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

Nitric oxide and intracellular heme

Y M Kim1, H A Bergonia, C Müller

  • 1Department of Surgery, University of Pittsburgh School of Medicine, Pennsylvania 15261, USA.

Advances in Pharmacology (San Diego, Calif.)
|January 1, 1995
PubMed
Summary

Nitric oxide (NO) disrupts heme in CYP proteins, decreasing heme synthesis and increasing degradation. This process may protect cells from injury, highlighting a novel cellular defense mechanism.

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

Improved spatial resolution of matrix-assisted laser desorption/ionization imaging of lipids in the brain by alkylated derivatives of 2,5-dihydroxybenzoic acid.

Rapid communications in mass spectrometry : RCM·2014
Same author

Methods for retrovirus-mediated gene transfer to fetal lung.

Methods in molecular medicine·2014
Same author

Physiology, reductionism, and translational medicine: the right mix.

American journal of physiology. Lung cellular and molecular physiology·2011
Same author

Nitric oxide-induced changes in intracellular zinc homeostasis are mediated by metallothionein/thionein.

American journal of physiology. Lung cellular and molecular physiology·2002
Same author

Signal transduction pathways of IL-1beta-mediated iNOS in pulmonary vascular smooth muscle cells.

American journal of physiology. Lung cellular and molecular physiology·2001
Same author

CFTR trafficking and signaling in respiratory epithelium.

American journal of physiology. Lung cellular and molecular physiology·2001

Area of Science:

  • Biochemistry
  • Cellular Biology
  • Toxicology

Background:

  • Cytochrome P450 (CYP) proteins are crucial for cellular metabolism.
  • Heme is essential for CYP protein function.
  • Nitric oxide (NO) plays diverse physiological and pathological roles.

Purpose of the Study:

  • To elucidate the mechanism by which NO affects CYP proteins and heme metabolism.
  • To investigate the consequences of NO-induced heme loss on cellular processes.
  • To explore the potential protective role of NO-related pathways against cellular injury.

Main Methods:

  • Hypothetical model based on experimental results (Figure 2).
  • Analysis of heme content in CYP proteins.
  • Measurement of heme synthesis (ALAS) and degradation (HO) enzyme activities.

Related Experiment Videos

  • Assessment of ferrochelatase activity.
  • Investigation of CYP repair mechanisms.

    • Main Results:

    • NO synthesis causes heme loss from CYP proteins, leaving the proteins largely intact.
    • Heme loss leads to decreased heme synthesis (reduced ALAS) and increased heme degradation (elevated HO).
    • NO directly inhibits ferrochelatase, further impeding heme synthesis.
    • Evidence suggests a mechanism for CYP repair or resynthesis after NO inhibition.
    • Increased HO activity, a response to cellular injury, is observed.

    Conclusions:

    • NO-induced heme loss from CYPs alters heme metabolism by decreasing synthesis and increasing degradation.
    • Ferrochelatase inhibition by NO contributes to reduced heme synthesis.
    • The cellular response, including increased HO, may offer protection against various forms of cellular injury.