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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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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.
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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,...
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Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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Glycopeptide Capture for Cell Surface Proteomics
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Mapping GlycoRNAs on an Exosomal Surface.

Anita Yadav1, Anu Sharma1, Parmeshwar V Gavande1

  • 1McGowan Institute for Regenerative Medicine, Department of Surgery, University of Pittsburgh, Pittsburgh, Pennsylvania 15219, United States.

Journal of the American Chemical Society
|January 6, 2026
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel method to detect glycoRNAs on exosomes, revealing direct glycan-RNA links. This breakthrough advances understanding of glycoRNA biology and intercellular communication.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Exosomes are crucial for intercellular communication, but detecting surface glycoRNAs presents challenges due to their nanoscale size.
  • Current detection methods lack specificity and sensitivity for surface-bound glycoRNAs on exosomes.

Purpose of the Study:

  • To develop and validate an innovative method for detecting glycoRNAs on exosome surfaces.
  • To investigate the biological significance of glycoRNAs in intercellular communication.

Main Methods:

  • Periodate oxidation and oxime ligation (OL) combined with RNA-binding dyes or molecular beacons (MB).
  • Sequential dual-labeling, flow cytometry, and direct stochastic optical reconstruction microscopy (dSTORM) for validation.
  • Enzymatic treatments (ribonucleases, PNGase F) to determine glycan modification location and stability.

Main Results:

  • Successfully detected and identified direct glycan-RNA linkages on exosome surfaces.
  • Validated method specificity and sensitivity, distinguishing exosome-surface-bound glycoRNAs.
  • Elucidated the role of glycoRNAs in cellular uptake and intercellular communication.

Conclusions:

  • The developed OL method offers a sensitive and specific approach for glycoRNA detection on exosomes.
  • GlycoRNAs play a significant role in intercellular communication via cellular uptake.
  • This work expands the scope of epitranscriptomics and offers potential therapeutic insights.