Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/37548
Title: Increased expression of immature mannose-containing glycoproteins and sialic acid in aged mouse brains
Author(s): Simon, Frieder
Bork, KayaLook up in the Integrated Authority File of the German National Library
Gnanapragassam, Vinayaga S.
Baldensperger, Tim
Glomb, Marcus A.
Sanzo, Simone
Ori, Alessandro
Horstkorte, Rüdiger
Issue Date: 2019
Type: Article
Language: English
Abstract: Aging represents the accumulation of changes in an individual over time, encompassing physical, psychological, and social changes. Posttranslational modifications of proteins such as glycosylation, including sialylation or glycation, are proposed to be involved in this process, since they modulate a variety of molecular and cellular functions. In this study, we analyzed selected posttranslational modifications and the respective proteins on which they occur in young and old mouse brains. The expression of neural cell adhesion molecule (NCAM), receptor for advanced glycation endproducts (RAGE), as well as the carbohydrate-epitopes paucimannose and high-mannose, polysialic acid, and O-GlcNAc were examined. We demonstrated that mannose-containing glycans increased on glycoproteins in aged mouse brains and identified synapsin-1 as one major carrier of paucimannose in aged brains. In addition, we found an accumulation of so-called advanced glycation endproducts, which are generated by non-enzymatic reactions and interfere with protein function. Furthermore, we analyzed the expression of sialic acid and found also an increase during aging.
URI: https://opendata.uni-halle.de//handle/1981185920/37791
http://dx.doi.org/10.25673/37548
Open Access: Open access publication
License: (CC BY 4.0) Creative Commons Attribution 4.0(CC BY 4.0) Creative Commons Attribution 4.0
Sponsor/Funder: Publikationsfond MLU
Journal Title: International journal of molecular sciences
Publisher: MDPI
Publisher Place: Basel
Volume: 20
Issue: 24
Original Publication: 10.3390/ijms20246118
Appears in Collections:Open Access Publikationen der MLU

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