Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Proteoglycans01:05

Proteoglycans

5.1K
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,...
5.1K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.8K
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...
3.8K
Protein Glycosylation01:25

Protein Glycosylation

10.2K
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...
10.2K
Glycosaminoglycans01:23

Glycosaminoglycans

7.5K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
7.5K
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.3K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.3K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.4K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.4K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Comparative analysis of growth and quality traits in promising yellow-fleshed kiwifruit genotypes in the North-Western Himalayas.

BMC plant biology·2026
Same author

Nanosized silver phosphate-based asymmetric and symmetric electrochemical capacitors for first- and second-order low-pass filter applications.

Nanoscale advances·2026
Same author

MYCN drives pediatric glioma transformation from neural progenitors and creates distinct therapeutic vulnerabilities.

Cell reports·2026
Same author

Therapeutic significance of surface-exposed virulence factors in Acinetobacter baumannii pathogenicity.

Molecular biology reports·2026
Same author

Fully plant-derived flaxseed mucilage-soy protein inks for extrusion-based 3D printing of tunable hydrogel scaffolds.

RSC advances·2026
Same author

Dordaviprone for Diffuse Midline Glioma: A Landmark Approval or a Premature Step?

Neuro-oncology·2026

Related Experiment Video

Updated: Mar 13, 2026

Synthesis of Stimuli-responsive Nanogels using Aqueous One-step Crosslinking and Co-nanopolymerization
06:26

Synthesis of Stimuli-responsive Nanogels using Aqueous One-step Crosslinking and Co-nanopolymerization

Published on: January 24, 2025

2.0K

The redox paradox in HGGs: ROS as drivers and destroyers.

Pooja Kumari1, Zacary P Germon1, Evangeline R Jackson1

  • 1Cancer Signalling Research Group, School of Biomedical Sciences and Pharmacy, College of Health, Medicine and Wellbeing, New Lambton Heights, Newcastle, New South Wales, Australia; Precision Medicine and Health Program, Hunter Medical Research Institute, New Lambton Heights, Newcastle, New South Wales, Australia; Pediatric Stream, Mark Hughes Foundation Centre for Brain Cancer Research, College of Health, Medicine and Wellbeing, Callaghan, New South Wales, Australia.

Trends in Cancer
|March 11, 2026
PubMed
Summary

Reactive oxygen species (ROS) drive high-grade glioma growth and resistance. Targeting ROS reveals a paradox: they fuel tumors but also create vulnerabilities for new cancer therapies.

Keywords:
diffuse midline gliomaepigeneticsglioblastomaoncogenic signalingoxidative stressreactive oxygen species

More Related Videos

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry
13:06

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Published on: November 20, 2014

12.5K
Facile and Efficient Preparation of Tri-component Fluorescent Glycopolymers via RAFT-controlled Polymerization
10:54

Facile and Efficient Preparation of Tri-component Fluorescent Glycopolymers via RAFT-controlled Polymerization

Published on: June 19, 2015

10.3K

Related Experiment Videos

Last Updated: Mar 13, 2026

Synthesis of Stimuli-responsive Nanogels using Aqueous One-step Crosslinking and Co-nanopolymerization
06:26

Synthesis of Stimuli-responsive Nanogels using Aqueous One-step Crosslinking and Co-nanopolymerization

Published on: January 24, 2025

2.0K
Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry
13:06

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Published on: November 20, 2014

12.5K
Facile and Efficient Preparation of Tri-component Fluorescent Glycopolymers via RAFT-controlled Polymerization
10:54

Facile and Efficient Preparation of Tri-component Fluorescent Glycopolymers via RAFT-controlled Polymerization

Published on: June 19, 2015

10.3K

Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • Reactive oxygen species (ROS) are crucial signaling molecules but their dysregulation fuels cancer progression and treatment resistance.
  • High-grade gliomas, including glioblastoma, diffuse hemispheric glioma, and diffuse midline glioma (DMG), exhibit chronic ROS production due to genetic, epigenetic, and metabolic alterations.
  • This sustained oxidative stress contributes to DNA damage, epigenetic changes, tumor proliferation, and immune evasion.

Purpose of the Study:

  • To explore the dual role of ROS in high-grade gliomas, focusing on their contribution to tumor growth and therapeutic resistance.
  • To investigate the specific mechanisms by which ROS impact DMG, including DNA/histone methylation and key signaling pathways.
  • To identify therapeutic vulnerabilities arising from the paradoxical nature of ROS in cancer.

Main Methods:

  • Review and synthesis of existing literature on ROS, oxidative stress, and high-grade gliomas.
  • Analysis of genetic, epigenetic, and metabolic alterations contributing to ROS production in gliomas.
  • Examination of ROS-dependent signaling pathways (MAPK, PI3K/Akt/mTOR) and their role in tumor survival.
  • Evaluation of emerging therapeutic strategies targeting ROS, such as NADPH oxidase inhibition and metabolic modulation.

Main Results:

  • Chronic ROS production and redox imbalance are hallmarks of high-grade gliomas, promoting tumor growth and resistance.
  • In DMG, oxidative stress exacerbates global DNA and histone hypomethylation, while activating pro-survival pathways.
  • Excess ROS paradoxically create an intrinsic vulnerability by overwhelming cellular defenses and inducing cytotoxicity.
  • Targeting ROS through novel strategies like NADPH oxidase inhibition and metabolic therapies presents potential treatment avenues.

Conclusions:

  • Understanding the complex redox paradox in high-grade gliomas is essential for developing effective therapeutic strategies.
  • Exploiting the ROS-induced vulnerabilities offers a promising approach to improve outcomes for patients with these aggressive brain tumors.
  • Further research into ROS-modulating therapies is critical for overcoming treatment resistance and enhancing patient survival in high-grade gliomas.