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    Cytosolic phospholipase A2 activation correlates with HER2 overexpression and mediates estrogen-dependent breast cancer cell growth.

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    Authors
    Caiazza, Francesco
    Harvey, Brian J
    Thomas, Warren
    Affiliation
    Department of Molecular Medicine, Royal College of Surgeons in Ireland, Education and Research Centre, Beaumont Hospital, Dublin 9, Ireland.
    Issue Date
    2010-05
    MeSH
    Blotting, Western
    Breast Neoplasms
    Cell Line, Tumor
    Cell Proliferation
    Estradiol
    Estrogens
    Gene Expression Regulation, Neoplastic
    Group IV Phospholipases A2
    Humans
    Immunoprecipitation
    Phosphorylation
    Protein Binding
    RNA Interference
    Receptor, erbB-2
    Reverse Transcriptase Polymerase Chain Reaction
    Signal Transduction
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    Citation
    Cytosolic phospholipase A2 activation correlates with HER2 overexpression and mediates estrogen-dependent breast cancer cell growth. 2010, 24 (5):953-68 Mol. Endocrinol.
    Journal
    Molecular endocrinology (Baltimore, Md.)
    URI
    http://hdl.handle.net/10147/127133
    DOI
    10.1210/me.2009-0293
    PubMed ID
    20211985
    Abstract
    Cytosolic phospholipase A(2)alpha (cPLA(2)alpha) catalyzes the hydrolysis of membrane glycerol-phospholipids to release arachidonic acid as the first step of the eicosanoid signaling pathway. This pathway contributes to proliferation in breast cancer, and numerous studies have demonstrated a crucial role of cyclooxygenase 2 and prostaglandin E(2) release in breast cancer progression. The role of cPLA(2)alpha activation is less clear, and we recently showed that 17beta-estradiol (E2) can rapidly activate cPLA(2)alpha in MCF-7 breast cancer cells. Overexpression or gene amplification of HER2 is found in approximately 30% of breast cancer patients and correlates with a poor clinical outcome and resistance to endocrine therapy. This study reports the first evidence for a correlation between cPLA(2)alpha enzymatic activity and overexpression of the HER2 receptor. The activation of cPLA(2)alpha in response to E2 treatment was biphasic with the first phase dependent on trans-activation through the matrix metalloproteinase-dependent release of heparin-bound epidermal growth factor. EGFR/HER2 heterodimerization resulted in downstream signaling through the ERK1/2 cascade to promote cPLA(2)alpha phosphorylation at Ser505. There was a correlation between HER2 and cPLA(2)alpha expression in six breast cancer cell lines examined, and inhibition of HER2 activation or expression in the SKBR3 cell line using herceptin or HER2-specific small interfering RNA, respectively, resulted in decreased activation and expression of cPLA(2)alpha. Pharmacological blockade of cPLA(2)alpha using a specific antagonist suppressed the growth of both MCF-7 and SKBR3 cells by reducing E2-induced proliferation and by stimulating cellular apoptosis and necrosis. This study highlights cPLAalpha(2) as a potential target for therapeutic intervention in endocrine-dependent and endocrine-independent breast cancer.
    Item Type
    Article
    Language
    en
    ISSN
    1944-9917
    ae974a485f413a2113503eed53cd6c53
    10.1210/me.2009-0293
    Scopus Count
    Collections
    Beaumont Hospital

    entitlement

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