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

Protein oxidation.

E R Stadtman1, R L Levine

  • 1Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-0320, USA. erstadtman@nih.gov

Annals of the New York Academy of Sciences
|June 23, 2000
PubMed
Summary

Oxidative modification of proteins, particularly by reactive oxygen species, contributes to many diseases. Increased levels of these modified proteins, measured by protein carbonyl content, disrupt cellular function and are linked to aging.

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

Pro-oxidant activity of Cu,Zn-superoxide dismutase.

Age·2013
Same author

Storage of dried fruit; influence of moisture and sulfur dioxide on deterioration of apricots.

Industrial and engineering chemistry·2010
Same author

IDH1 and IDH2 mutation studies in 1473 patients with chronic-, fibrotic- or blast-phase essential thrombocythemia, polycythemia vera or myelofibrosis.

Leukemia·2010
Same author

Accurate detection of uniparental disomy and microdeletions by SNP array analysis in myelodysplastic syndromes with normal cytogenetics.

Leukemia·2009
Same author

Detection of mutant TET2 in myeloid malignancies other than myeloproliferative neoplasms: CMML, MDS, MDS/MPN and AML.

Leukemia·2009
Same author

Frequent TET2 mutations in systemic mastocytosis: clinical, KITD816V and FIP1L1-PDGFRA correlates.

Leukemia·2009

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Oxidative modification of proteins by reactive species is a key factor in disease development.
  • Reactive species increase due to imbalances in production and scavenging, leading to cellular damage.
  • Oxidatively modified proteins accumulate due to impaired proteolytic degradation, impacting cellular function.

Purpose of the Study:

  • To highlight the role of protein oxidative modification in disease etiology and progression.
  • To explain the mechanisms leading to the accumulation of oxidatively modified proteins.
  • To emphasize the significance of measuring protein carbonyl content as a biomarker.

Main Methods:

  • Quantification of protein carbonyl content.
  • Analysis of protein degradation pathways.
  • Correlation of modified protein levels with disease states and aging.

Main Results:

  • Protein carbonyl content increases in various diseases and aging processes.
  • Accumulation of oxidatively modified proteins disrupts cellular integrity and function.
  • Impaired proteolysis exacerbates the buildup of damaged proteins.

Conclusions:

  • Oxidative protein modification is a significant contributor to numerous disorders.
  • Monitoring protein carbonyl levels can indicate disease progression and aging.
  • Maintaining efficient proteolysis is crucial for cellular health and preventing disease.

Related Experiment Videos