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

Some anti-chronic inflammatory compounds are DNA polymerase lambda-specific inhibitors.

Yoshiyuki Mizushina1, Mitsuru Hirota, Chikako Murakami

  • 1Department of Nutritional Science, Kobe-Gakuin University, Nishi-ku, Kobe, 651-2180 Hyogo, Japan. mizushin@nutr.kobegakuin.ac.jp

Biochemical Pharmacology
|November 6, 2003
PubMed
Summary

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

Crystal structures of Klebsiella oxytoca ribitol dehydrogenase in complex with NAD<sup>+</sup>, d-allose, or d-allulose reveal insight into substrate recognition.

FEBS letters·2026
Same author

A Survey of Medical Resuscitation Practices and Resources in Academic Pediatric Emergency Departments.

Pediatric emergency care·2026
Same author

Production of rare sugars by transketolase in combination with ketose 3-epimerase.

Methods in enzymology·2025
Same author

Unraveling the Effect of the C-terminal Tail of <i>Agaricus bisporus</i> Mannose-Binding Protein and Discovery of a Second Functional Sugar-Binding Site.

Biochemistry. Biokhimiia·2025
Same author

Synthetic Study of 8- and 9-Carbon Sugars by Transaldolase.

Journal of agricultural and food chemistry·2025
Same author

Efficient production of d-sedoheptulose using transketolase from Thermus thermophilus HB8 and epimerization reaction using d-tagatose 3-epimerase from Pseudomonas cichorii ST24.

Bioscience, biotechnology, and biochemistry·2025

Curcumin and petasiphenol selectively inhibit DNA polymerase lambda (pol lambda), a key enzyme in DNA replication. These compounds show potential for cancer therapy by halting cell growth through different mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Petasiphenol was previously identified as a selective inhibitor of DNA polymerase lambda (pol lambda).
  • Curcumin, a known anti-inflammatory agent, shares structural similarities with petasiphenol.
  • Mammalian DNA polymerases play crucial roles in DNA replication and repair.

Purpose of the Study:

  • To investigate the inhibitory effects of curcumin and petasiphenol on various DNA polymerases.
  • To compare the functional differences between curcumin and petasiphenol in cancer cell lines.
  • To explore the potential link between pol lambda inhibition and inflammation.

Main Methods:

  • In vitro enzymatic assays were performed to determine the IC(50) values for pol lambda inhibition.

Related Experiment Videos

  • Assays were conducted to assess the effects on other DNA polymerases, including replicative polymerases and pol beta.
  • Cell proliferation assays (LD(50)) and cell cycle analysis were performed on human cancer cells (NUGC-3).

    • Main Results:

    • Both petasiphenol (IC(50) = 7.8 microM) and curcumin (IC(50) = 7.0 microM) potently inhibited pol lambda.
    • Neither compound affected replicative DNA polymerases (alpha, gamma, delta, epsilon) or pol beta.
    • Curcumin halted cancer cell growth at the G2/M phase (LD(50) = 13 microM), while petasiphenol arrested cells at the G1 phase (LD(50) = 66 microM).

    Conclusions:

    • Curcumin and petasiphenol are selective inhibitors of DNA polymerase lambda.
    • These compounds exhibit distinct mechanisms in halting cancer cell proliferation.
    • The findings suggest a potential physiological role for pol lambda inhibition in inflammation.