The actions of cyclic AMP on biosynthetic processes are mediated indirectly by cyclic AMP-dependent protein kinase

    Research output: Contribution to journalReview article

    43 Citations (Scopus)

    Abstract

    Adrenalin and glucagon inhibit glycogen, fatty acid and cholesterol synthesis by elevation of cyclic AMP, activation of cyclic AMP-dependent protein kinase and increased phosphorylation of the rate-limiting enzymes of these pathways. Here, we review recent evidence which indicates that inhibition of these biosynthetic pathways in muscle, adipose tissue and liver is much more indirect than has previously been supposed. In particular, cyclic AMP-dependent protein kinase does not appear to inhibit glycogen synthase, acetyl-CoA carboxylase and HMG-CoA reductase by phosphorylating them directly. It appears to achieve the same end result by inactivation of the protein phosphatases which dephosphorylate these regulatory enzymes in vivo, although this has only been established definitively in the case of glycogen synthesis.

    Original languageEnglish
    Pages (from-to)292-299
    Number of pages8
    JournalBBA - Molecular Cell Research
    Volume1094
    Issue number3
    DOIs
    Publication statusPublished - 24 Sep 1991

    Fingerprint

    Cyclic AMP-Dependent Protein Kinases
    Glycogen
    Cyclic AMP
    Hydroxymethylglutaryl CoA Reductases
    Acetyl-CoA Carboxylase
    Glycogen Synthase
    Phosphoprotein Phosphatases
    Biosynthetic Pathways
    Enzymes
    Glucagon
    Epinephrine
    Adipose Tissue
    Fatty Acids
    Cholesterol
    Phosphorylation
    Muscles
    Liver

    Keywords

    • Cholesterol synthesis
    • cyclic AMP
    • Fatty acid synthesis
    • Glycogen metabolism
    • Protein kinase

    Cite this

    @article{e62f50e90e194118a6884660b05eb320,
    title = "The actions of cyclic AMP on biosynthetic processes are mediated indirectly by cyclic AMP-dependent protein kinase",
    abstract = "Adrenalin and glucagon inhibit glycogen, fatty acid and cholesterol synthesis by elevation of cyclic AMP, activation of cyclic AMP-dependent protein kinase and increased phosphorylation of the rate-limiting enzymes of these pathways. Here, we review recent evidence which indicates that inhibition of these biosynthetic pathways in muscle, adipose tissue and liver is much more indirect than has previously been supposed. In particular, cyclic AMP-dependent protein kinase does not appear to inhibit glycogen synthase, acetyl-CoA carboxylase and HMG-CoA reductase by phosphorylating them directly. It appears to achieve the same end result by inactivation of the protein phosphatases which dephosphorylate these regulatory enzymes in vivo, although this has only been established definitively in the case of glycogen synthesis.",
    keywords = "Cholesterol synthesis, cyclic AMP, Fatty acid synthesis, Glycogen metabolism, Protein kinase",
    author = "Philip Cohen and {Grahame Hardie}, D.",
    year = "1991",
    month = "9",
    day = "24",
    doi = "10.1016/0167-4889(91)90089-G",
    language = "English",
    volume = "1094",
    pages = "292--299",
    journal = "Biochimica et Biophysica Acta. Molecular Cell Research",
    issn = "0167-4889",
    publisher = "Elsevier",
    number = "3",

    }

    TY - JOUR

    T1 - The actions of cyclic AMP on biosynthetic processes are mediated indirectly by cyclic AMP-dependent protein kinase

    AU - Cohen, Philip

    AU - Grahame Hardie, D.

    PY - 1991/9/24

    Y1 - 1991/9/24

    N2 - Adrenalin and glucagon inhibit glycogen, fatty acid and cholesterol synthesis by elevation of cyclic AMP, activation of cyclic AMP-dependent protein kinase and increased phosphorylation of the rate-limiting enzymes of these pathways. Here, we review recent evidence which indicates that inhibition of these biosynthetic pathways in muscle, adipose tissue and liver is much more indirect than has previously been supposed. In particular, cyclic AMP-dependent protein kinase does not appear to inhibit glycogen synthase, acetyl-CoA carboxylase and HMG-CoA reductase by phosphorylating them directly. It appears to achieve the same end result by inactivation of the protein phosphatases which dephosphorylate these regulatory enzymes in vivo, although this has only been established definitively in the case of glycogen synthesis.

    AB - Adrenalin and glucagon inhibit glycogen, fatty acid and cholesterol synthesis by elevation of cyclic AMP, activation of cyclic AMP-dependent protein kinase and increased phosphorylation of the rate-limiting enzymes of these pathways. Here, we review recent evidence which indicates that inhibition of these biosynthetic pathways in muscle, adipose tissue and liver is much more indirect than has previously been supposed. In particular, cyclic AMP-dependent protein kinase does not appear to inhibit glycogen synthase, acetyl-CoA carboxylase and HMG-CoA reductase by phosphorylating them directly. It appears to achieve the same end result by inactivation of the protein phosphatases which dephosphorylate these regulatory enzymes in vivo, although this has only been established definitively in the case of glycogen synthesis.

    KW - Cholesterol synthesis

    KW - cyclic AMP

    KW - Fatty acid synthesis

    KW - Glycogen metabolism

    KW - Protein kinase

    UR - http://www.scopus.com/inward/record.url?scp=0025800169&partnerID=8YFLogxK

    U2 - 10.1016/0167-4889(91)90089-G

    DO - 10.1016/0167-4889(91)90089-G

    M3 - Review article

    C2 - 1655040

    AN - SCOPUS:0025800169

    VL - 1094

    SP - 292

    EP - 299

    JO - Biochimica et Biophysica Acta. Molecular Cell Research

    JF - Biochimica et Biophysica Acta. Molecular Cell Research

    SN - 0167-4889

    IS - 3

    ER -