by mass spectrometry. Future research into the structure of these adducts and protein targets of dicarbonyl compounds may improve the understanding of how the mechanisms of diabetes and aging-related physiological damage occur.

Analysis of Trace Level Perchlorate in Drinking Water and Ground Water by Electrospray Mass Spectrometry

1998 ◽  
Author(s):  
Rebecca A. Clewell ◽  
Wayne T. Brashear ◽  
David T. Tsui ◽  
Sanwat Chaudhuri ◽  
Rachel S. Cassady
Keyword(s):  
Mass Spectrometry ◽  
Drinking Water ◽  
Ground Water ◽  
Electrospray Mass Spectrometry ◽  
Trace Level

Determination of the endogenous phosphorylation state of B-50/GAP-43 and neurogranin in different brain regions by electrospray mass spectrometry

FEBS Letters ◽  
1996 ◽  
Vol 389 (3) ◽  
pp. 309-313 ◽  
Author(s):  
Monica Di Luca ◽  
Lucia Pastorino ◽  
Vittorio Raverdino ◽  
Pierre N.E. De Graan ◽  
Antonio Caputi ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Brain Regions ◽  
Phosphorylation State

A polymeric microchip with integrated tips and in situ polymerized monolith for electrospray mass spectrometry

Lab on a Chip ◽  
2005 ◽  
Vol 5 (8) ◽  
pp. 869 ◽  
Author(s):  
Yanou Yang ◽  
Chen Li ◽  
Jun Kameoka ◽  
Kelvin H. Lee ◽  
H. G. Craighead
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry
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