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Altersolanol A: a selective cytotoxic anthraquinone from a P homopsis sp.
Author(s) -
Mishra P.D.,
Verekar S.A.,
Deshmukh S.K.,
Joshi K.S.,
Fiebig H.H.,
Kelter G.
Publication year - 2015
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/lam.12384
Subject(s) - phomopsis , cytotoxic t cell , biology , botany , microbiology and biotechnology , stereochemistry , chemistry , genetics , in vitro
Abstract The cytotoxic compound Altersolanol A, an anthraquinone derivative was isolated from PM 0409092 a fungus of Nyctanthes arbor‐tristis (family Oleaceae). It was identified as a Phomopsis sp. by DNA amplification and sequencing of the ITS region. The chemical structure of Altersolanol A was elucidated from its physicochemical properties, 2D NMR spectroscopy and other spectroscopic data. The compound has in vitro cytotoxic activity against 34 human cancer cell lines with mean IC 50 ( IC 70 ) values of 0·005 μ g ml −1 (0·024 μ g ml −1 ) respectively. Altersolanol A, a kinase inhibitor, induces cell death by apoptosis through the cleavage by Caspase‐3 and ‐9 and by decreased anti‐apoptotic protein expression. There are several previous reports of the anticancer activity of Altersolanol A, but we report here an extensive study using 36 cell lines which gives wider spectrum of results. Significance and Impact of the Study This study confirms the cytotoxic potential of Altersolanol A isolated from the endophyte Phomopsis sp. (PM0409092) of the plant Nyctanthes arbor‐tristis . The compound exhibits in vitro cytotoxicity against 34 human cancer cell lines with mean IC 50 (IC 70 ) value of 0·005 μ g ml −1 (0·024 μ g ml −1 ). This is an in‐depth report of Altersolanol A against a panel of 34 human cancer cell lines and extends observations from previous studies indicating that Altersolanol A can be used for the development of chemotherapeutics. Altersolanol A, a kinase inhibitor, induces cell death by apoptosis through the cleavage of Caspase‐3 and ‐9 and by decreased anti‐apoptotic protein expression.