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

Assaying lipid phosphate phosphatase activities.

Gil-Soo Han1, George M Carman

  • 1Department of Food Science, Rutgers University, New Brunswick, NJ, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 3, 2004
PubMed
Summary

This study details enzymatic assays for measuring lipid phosphate phosphatase activity, crucial for understanding cellular signaling. Assays track inorganic phosphate release from lipid substrates, providing a marker for cell signaling events.

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

JBC reviews tribute to the memory of Dr William (Bill) Smith (1945-2024).

The Journal of biological chemistry·2026
Same author

Valproate causes inositol depletion in yeast by decreasing levels of phosphatidic acid and increasing Opi1-mediated repression of INO1 expression.

Biochimica et biophysica acta. Molecular and cell biology of lipids·2026
Same author

Erratum to: The antidepressant drug sertraline is a novel inhibitor of yeast Pah1 and human lipin 1 phosphatidic acid phosphatases [Journal of Lipid Research 66/1 (2025) 100711].

Journal of lipid research·2025
Same author

Active site determinants of yeast Pah1 phosphatidate phosphatase activity and cellular functions.

The Journal of biological chemistry·2025
Same author

Insights into phosphatidic acid phosphatase and its potential role as a therapeutic target.

Advances in biological regulation·2025
Same author

Partitioning of fatty acids between membrane and storage lipids controls ER membrane expansion.

The EMBO journal·2025

Area of Science:

  • Biochemistry
  • Cellular Biology
  • Enzymology

Background:

  • Lipid phosphate molecules (phosphatidate, lysophosphatidate, diacylglycerol pyrophosphate) are key signaling molecules in cells.
  • Lipid phosphate phosphatase enzymes regulate these signaling pathways.
  • Enzyme activity levels can serve as biomarkers for cellular signaling events.

Purpose of the Study:

  • To describe standard enzymatic assays for measuring phosphatidate phosphatase, lysophosphatidate phosphatase, and diacylglycerol pyrophosphate phosphatase activities.
  • To provide a method for quantifying enzyme activity relevant to cellular signaling.

Main Methods:

  • Enzymatic assays were developed to measure lipid phosphate phosphatase activities.
  • Assays involve monitoring the release of radioactive inorganic phosphate.

Related Experiment Videos

  • Substrates are chloroform-soluble radioactive lipid phosphates.
  • Phase partitioning (chloroform/methanol/water) separates products from substrates.
  • Main Results:

    • Established routine assays for key lipid phosphate phosphatase enzymes.
    • Demonstrated a reliable method for quantifying enzyme activity.
    • Validated the use of radioactive inorganic phosphate release as a readout.

    Conclusions:

    • The described enzymatic assays are effective for measuring lipid phosphate phosphatase activities.
    • These assays provide a valuable tool for studying cellular lipid phosphate signaling.
    • Quantifying these enzyme activities can help elucidate signaling mechanisms and identify biomarkers.