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

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation01:22

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion.
Several distinctive characteristics distinguish glutathione conjugation from other phase II...
Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
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...
Drug Metabolism: Phase II Reactions01:14

Drug Metabolism: Phase II Reactions

Phase II reactions are essential for the detoxification and elimination of drugs from the body. These reactions involve the conjugation of parent drugs or their phase I metabolites with endogenous molecules, resulting in more hydrophilic drug conjugates. The primary conjugation reactions in this phase are sulfation and glucuronidation. Both sulfation and glucuronidation typically produce biologically inactive metabolites. However, in some cases involving prodrugs, active metabolites may be...
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme activation, sulfur...

You might also read

Related Articles

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

Sort by
Same author

Refined liver MRI-derived cT1 thresholds capturing hepatic fat fraction enhance mortality risk prediction.

JHEP reports : innovation in hepatology·2026
Same author

Erratum: Reciprocal regulation between forkhead box M1/NF-κB and methionine adenosyltransferase 1A drives liver cancer.

Hepatology (Baltimore, Md.)·2026
Same author

Extracellular vesicles in fatty liver promote a metastatic tumor microenvironment.

Cell metabolism·2026
Same author

Forkhead box protein M1 network induction and crosstalk drives the development of alcohol-associated liver disease.

Hepatology (Baltimore, Md.)·2026
Same author

Loss of fungal sensing exacerbates liver injury in a murine model of MASLD.

JCI insight·2026
Same author

A small molecule inhibitor of ARF GTPase protein 1 limits liver and colon cancer cell growth and metastasis.

Cell death & disease·2026
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Related Experiment Video

Updated: May 18, 2026

Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro
03:35

Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro

Published on: June 28, 2024

Glutathione synthesis.

Shelly C Lu1

  • 1Keck School of Medicine USC, Los Angeles, CA 90033, USA. shellylu@usc.edu

Biochimica Et Biophysica Acta
|September 22, 2012
PubMed
Summary
This summary is machine-generated.

Glutathione (GSH) is a vital antioxidant regulating cellular processes. Its synthesis, controlled by enzymes like glutamate cysteine ligase (GCL), is crucial for health and implicated in various diseases when dysregulated.

More Related Videos

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
14:57

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases

Published on: October 10, 2020

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins
09:22

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

Published on: December 13, 2013

Related Experiment Videos

Last Updated: May 18, 2026

Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro
03:35

Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro

Published on: June 28, 2024

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
14:57

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases

Published on: October 10, 2020

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins
09:22

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

Published on: December 13, 2013

Area of Science:

  • Biochemistry
  • Cellular Biology
  • Molecular Medicine

Background:

  • Glutathione (GSH) is the primary endogenous antioxidant in mammalian tissues, crucial for defending against oxidative stress.
  • GSH plays a key role in redox signaling, xenobiotic detoxification, cell proliferation, apoptosis, immune function, and fibrogenesis.
  • GSH biosynthesis occurs in the cytosol, regulated by precursor availability (cysteine) and the activity of glutamate cysteine ligase (GCL) and GSH synthetase (GS).

Purpose of the Study:

  • This review summarizes the critical functions of glutathione (GSH).
  • It focuses on the regulatory factors governing GSH biosynthesis.
  • The review also examines pathological conditions characterized by dysregulated GSH synthesis.

Main Methods:

  • Literature review of key functions and regulation of GSH biosynthesis.
  • Analysis of factors influencing GCL and GS enzyme activity and gene expression.
  • Examination of the role of GSH dysregulation in various disease states.

Main Results:

  • GCL subunits (GCLC, GCLM) and GS are regulated at multiple levels, often coordinately.
  • Transcription factors like Nrf2, AP-1, and NFκB significantly influence the expression of genes involved in GSH synthesis.
  • Dysregulation of GSH synthesis is increasingly recognized as a contributor to the pathogenesis of numerous diseases.

Conclusions:

  • The synthesis of GSH is tightly controlled by complex regulatory mechanisms involving multiple enzymes and transcription factors.
  • Impaired GSH synthesis is linked to the development and progression of diseases including diabetes, fibrosis, liver diseases, and cancer.
  • Understanding GSH synthesis regulation and its pathological dysregulation offers potential therapeutic strategies for these disorders.