N-Glycomic Changes in Serum Proteins During Human Aging

Vanhooren, Valerie; Desmyter, Liesbeth; Liu, Xue-En; Cardelli, Maurizio; Franceschi, Claudio; Federico, Antonio; Libert, Claude; Laroy, Wouter; Dewaele, Sylviane; Contreras, Roland; Chen, Cuiying

doi:10.1089/rej.2007.0556

Cited by 102 publications

(91 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…We previously showed that three major N-glycan structures present in human blood glycoproteins are altered with age (Vanhooren et al, 2007. Here, we investigated the possibility that age-related N-glycosylation changes occur also in mice.…”

Section: Discussionmentioning

confidence: 99%

“…In our previous studies, we demonstrated that three major N-glycan structures (NGA2F, NGA2FB, and NA2F) present in human blood glycoproteins undergo changes during aging (Vanhooren et al, 2007. These results indicate that the measurement of N-glycan levels could provide a noninvasive surrogate marker for general health, for forecasting disease progression upon aging, and for monitoring the efficacy of antiaging medications.…”

Section: Introductionmentioning

confidence: 87%

“…In our previous study, we demonstrated the alteration in serum N-glycans during human aging (Vanhooren et al, 2007. To investigate whether this holds true in mice, we studied the serum N-glycome during mouse aging in inbred mice.…”

Section: Serum Glycomic Profiling Of Aging Healthy C57bl ⁄ 6 Micementioning

confidence: 97%

See 2 more Smart Citations

Alteration in N‐glycomics during mouse aging: a role for FUT8

et al. 2011

Self Cite

View full text Add to dashboard Cite

SummaryWe recently reported that N-glycosylation changes during human aging. To further investigate the molecular basis determining these alterations, the aging process in mice was studied. N-glycan profiling of mouse serum glycoproteins in different age groups of healthy C57BL ⁄ 6 mice showed substantial age-related changes in three major N-glycan structures: under-galactosylated biantennary (NGA2F), biantennary (NA2), and core a-1,6-fucosylated -bgalactosylated biantennary structures (NA2F). Mice defective in klotho gene expression (kl ⁄ kl), which have a shortened lifespan, displayed a similar but accelerated trend. Interestingly, the opposite trend was observed in slow-aging Snell Dwarf mice (dw ⁄ dw) and in mice fed a calorically restricted diet. We also discovered that increased expression and activity of a-1,6-fucosyltransferase (FUT8) in the liver are strongly linked to the age-related changes in glycosylation and that this increased FUT8 and fucosylation influence IGF-1 signaling. These data demonstrate that the glycosylation machinery in liver cells is significantly affected during aging and that age-related increased FUT8 activity could influence the aging process by altering the sensitivity of the IGF-1R signaling pathway.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 87%

See 1 more Smart Citation

Alteration in N‐glycomics during mouse aging: a role for FUT8

et al. 2011

Self Cite

View full text Add to dashboard Cite

show abstract

“…Previous studies of suitable size (n Ͼ 200) have performed this to various degrees, finding plasma N-glycans to be highly associated with e.g. age, sex, inflammation, body mass index (BMI), cholesterol and lipid levels (17)(18)(19)(20)(21)(22)(23)(24). However, these studies have either been performed on single proteins, immunoglobulin G (IgG) being a particularly wellstudied example, or predominantly by methods of liquid chromatographic and electrophoretic separation (e.g.…”

mentioning

confidence: 99%

Human Plasma N-glycosylation as Analyzed by Matrix-Assisted Laser Desorption/Ionization-Fourier Transform Ion Cyclotron Resonance-MS Associates with Markers of Inflammation and Metabolic Health

Reiding

Ruhaak

et al. 2017

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Glycosylation is an abundant co-and post-translational protein modification of importance to protein processing and activity. Although not template-defined, glycosylation does reflect the biological state of an organism and is a high-potential biomarker for disease and patient stratification. However, to interpret a complex but informative sample like the total plasma N-glycome, it is important to establish its baseline association with plasma protein levels and systemic processes. Thus far, large-scale studies (n >200) of the total plasma N-glycome have been performed with methods of chromatographic and electrophoretic separation, which, although being informative, are limited in resolving the structural complexity of plasma N-glycans. MS has the opportunity to contribute additional information on, among others, antennarity, sialylation, and the identity of high-mannose type species.Here, we have used matrix-assisted laser desorption/ ionization ( Glycosylation is a ubiquitous co-and post-translational protein modification of functional relevance to the processing and activity of the conjugate. Examples include quality control during protein folding, regulation of circulatory half-life, and modulation of receptor interactions by either providing the recognition motif or by affecting protein conformation (1-7). Consequentially, glycosylation has been associated with a multitude of diseases and states thereof, among which the progression and metastasis of cancer and the remission of rheumatoid arthritis (8 -11). Because the process of glycosylation is not template-defined, glycosylation integrates a large series of cellular conditions such as glycosidase/glycosyltransferase abundance and activity, endoplasmic reticulum From the ‡Center

show abstract

“…Moreover, SPRET/Ei mice have attracted interest because they display interesting and robust phenotypes. For instance, they are long-lived (8), and resist the development of multiple forms of cancer or lethal inflammation induced by high doses of LPS or of the cytokine tumor necrosis factor (TNF) (9)(10)(11).…”

mentioning

confidence: 99%

Efficient analysis of mouse genome sequences reveal many nonsense variants

Steeland

Timmermans

Ryckeghem

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Genetic polymorphisms in coding genes play an important role when using mouse inbred strains as research models. They have been shown to influence research results, explain phenotypical differences between inbred strains, and increase the amount of interesting gene variants present in the many available inbred lines. SPRET/Ei is an inbred strain derived from Mus spretus that has ∼1% sequence difference with the C57BL/6J reference genome. We obtained a listing of all SNPs and insertions/deletions (indels) present in SPRET/Ei from the Mouse Genomes Project (Wellcome Trust Sanger Institute) and processed these data to obtain an overview of all transcripts having nonsynonymous coding sequence variants. We identified 8,883 unique variants affecting 10,096 different transcripts from 6,328 protein-coding genes, which is about 28% of all coding genes. Because only a subset of these variants results in drastic changes in proteins, we focused on variations that are nonsense mutations that ultimately resulted in a gain of a stop codon. These genes were identified by in silico changing the C57BL/6J coding sequences to the SPRET/Ei sequences, converting them to amino acid (AA) sequences, and comparing the AA sequences. All variants and transcripts affected were also stored in a database, which can be browsed using a SPRET/Ei M. spretus variants web tool (www.spretus.org), including a manual. We validated the tool by demonstrating the loss of function of three proteins predicted to be severely truncated, namely Fas, IRAK2, and IFNγR1.bioinformatics | genomics | mouse | mutations | inflammation

show abstract

N-Glycomic Changes in Serum Proteins During Human Aging

Cited by 102 publications

References 38 publications

Alteration in N‐glycomics during mouse aging: a role for FUT8

Alteration in N‐glycomics during mouse aging: a role for FUT8

Human Plasma N-glycosylation as Analyzed by Matrix-Assisted Laser Desorption/Ionization-Fourier Transform Ion Cyclotron Resonance-MS Associates with Markers of Inflammation and Metabolic Health

Efficient analysis of mouse genome sequences reveal many nonsense variants

Contact Info

Product

Resources

About