Publications by authors named "Mika Araki"
Article Synopsis
- Glutathione transferases (GSTs) are often overexpressed in tumors, leading to poorer prognosis and resistance to cancer drugs; the study aims to create prodrugs that target these GST-overexpressing cells while sparing normal cells.
- Newly synthesized compounds like ANS-etoposide and ANS-DOX effectively target cell lines overexpressing GSTA1 and MGST1, with ANS-DOX showing significant cytotoxicity and DNA damage in a GST-dependent manner.
- The mechanism of action involves reducing glutathione (GSH) levels and inhibiting the enzyme thioredoxin reductase 1 (TrxR1), both of which are linked to chemotherapy resistance and poor outcomes
We have synthesized a series of 4-substituted-2-nitrobenzene-sulfonyl compounds for caged fluorogenic probes and conducted a Hammett plot analysis using the steady-state kinetic parameters. The results revealed that the glutathione transferase (GST) alpha catalyzed reaction was dependent on the σ value in the same way as the non-enzymatic reaction, whereas the dependence of the σ value of the GST mu and pi was not as pronounced as that of GST alpha.
View Article and Find Full Text PDFSoapfishes contain peptide toxins (grammistins) in the skin secretion. Two grammistins (Gs 1 and Gs 2) and six grammistins (Pp 1, Pp 2a, Pp 2b, Pp 3, Pp 4a and Pp 4b) have already been isolated from Grammistes sexlineatus and Pogonoperca punctata, respectively. In this study, five grammistins (Gs A-E), together with grammistins Gs 1 and Gs 2, were further isolated from G.
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