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Expression of Concern: Laccase treatment impairs bisphenol A‐induced cancer cell proliferation affecting estrogen receptor α‐dependent rapid signals
Author(s) -
Bolli Alessandro,
Galluzzo Paola,
Ascenzi Paolo,
Del Pozzo Giovanna,
Manco Immacolata,
Vietri Maria Teresa,
Mita Luigi,
Altucci Lucia,
Mita Damiano Gustavo,
Marino Maria
Publication year - 2008
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.130
Subject(s) - estrogen receptor , laccase , cell growth , cancer cell , chemistry , protein kinase b , estrogen , signal transduction , estrogen receptor alpha , biochemistry , biology , cancer research , microbiology and biotechnology , enzyme , cancer , endocrinology , genetics , breast cancer
A wide variety of environmental contaminants exert estrogenic actions in wildlife, laboratory animals, and in human beings through binding to nuclear estrogen receptors (ERs). Here, the mechanism(s) of bisphenol A (BPA) to induce cell proliferation and the occurrence of its bioremediation by treatment with laccase are reported. BPA, highly present in natural world and considered as a model of environmental estrogen action complexity, promotes human cancer cell proliferation via ERα‐dependent signal transduction pathways. Similar to 17β‐estradiol, BPA increases the phosphorylation of both extracellular regulated kinase and AKT. Specific inhibitors of these kinase completely block the BPA effect on cancer cell proliferation. Notably, high BPA concentrations ( i.e., 0.1 and 1 mM) are cytotoxic even in ERα‐devoid cancer cells, indicating that an ERα‐independent mechanism participates to BPA‐induced cytotoxicity. On the other hand, BPA oxidation by laccase impairs the binding of this environmental estrogen to ERα loosing at all ERα‐dependent effect on cancer cell proliferation. Moreover, the laccase‐catalyzed oxidation of BPA reduces the BPA cytotoxic effect. Thus, laccase appears to impair BPA action(s), representing an invaluable bioremediation enzyme. © 2008 IUBMB IUBMB Life, 60(12): 843–852, 2008