Research output: Contribution to journal › Article › peer-review
A Snapshot of the Plant Glycated Proteome : STRUCTURAL, FUNCTIONAL, AND MECHANISTIC ASPECTS. / Bilova, T.; Lukasheva, E.; Brauch, D.; Greifenhagen, U.; Paudel, G.; Tarakhovskaya, E.; Frolova, N.; Mittasch, J.; Balcke, G.U.; Tissier, A.; Osmolovskaya, N.; Vogt, T.; Wessjohann, L.A.; Birkemeyer, C.; Milkowski, C.; Frolov, A.
In: Journal of Biological Chemistry, Vol. 291, No. 14, 2016, p. 7621-7636.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - A Snapshot of the Plant Glycated Proteome
T2 - STRUCTURAL, FUNCTIONAL, AND MECHANISTIC ASPECTS
AU - Bilova, T.
AU - Lukasheva, E.
AU - Brauch, D.
AU - Greifenhagen, U.
AU - Paudel, G.
AU - Tarakhovskaya, E.
AU - Frolova, N.
AU - Mittasch, J.
AU - Balcke, G.U.
AU - Tissier, A.
AU - Osmolovskaya, N.
AU - Vogt, T.
AU - Wessjohann, L.A.
AU - Birkemeyer, C.
AU - Milkowski, C.
AU - Frolov, A.
N1 - © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2016
Y1 - 2016
N2 - Glycation is the reaction of carbonyl compounds (reducing sugars and α-dicarbonyls) with amino acids, lipids, and proteins, yielding early and advanced glycation end products (AGEs). The AGEs can be formed via degradation of early glycation intermediates (glycoxidation) and by interaction with the products of monosaccharide autoxidation (autoxidative glycosylation). Although formation of these potentially deleterious compounds is well characterized in animal systems and thermally treated foods, only a little information about advanced glycation in plants is available. Thus, the knowledge of the plant AGE patterns and the underlying pathways of their formation are completely missing. To fill this gap, we describe the AGE-modified proteome ofBrassica napusand characterize individual sites of advanced glycation by the methods of liquid chromatography-based bottom-up proteomics. The modification patterns were complex but reproducible: 789 AGE-modified peptides in 772 proteins were detected in two independent experiments. In contrast, only 168 polypeptides contained early glycated lysines, which did not resemble the sites of advanced glycation. Similar observations were made withArabidopsis thaliana The absence of the early glycated precursors of the AGE-modified protein residues indicated autoxidative glycosylation, but not glycoxidation, as the major pathway of AGE formation. To prove this assumption and to identify the potential modifying agents, we estimated the reactivity and glycative potential of plant-derived sugars using a model peptide approach and liquid chromatography-mass spectrometry-based techniques. Evaluation of these data sets together with the assessed tissue carbohydrate contents revealed dihydroxyacetone phosphate, glyceraldehyde 3-phosphate, ribulose, erythrose, and sucrose as potential precursors of plant AGEs.
AB - Glycation is the reaction of carbonyl compounds (reducing sugars and α-dicarbonyls) with amino acids, lipids, and proteins, yielding early and advanced glycation end products (AGEs). The AGEs can be formed via degradation of early glycation intermediates (glycoxidation) and by interaction with the products of monosaccharide autoxidation (autoxidative glycosylation). Although formation of these potentially deleterious compounds is well characterized in animal systems and thermally treated foods, only a little information about advanced glycation in plants is available. Thus, the knowledge of the plant AGE patterns and the underlying pathways of their formation are completely missing. To fill this gap, we describe the AGE-modified proteome ofBrassica napusand characterize individual sites of advanced glycation by the methods of liquid chromatography-based bottom-up proteomics. The modification patterns were complex but reproducible: 789 AGE-modified peptides in 772 proteins were detected in two independent experiments. In contrast, only 168 polypeptides contained early glycated lysines, which did not resemble the sites of advanced glycation. Similar observations were made withArabidopsis thaliana The absence of the early glycated precursors of the AGE-modified protein residues indicated autoxidative glycosylation, but not glycoxidation, as the major pathway of AGE formation. To prove this assumption and to identify the potential modifying agents, we estimated the reactivity and glycative potential of plant-derived sugars using a model peptide approach and liquid chromatography-mass spectrometry-based techniques. Evaluation of these data sets together with the assessed tissue carbohydrate contents revealed dihydroxyacetone phosphate, glyceraldehyde 3-phosphate, ribulose, erythrose, and sucrose as potential precursors of plant AGEs.
KW - Brassica napus/genetics
KW - Glycoproteins/genetics
KW - Glycosylation
KW - Plant Proteins/genetics
KW - Proteome/genetics
KW - Proteomics
UR - http://www.jbc.org/content/early/2016/01/19/jbc.M115.678581.short http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84971367754&origin=inward
U2 - 10.1074/jbc.M115.678581
DO - 10.1074/jbc.M115.678581
M3 - Article
C2 - 26786108
VL - 291
SP - 7621
EP - 7636
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 14
ER -
ID: 7554227