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

Carbohydrate Metabolism01:36

Carbohydrate Metabolism

Carbohydrates are polymers composed of molecules containing atoms of carbon, hydrogen and oxygen. One gram of carbohydrate can provide four kilo-calories of energy, which makes it the most efficient instant energy source.
Starch accounts for approximately 60% of the carbohydrates consumed by humans. Since amylase enzymes cannot function in the stomach's acidic environment, starch can only be digested in the mouth and small intestine. Simple sugars are found naturally in milk and fruits in the...
Carbohydrate Metabolism01:36

Carbohydrate Metabolism

Carbohydrates are polymers composed of molecules containing atoms of carbon, hydrogen and oxygen. One gram of carbohydrate can provide four kilo-calories of energy, which makes it the most efficient instant energy source.
Starch accounts for approximately 60% of the carbohydrates consumed by humans. Since amylase enzymes cannot function in the stomach's acidic environment, starch can only be digested in the mouth and small intestine. Simple sugars are found naturally in milk and fruits in the...
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...
Pyruvate Oxidation01:15

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
Phase II Reactions: Glucuronidation01:24

Phase II Reactions: Glucuronidation

Glucuronidation, a pivotal phase II biotransformation process, involves the coupling of glucuronic acid to a drug or xenobiotic. Given its widespread occurrence and critical role in drug metabolism, it's considered the most crucial phase II reaction. It enhances the water solubility of substances, aiding their expulsion from the body. The driving force behind these reactions is a group of enzymes known as UDP-glucuronosyltransferases (UGTs). UGTs facilitate the transfer of a glucuronic acid...
Overview of Carbohydrate Metabolism01:19

Overview of Carbohydrate Metabolism

Carbohydrate metabolism is a fundamental biochemical process that ensures a constant supply of energy to living cells. The most important carbohydrate is glucose, which can be broken down via glycolysis to enter into the Krebs cycle and eventually lead to the production of ATP through oxidative phosphorylation.
Glucose transport into cells is facilitated by a family of transport proteins called GLUT (Glucose Transporters). GLUT4 is the primary glucose transporter for insulin-stimulated glucose...

You might also read

Related Articles

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

Sort by
Same author

Complement 3a Receptor mediates high fat diet induced hypothalamic accumulation of lipid associated microglia to regulate neuroinflammation and obesity.

bioRxiv : the preprint server for biology·2026
Same author

Age-dependent progenitor switching shapes adult brown adipose tissue heterogeneity.

Research square·2026
Same author

Cutting the Gordian knot: Untangling gasdermin C from pyroptosis.

Immunity·2025
Same author

Ketone body driven lipid remodeling supports thermogenic adaptation to fasting.

bioRxiv : the preprint server for biology·2025
Same author

Corrigendum to "Monogenic deficiency in murine intestinal Cdc42 leads to mucosal inflammation that induces crypt dysplasia" [Genes & Dis 11 (2024) 413-429].

Genes & diseases·2025
Same author

Mowing management favors primary productivity and carbon sequestration without changing species diversity in a temperate hayfield in Central Interior British Columbia, Canada.

PloS one·2025

Related Experiment Video

Updated: May 11, 2026

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

Cracking the O-GlcNAc code in metabolism.

Hai-Bin Ruan1, Jay Prakash Singh, Min-Dian Li

  • 1Program in Integrative Cell Signaling and Neurobiology of Metabolism, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06519, USA.

Trends in Endocrinology and Metabolism: TEM
|May 8, 2013
PubMed
Summary
This summary is machine-generated.

O-linked β-N-acetylglucosamine (O-GlcNAc) is a crucial sugar modification impacting cellular processes and metabolism. Understanding O-GlcNAc

More Related Videos

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
10:17

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells

Published on: April 27, 2010

Related Experiment Videos

Last Updated: May 11, 2026

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
10:17

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells

Published on: April 27, 2010

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Metabolism
  • Glycoscience

Background:

  • O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic post-translational modification found on nuclear, cytoplasmic, and mitochondrial proteins.
  • This modification plays a critical role in regulating fundamental cellular processes in response to nutrient and hormonal signals.
  • Aberrant O-GlcNAcylation is linked to various human diseases, including diabetes, cancer, aging, cardiovascular, and neurodegenerative disorders.

Purpose of the Study:

  • To review the current understanding of O-GlcNAc's functions in cellular signaling and gene transcription related to metabolism.
  • To highlight the significance of O-GlcNAc in metabolic dysregulation associated with major human diseases.
  • To focus on the specific roles of O-GlcNAc in diabetes, cancer, circadian rhythm, and mitochondrial function.

Main Methods:

  • Literature review of existing research on O-GlcNAc.
  • Analysis of the roles of O-GlcNAc transferase (OGT) and O-linked β-N-acetylglucosaminase (O-GlcNAcase).
  • Synthesis of findings related to O-GlcNAc's impact on metabolic pathways and disease.

Main Results:

  • O-GlcNAc modification is a key regulator of cellular metabolism and signaling.
  • Dysregulation of O-GlcNAc pathways is implicated in the pathogenesis of metabolic diseases.
  • O-GlcNAc influences critical metabolic processes, including those related to cancer, diabetes, circadian rhythms, and mitochondrial health.

Conclusions:

  • O-GlcNAc is a central player in metabolic regulation and cellular homeostasis.
  • Targeting O-GlcNAc pathways presents potential therapeutic strategies for metabolic diseases.
  • Further research into O-GlcNAc's role in specific diseases and cellular functions is warranted.