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 Experiment Videos

Peroxynitrite-mediated oxidative protein modifications

H Ischiropoulos1, A B al-Mehdi

  • 1Institute for Environmental Medicine, University of Pennsylvania, School of Medicine, Philadelphia 19104, USA.

FEBS Letters
|May 15, 1995
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Detection of peroxynitrite in biological fluids.

Methods in molecular medicine·2011
Same author

Sex differences in corticotropin-releasing factor receptor signaling and trafficking: potential role in female vulnerability to stress-related psychopathology.

Molecular psychiatry·2010
Same author

Lung metastatic load limitation with hyperbaric oxygen.

Undersea & hyperbaric medicine : journal of the Undersea and Hyperbaric Medical Society, Inc·2007
Same author

Reactive nitrogen species and proteins: biological significance and clinical relevance.

Advances in experimental medicine and biology·2002
Same author

Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction.

Free radical research·2001
Same author

Signaling pathway for nitric oxide generation with simulated ischemia in flow-adapted endothelial cells.

American journal of physiology. Heart and circulatory physiology·2001
Same journal

Investigating transcription factor dynamics in health and disease using FRAP.

FEBS letters·2026
Same journal

Regulation of CFTR stability at the plasma membrane-Mechanisms and therapeutic opportunities in cystic fibrosis.

FEBS letters·2026
Same journal

Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

FEBS letters·2026
Same journal

The dual role of lectins in cancer-immunotherapy tools and therapeutic targets.

FEBS letters·2026
Same journal

Decoding the dynamic extracellular matrix in cancer-3D models and bioscaffolds rewire the rules of tumor progression.

FEBS letters·2026
Same journal

Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

FEBS letters·2026
See all related articles

Peroxynitrite causes significant protein damage, including modifications to tryptophan, cysteine, and tyrosine. The formation of 3-nitrotyrosine is a specific marker of peroxynitrite-induced oxidative stress in proteins.

Area of Science:

  • Biochemistry
  • Oxidative Stress Research
  • Protein Chemistry

Background:

  • Oxidative stress, indicated by modified proteins, is a significant biological process.
  • Peroxynitrite, a potent oxidant formed from nitric oxide and superoxide, plays a role in cellular damage.
  • Understanding peroxynitrite's impact on proteins is crucial for studying oxidative stress.

Purpose of the Study:

  • To investigate the specific modifications induced by peroxynitrite on proteins.
  • To differentiate peroxynitrite-mediated protein damage from that caused by other reactive oxygen species.
  • To utilize fatty acid-free bovine serum albumin as a model for these studies.

Main Methods:

  • Incubation of fatty acid-free bovine serum albumin with peroxynitrite.

Related Experiment Videos

  • Analysis of protein modifications including amino acid oxidation, nitration, dityrosine formation, carbonyl production, and fragmentation.
  • Detection of 3-nitrotyrosine as a specific marker.

    • Main Results:

    • Peroxynitrite induced oxidation of tryptophan and cysteine residues.
    • Tyrosine residues underwent nitration, forming 3-nitrotyrosine, and dityrosine cross-linking.
    • Significant protein fragmentation and the generation of 2,4-dinitrophenylhydrazine-reactive carbonyls were observed.
    • 3-nitrotyrosine formation was identified as a distinct marker of peroxynitrite-induced modification.

    Conclusions:

    • Peroxynitrite causes a range of detrimental modifications to proteins.
    • The formation of 3-nitrotyrosine is a specific indicator of peroxynitrite-mediated protein damage.
    • These findings contribute to understanding the molecular mechanisms of oxidative stress and peroxynitrite toxicity.