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

P-57 is a neural specific calmodulin-binding protein.

B M Cimler, T J Andreasen, K I Andreasen

    The Journal of Biological Chemistry
    |September 5, 1985
    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

    Constitutive μ-opioid receptor activity leads to long-term endogenous analgesia and dependence.

    Science (New York, N.Y.)·2013
    Same author

    Inactivation of Pde8b enhances memory, motor performance, and protects against age-induced motor coordination decay.

    Genes, brain, and behavior·2012
    Same author

    High precision stereotaxic surgery in mice.

    Current protocols in neuroscience·2008
    Same author

    Inactivation of the mouse adenylyl cyclase 3 gene disrupts male fertility and spermatozoon function.

    Molecular endocrinology (Baltimore, Md.)·2005
    Same author

    The CRE/CREB pathway is transiently expressed in thalamic circuit development and contributes to refinement of retinogeniculate axons.

    Neuron·2001
    Same author

    Adenylyl cyclase 3 mediates prostaglandin E(2)-induced growth inhibition in arterial smooth muscle cells.

    The Journal of biological chemistry·2001

    P-57 is a novel calmodulin-binding protein found predominantly in neural tissues. This protein binds calmodulin with high affinity, even without calcium, suggesting a significant role in brain function.

    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Biochemistry

    Background:

    • Calmodulin (CaM) is a crucial calcium-binding protein involved in cellular signaling.
    • Most known CaM-binding proteins exhibit altered affinity for CaM in the presence or absence of calcium.
    • P-57 is a recently identified CaM-binding protein from bovine cerebral cortex.

    Purpose of the Study:

    • To investigate the tissue distribution of P-57.
    • To determine the abundance and localization of P-57 within the brain.
    • To characterize the binding properties of P-57 with calmodulin.

    Main Methods:

    • Radioimmune assay was employed to quantify P-57 levels across various tissues.
    • Photoaffinity labeling with azido-125I-calmodulin was used to study P-57 binding.

    Related Experiment Videos

  • Differential fractionation was performed to localize P-57 within cellular compartments.

    • Main Results:

    • P-57 was exclusively detected in brain, retina, and spinal cord, indicating neural specificity.
    • P-57 constituted up to 0.5% of total protein in cell body-rich brain fractions.
    • The protein was found in both soluble and membrane fractions within the brain.
    • P-57 demonstrated high affinity for calmodulin independent of calcium levels.

    Conclusions:

    • P-57 is the most abundant calmodulin-binding protein in the brain and exhibits neural specificity.
    • Its high affinity for calmodulin, even in the absence of calcium, suggests a unique regulatory role.
    • P-57 has the potential to bind a substantial portion of total calmodulin in the brain.