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Related Experiment Videos

Phosphorylation of prolactin.

W S Oetting, P T Tuazon, J A Traugh

    The Journal of Biological Chemistry
    |February 5, 1986
    PubMed
    Summary

    Rat prolactin shows microheterogeneity due to differential phosphorylation. In vitro and in vivo studies confirm that protein kinases add phosphate groups to rat prolactin isoforms 2 and 3, explaining charge variations.

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    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Biochemistry

    Background:

    • Rat prolactin displays microheterogeneity, appearing as three isoforms (1, 2, and 3) with identical molecular weights but distinct net charges.
    • Phosphorylation is a known mechanism causing microheterogeneity in pituitary hormones.

    Purpose of the Study:

    • To investigate if rat prolactin exists in differentially phosphorylated forms.
    • To identify the specific protein kinases involved in rat prolactin phosphorylation.
    • To confirm prolactin phosphorylation in vivo.

    Main Methods:

    • In vitro phosphorylation assays using purified rat prolactin incubated with [gamma-32P]ATP and various protein kinases.
    • Identification of phosphorylated rat prolactin via autoradiography on one- and two-dimensional gels.
    • In vivo studies involving rat anterior pituitary cells cultured with H3 32PO4, followed by protein extraction and analysis on two-dimensional gels.

    Main Results:

    • Rat prolactin was successfully phosphorylated in vitro by cAMP-dependent protein kinase, casein kinase I, protease-activated kinase I, and calcium/phospholipid-dependent kinase.
    • Phosphorylation incorporated phosphate groups exclusively into rat prolactin isoforms 2 and 3.
    • Evidence of prolactin phosphorylation was also observed in rat pituitary cells cultured in vitro.

    Conclusions:

    • Differential phosphorylation by specific protein kinases accounts for the observed microheterogeneity of rat prolactin isoforms.
    • Isoforms 2 and 3 are the primary targets for phosphorylation in rat prolactin.
    • These findings provide molecular insights into the post-translational modifications of rat prolactin.

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