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    The protein acetyltransferase ARD1: a novel cancer drug target

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    Authors
    Arnesen, Thomas
    Thompson, Paul R
    Varhaug, Jan Erik.
    Lillehaug, Johan R.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2008-11-01
    Keywords
    Acetyltransferases
    Animals
    Antineoplastic Agents
    Apoptosis
    Cell Line, Tumor
    Drug Delivery Systems
    Enzyme Inhibitors
    Growth Inhibitors
    Humans
    N-Terminal Acetyltransferase A
    N-Terminal Acetyltransferase E
    Neoplasms
    hARD1
    NATH
    cell cycle arrest
    apoptosis
    protein acetylation
    N-terminal
    co-translational
    HIF-1α
    Biochemistry
    Enzymes and Coenzymes
    Medicinal-Pharmaceutical Chemistry
    Neoplasms
    Therapeutics
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    Link to Full Text
    http://dx.doi.org/10.2174/156800908786241113
    Abstract
    Evasion of apoptosis and active cell proliferation are among the characteristics of cancer cells. Triggering the induction of apoptosis or reducing the proliferative rate will potentially be helpful for cancer treatment. Recently, several reports demonstrated that knockdown of the protein acetyltransferase hARD1 significantly reduced the growth rate of human cancer cell lines. Furthermore, hARD1 knockdown induced apoptosis or sensitized cells to drug induced apoptosis. hARD1 acts in complex with the NATH protein and catalyzes cotranslational acetylation of protein N-termini. Thus, it was suggested that the effects on cell proliferation and apoptosis induction are due to a reduced level of N-terminal acetylation of certain substrate proteins. NATH was originally identified as upregulated in thyroid papillary carcinomas and has lately also been found to correlate with aggressiveness and differentiation status of neuroblastic tumours. On the other hand, researchers recently reported that hARD1 acetylates Beta-catenin. Knockdown of hARD1 reduced the transcriptional activity of the Beta-Catenin/TCF4 complex, downregulating cyclin D1 and thereby promoting G1-arrest and inhibition of cell proliferation of lung cancer cells. Although the underlying molecular mechanisms need further clarification, several reports suggest that reduction of hARD1 negatively affects cell growth. Thus, hARD1 or the hARD1-NATH complex stands out as attractive drug targets in cancer treatment. One challenge will be to develop specific inhibitors that discriminate between hARD1 and the many other enzymes, including the histone acetyltransferases, using acetyl-coenzyme A as acetyl donor. This review focuses on the enzymatic and biological activities of hARD1, and potential mechanisms of functional inhibition.
    Source
    Curr Cancer Drug Targets. 2008 Nov;8(7):545-53. doi:10.2174/156800908786241113
    DOI
    10.2174/156800908786241113
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50057
    Notes

    At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

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    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.2174/156800908786241113
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