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Related Concept Videos

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,...
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...

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Glycopeptide Capture for Cell Surface Proteomics
10:11

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

Human hemolysate glycated proteome.

Feliciano Priego-Capote1, Maria Ramirez-Boo, Christine Hoogland

  • 1Department of Human Protein Sciences, University Medical Centre, University of Geneva, Geneva, Switzerland.

Analytical Chemistry
|June 3, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces glycation isotopic labeling to quantify blood glycated proteins in human hemolysate. This method offers new insights into hyperglycemia and its impact on protein modifications in diabetes.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Endocrinology

Background:

  • Precise hyperglycemia control in diabetes relies on glucose and glycated hemoglobin monitoring.
  • New blood glycated proteins from nonenzymatic glucose reactions offer an alternative monitoring perspective.
  • Human hemolysate is a valuable source for studying glycated proteins and post-translational modifications.

Purpose of the Study:

  • To develop and apply a novel glycation isotopic labeling method for analyzing human hemolysate.
  • To identify and quantify specific protein glycation sites and modification abundance.
  • To correlate protein glycation levels with different glycemic states.

Main Methods:

  • Differential labeling of human hemolysate proteins using isotopically labeled glucose ([(13)C(6)] glucose).
  • Utilizing chemoselectivity of glycation for preferential protein target labeling.
  • Applying the strategy to hemolysate samples from individuals with varying glycated hemoglobin levels.

Main Results:

  • The glycation isotopic labeling approach successfully identified preferential protein glycation sites.
  • Qualitative and quantitative data on protein glycation abundance were obtained.
  • Protein glycation levels were correlated with glycemic states, providing insights into glucose exposure effects.

Conclusions:

  • This method provides molecular insights into protein glycation mechanisms.
  • It offers a new tool for understanding pathologies associated with prolonged hyperglycemia.
  • Potential to generate new hypotheses for clinicians to improve diabetes management.