PXD006434

PXD006434 is an original dataset announced via ProteomeXchange.

Title	Advanced glycation end products as markers of ageing in plants: glycation hotspots in the plant proteome
Description	Glycation is a post-translational modification underlied by the interaction of protein amino and guanidino groups with carbonyl compounds like reducing sugars and α-dicarbonyls. In the first steps of this process, the protein amino groups react with reducing carbohydrates yielding the corresponding keto- and aldimines, i.e. Amadori and Heyns compounds, respectively. Further degradation of these products results in the formation of advanced glycation end products (AGEs). Alternatively, some representatives of this heterogeneous compound group can originate from α-dicarbonyl products of monosaccharide autoxidation or primary cellular metabolism. In mammals, AGEs are continuously formed during the life of the organism, and accumulate in the tissues, being well-known markers of ageing and impacting age-related stiffing of tissues, decrease of muscle performance, and atherosclerotic changes. However, although the role of AGEs in the ageing of animal tissues is well-studied, their impact in the age-related molecular alterations in plants is completely unknown. To fill this gap, we present here a comprehensive study of the age-related changes in the plant glycated proteome in terms of affected proteins and individual glycation sites therein. Thereby, we consider the qualitative and quantitative changes in glycation patterns in terms of the general metabolic background, pathways of AGE formation, and the status of plant anti-oxidative/anti-glycative defense. Although the patterns of glycated proteins were only minimally influenced by plant age, the abundances of 96 advanced glycation sites in 71 proteins were significantly affected in an age-dependent manner and clearly indicate the existence of glycation hotspots in the plant proteome, the nature of which is discussed here in the sense of structural considerations.
HostingRepository	PRIDE
AnnounceDate	2017-06-19
AnnouncementXML	Submission_2017-06-19_01:34:45.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nikita Shilyaev
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	dihydroxylated residue; N6-carboxymethyl-L-lysine; carboxylated residue; hexose glycated L-lysine; monohydroxylated residue; acetylated residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2017-05-03 02:24:01	ID requested
⏵ 1	2017-06-19 01:34:46	announced

Bilova T, Paudel G, Shilyaev N, Schmidt R, Brauch D, Tarakhovskaya E, Milrud S, Smolikova G, Tissier A, Vogt T, Sinz A, Brandt W, Birkemeyer C, Wessjohann LA, Frolov A, proteome provides evidence for age-related glycation hot spots. J Biol Chem, 292(38):15758-15776(2017) [pubmed]

curator keyword: Biological

submitter keyword: Glycation, AGEs, Plant Proteomics

Dr. Andrej Frolov
contact affiliation	Leibniz Institute of Plant Biochemistry Department of Bioorganic Chemistry
contact email	afrolov@ipb-halle.de
lab head
Nikita Shilyaev
contact affiliation	SPbSU
contact email	shilyaev.n.g@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD006434
     1. Label: PRIDE project
     2. Name: Advanced glycation end products as markers of ageing in plants: glycation hotspots in the plant proteome