Pregled bibliografske jedinice broj: 1281159
Structural analysis and signatures of a naked mole-rat blood plasma N-glycome
Structural analysis and signatures of a naked mole-rat blood plasma N-glycome // HPLC2023 - 51st International Symposium on High Performance Liquid Phase Separations and Related Techniques
Düsseldorf, Njemačka, 2023. (poster, međunarodna recenzija, neobjavljeni rad, znanstveni)
CROSBI ID: 1281159 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Structural analysis and signatures of a naked mole-rat blood plasma N-glycome
Autori
Habazin, Siniša ; Smith St. John, Ewan ; Lauc, Gordan ; Novokmet, Mislav
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, neobjavljeni rad, znanstveni
Skup
HPLC2023 - 51st International Symposium on High Performance Liquid Phase Separations and Related Techniques
Mjesto i datum
Düsseldorf, Njemačka, 18.06.2023. - 22.06.2023
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
N-glycans ; Mass spectrometry ; Longevity
Sažetak
The naked mole-rat (NMR) is a most unusual eusocial burrowing rodent native to East Africa. Remarkable physiological traits such as a long lifespan of ˃30 years, hypoxia and pain tolerance, attenuated neurodegeneration as well as exceptional cancer resistance have rendered them a popular lesser-known animal model for longevity research [1]. On the proteome level, the underlying molecular mechanisms of a NMR delayed ageing phenotype include enhanced proteostasis, high proteasome activity, and unusual concurrent upregulation and downregulation of ageing-regulating signaling pathways. Still, the landscape of NMR protein posttranslational modifications (PTMs) is unmapped. Here, we focused on protein N-glycosylation – a large and structurally highly diverse PTM essential for protein folding, biological recognition, immune response, inflammation, and carcinogenesis. Using an offline WAX-HILIC 2D-LC coupled with ESI-Qq-TOF-MS/MS, a comprehensive structural analysis of PNGaseF-released and procainamide-labelled plasma N-glycans was performed. A total of 132 N-glycans were annotated revealing for the first time an insight into NMR major plasma proteins N-glycosylation. The hallmark of NMR plasma N-glycome is the extensive N-glycan sialylation with both N-acetyl- and N-glycolylneuraminic acid and their 4-O-acetylated modifications (Neu4, 5Ac2 and Neu4Ac5Gc). These exciting discoveries emphasize the subtle interspecies differences in protein glycosylation and are yet to be linked with NMR resilience.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb,
GENOS d.o.o.