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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Pharmacokinetics in Geriatric Patients: Effect of Age on Drug Distribution01:00

Pharmacokinetics in Geriatric Patients: Effect of Age on Drug Distribution

Drug distribution in the human body is influenced by several factors, including plasma protein concentration, body composition, blood flow, tissue-protein concentration, and tissue fluid pH. Among these, changes in plasma protein concentration and body composition due to aging significantly affect how drugs are distributed within the body. Specifically, aging is associated with a decrease in albumin levels by about 10% and an increase in α1-acid glycoprotein levels. These alterations are not...
The Effect of Aging on Tissues01:19

The Effect of Aging on Tissues

Several body functions deteriorate with age. The external signs of aging are easily identifiable. For example, the skin becomes dry, less elastic, and thins out, forming wrinkles. The skin of the face begins to appear looser due to a decrease in the levels of elastic and collagen fibers in the connective tissue. Additionally, melanin production in the hair follicle decreases with age, resulting in gray hair. Moreover, the senses of sight and hearing decline, so glasses and hearing aids may...
Pharmacodynamics in Geriatric Patients: Effects of Age01:27

Pharmacodynamics in Geriatric Patients: Effects of Age

Age-related pharmacokinetic changes are extensively documented, but understanding age-related pharmacodynamic alterations is relatively limited. This knowledge gap can be partly attributed to the complexity of developing appropriate measures of drug responses compared to bioanalytical methods for determining drug concentrations.Most information regarding age-related differences in human pharmacodynamics originates from cross-sectional studies. However, these studies assume that observed mean...

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Related Experiment Video

Updated: Jul 9, 2026

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
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Published on: May 18, 2017

N-glycomic changes in serum proteins during human aging.

Valerie Vanhooren1, Liesbeth Desmyter, Xue-En Liu

  • 1Department of Molecular Biology, Ghent University and Flanders Interuniversity Institute for Biotechnology, Technologiepark 927, Ghent, Belgium.

Rejuvenation Research
|December 1, 2007
PubMed
Summary

Changes in N-glycan structures in human serum glycoproteins are linked to aging and Werner syndrome. These N-glycan alterations may serve as biomarkers for health status and disease progression.

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Last Updated: Jul 9, 2026

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
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Published on: May 18, 2017

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Published on: January 18, 2020

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Area of Science:

  • Biochemistry
  • Immunology
  • Gerontology

Background:

  • Human serum glycoproteins undergo significant alterations in N-glycan structures with advancing age.
  • Specific N-glycan changes observed in aging are also present in individuals with Werner syndrome.

Purpose of the Study:

  • To investigate age-related changes in N-glycan profiles of human serum glycoproteins.
  • To compare N-glycan profiles in aging individuals with those in Werner syndrome patients.

Main Methods:

  • N-glycan profiling of immunoglobulin fractions from healthy individuals across different age groups.
  • Comparative analysis of glycan structures in healthy aging individuals, centenarians, and Werner syndrome patients.

Main Results:

  • Significant age-dependent shifts in three major N-glycan structures were identified.
  • Increased under-galactosylated glycans and decreased core alpha-1,6-fucosylated bi-galactosylated biantennary structures were observed in older individuals (>40-50 years).
  • Werner syndrome patients exhibited N-glycan changes comparable to or exceeding those in healthy centenarians.

Conclusions:

  • Glycosylation machinery in diverse cell types (liver and B-cells) is similarly affected by aging.
  • Observed N-glycan alterations suggest involvement of biosynthetic processes and altered serum clearance.
  • N-glycan profiling may offer a noninvasive surrogate marker for general health, age-related disease progression, and therapeutic monitoring.