Related Experiment Video
Updated: Jun 20, 2026
11:57
Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
Published on: November 26, 2017
8.5K
GlycA as an Effect Modifier of Protein-Mortality Associations: A Prospective Cohort Study
Xinru Wang1,2,3, Ziyan Qiao1,2,3, Chengzhe Tao2,3,4
1Changzhou Maternal and Child Health Care Hospital, Changzhou Medical Center, Nanjing Medical University, Nanjing, China.
Clinical and Translational Science
|April 21, 2026
Summary
Glycoprotein acetyls (GlycA) levels modify how certain proteins affect mortality risk. This inflammation biomarker highlights differing protein-health associations and potential therapeutic targets.
Area of Science:
- Biomarkers
- Proteomics
- Inflammation
Background:
- Heterogeneity in circulating protein health effects is unclear.
- Glycoprotein acetyls (GlycA), an inflammation biomarker, links to mortality and chronic diseases.
- GlycA's role in modifying protein-health associations needs investigation.
Purpose of the Study:
- To evaluate if GlycA modifies protein-mortality associations.
- To explore GlycA's influence on protein-disease links.
- To identify potential therapeutic targets based on inflammation status.
Main Methods:
- Utilized multi-omics profiling of the UK Biobank prospective cohort.
- Performed statistical analyses to assess GlycA's modifying effects.
- Replicated findings in independent discovery and validation datasets.
Main Results:
- GlycA significantly modified associations of ANG, CRHBP, CXCL16, and PRRT3 with all-cause mortality.
- Subgroup analyses confirmed GlycA's modulation of protein-mortality links.
- Exploratory analyses linked GlycA-protein interactions to cancer mortality and heart failure.
Conclusions:
- GlycA influences the health effects of specific circulating proteins.
- Findings reveal heterogeneity in protein-health associations modulated by inflammation.
- Identified potential therapeutic targets for conditions influenced by inflammation.
Related Concept Videos
01:25Protein 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...
Glycosylation occurs in...
01:05Proteoglycans
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,...
01:20Factors Affecting Protein-Drug Binding: Protein-Related Factors
Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
01:29Factors Affecting Protein-Drug Binding: Patient-Related Factors
Protein-drug binding, a pivotal aspect of pharmacokinetics, is subject to considerable variability influenced by an array of patient-related factors. The intricate interplay of age, individual differences, and pathological conditions significantly impact the binding dynamics and subsequent pharmacological effects.
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...
01:09Hepatic Drug Clearance: Effect of Protein Binding
Hepatic clearance is influenced by protein binding based on the drug's extraction ratio. Drugs with high extraction ratios are considered flow-limited and remain unaffected by protein binding during hepatic clearance. On the other hand, drugs with low extraction ratios may be impacted by plasma protein binding, although the extent of this influence depends on the fraction of the drug bound.
For low-extraction-ratio drugs that are less than 80% protein-bound, minor changes in protein binding...
For low-extraction-ratio drugs that are less than 80% protein-bound, minor changes in protein binding...
01:13Physiological Pharmacokinetic Models: Assumption with Protein Binding
Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...