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

Phosphatidate-dependent protein phosphorylation.

S B Bocckino1, P B Wilson, J H Exton

  • 1Howard Hughes Medical Institute Laboratory, Vanderbilt University School of Medicine, Nashville, TN 37232-0295.

Proceedings of the National Academy of Sciences of the United States of America
|July 15, 1991
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

Of growing importance: combining greater early vigour and transpiration efficiency for wheat in variable rainfed environments.

Functional plant biology : FPB·2020
Same author

Glucose-fructose likely improves gastrointestinal comfort and endurance running performance relative to glucose-only.

Scandinavian journal of medicine & science in sports·2015
Same author

Moderate-to-vigorous physical activity in individuals with psoriasis: associations with body surface area and subjective disease severity.

Giornale italiano di dermatologia e venereologia : organo ufficiale, Societa italiana di dermatologia e sifilografia·2013
Same author

Psoriasis and physical activity: a review.

Journal of the European Academy of Dermatology and Venereology : JEADV·2012
Same author

Elevated plasma CD105 and vitreous VEGF levels in diabetic retinopathy.

Journal of cellular and molecular medicine·2005
Same author

Phospholipase D-structure, regulation and function.

Reviews of physiology, biochemistry and pharmacology·2002

Phosphatidate triggers protein phosphorylation in rat tissues, sometimes requiring calcium. A specific 30-kDa heart protein is phosphorylated independently of calcium by phosphatidate in various tissues, suggesting a kinase-mediated mechanism.

Area of Science:

  • Biochemistry
  • Cellular Biology
  • Molecular Biology

Background:

  • Phosphatidate is a key lipid mediator involved in various cellular processes.
  • Protein phosphorylation is a critical regulatory mechanism in cell signaling.
  • The specific roles of phosphatidate in protein phosphorylation across different tissues are not fully elucidated.

Purpose of the Study:

  • To investigate phosphatidate-dependent protein phosphorylation in soluble extracts from various rat tissues.
  • To determine the role of calcium (Ca2+) in phosphatidate-mediated protein phosphorylation.
  • To identify potential protein substrates and characterize the nature of phosphatidate-dependent phosphorylation.

Main Methods:

  • Preparation of soluble protein extracts from rat liver, brain, lung, testis, and heart.

Related Experiment Videos

  • In vitro protein phosphorylation assays using [32P]ATP in the presence of phosphatidate.
  • Varying concentrations of free Ca2+ were used to assess its effect on phosphorylation.
  • Comparison of phosphorylation profiles using phosphatidate versus phosphatidylserine and 1,2-diolein.
  • Analysis of specific protein phosphorylation, including a 30-kDa protein from heart tissue.

    • Main Results:

    • Phosphatidate-dependent protein phosphorylation was detected in soluble extracts from rat liver, brain, lung, and testis.
    • Calcium (360-800 nM) stimulated this phosphorylation in a dose-dependent manner in most tissues.
    • Phosphatidate yielded different phosphorylation profiles compared to phosphatidylserine plus 1,2-diolein.
    • A 30-kDa protein in heart soluble fractions underwent phosphatidate-dependent phosphorylation independently of Ca2+.
    • Soluble extracts from liver, testis, brain, and lung also phosphorylated this 30-kDa heart protein in a Ca2+-independent manner.

    Conclusions:

    • Phosphatidate can mediate protein phosphorylation in various rat tissues.
    • The mechanism can be either calcium-dependent or calcium-independent, depending on the specific protein and tissue.
    • The findings suggest that phosphatidate may exert some of its cellular functions through the activation of protein kinase(s).
    • A specific 30-kDa protein is a target for phosphatidate-dependent, calcium-independent phosphorylation, potentially involving a distinct kinase pathway.