Biomarkers indicating biological age are of significant interest for prevention, diagnosis and monitoring (and the treatment) of age-related diseases. We previously reported an alteration of serum N-glycan profile in old humans using "DNA Sequencer Adapted-Fluorophore Assisted Carbohydrate Electrophoresis" (DSA-FACE). To validate the shift in serum N-glycan profile during ageing, we studied serum N-glycan profiles in different age groups of healthy volunteers, patients with dementia, and patients with Cockayne syndrome, a genetic DNA repair disorder involving neurodegeneration and premature ageing. We found that the log of the ratio of two glycans (NGA2F and NA2F), named GlycoAgeTest, remained steady up to the age of 40years and thereafter gradually increased to reach its highest level in nonagenarians. Patients with dementia or Cockayne syndrome had a higher GlycoAgeTest level than age-matched healthy individuals. We thus demonstrate that the value of GlycoAgeTest is better than chronological age for estimating the physiological age of a human individual, and that it could be used as an ageing biomarker for healthy humans. Our data indicate that the GlycoAgeTest could be used as a non-invasive surrogate marker for general health, for forecasting disease progression during ageing, and for monitoring the efficacy of anti-ageing food compounds.
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http://dx.doi.org/10.1016/j.exger.2010.08.009 | DOI Listing |
Int J Transl Med (Basel)
September 2024
Department of Biochemistry and Molecular Biology, Brody School of Medicine, East Carolina University Greenville, 600 Moye Boulevard, Greenville, NC 27834, USA.
Aberrant N-glycosylation has been associated with progression of the pediatric cancer neuroblastoma (NB) but remains understudied. Here we investigated oligomannose N-glycans in NB by genetic editing of in a human NB cell line, BE(2)-C, called BE(2)-C(MGAT1). Lectin binding studies confirmed that BE(2)-C(MGAT1) had decreased complex and increased oligomannose N-glycans.
View Article and Find Full Text PDFEur J Neurol
January 2025
Department of Neurology, Nagoya University Graduate School of Medicine, Nagoya, Aichi, Japan.
Metabolomics
December 2024
Centre for Metabolomics Research (CMR), Department of Biochemistry, Cell, and Systems Biology, Institute of Systems Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
Introduction: Outside of case-control settings, ethnicity specific changes in the human metabolome are understudied especially in community dwelling, ageing men. Characterising serum for age and ethnicity specific features can enable tailored therapeutics research and improve our understanding of the interplay between age, ethnicity, and metabolism in global populations.
Objective: A metabolomics approach was adopted to profile serum metabolomes in middle-aged and elderly men of different ethnicities from the Northwest of England, UK.
Biochim Biophys Acta Rev Cancer
December 2024
Dept. Medical Oncology, Ghent University Hospital, Ghent, Belgium; Biomarkers in Cancer research group, Dept. Basic and Applied Medicine, Ghent University, Ghent, Belgium; Cancer Research Institute Ghent, Ghent, Belgium. Electronic address:
Alterations in the prostate cancer (PCa) N-glycome have gained attention as a potential biomarker. This comprehensive review explores the diversity of N-glycosylation patterns observed in PCa-related cell lines, tissue, serum and urine, focusing on prostate-specific antigen (PSA) and the total pool of glycoproteins. Within the context of PCa, altered N-glycosylation patterns are a mechanism of immune escape and a disruption in normal glycoprotein distribution and trafficking.
View Article and Find Full Text PDFBiochem Biophys Res Commun
January 2025
Glycometabolic Biochemistry Laboratory, RIKEN-Cluster for Pioneering Research, Wako, Saitama, 351-0198, Japan. Electronic address:
Free N-glycans (FNGs) are oligosaccharides that are structurally related to N-linked glycans, and are widely found in nature. The mechanisms responsible for the formation and degradation of intracellular FNGs are well characterized in mammalian cells. More recent analysis in mammalian sera shows that there are various types of extracellular free glycans, including FNGs.
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