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- 저자 : Gyo¨rgy Marko-Varga (검색결과 2 건)
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Kim, Dongyoung,Hwang, Hui-Yun,Kim, Jin Young,Lee, Ju Yeon,Yoo, Jong Shin,Marko-Varga, Gyö,rgy,Kwon, Ho Jeong American Chemical Society 2017 JOURNAL OF PROTEOME RESEARCH Vol.16 No.1
<P>The drug FK506 (tacrolimus, fujimycin) exerts its immunosuppressive effects by regulating the nuclear factor of the activated T-cell (NFAT) family of transcription factors. However, FK506 also exhibits neuroprotective effects, but its direct target proteins that mediate these effects have not been determined. To identify the target proteins responsible for FK506's neuroprotective effects, the drug affinity responsive target stability (DARTS) method was performed using label free FK506, and LC-MS/MS analysis of the FK506-treated proteome was also performed. Using DARTS and LC-MS/MS analyses in combination with reference studied, V-ATPase catalytic subunit A (ATP6V1A) was identified as a new target protein of FK506. The biological relevance of ATP6V1A in mediating the neuroprotective effects of FK506 was validated by analyzing FK506 activity with respect to autophagy via acridine orange staining and transcription factor EB (TFEB) translocation assay. These analyses demonstrated that the binding of FK506 with ATP6V1A induces autophagy by activating the translocation of TFEB from the cytosol into the nucleus. Because autophagy has been identified as a mechanism for treating neurodegenerative diseases and because we have demonstrated that FK506 induces autophagy, this study demonstrates that'FK.506 is a possible new therapy for treating, neurodegenerative diseases.</P>
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Drug compound characterization by mass spectrometry imaging in cancer tissue
권호정,Johan Malm,김용효,Yutaka Sugihara,Bo Baldetorp,Charlotte Welinder,Ken-ichi Watanabe,Toshihide Nishimura,Gyo¨rgy Marko-Varga,Szilvia To¨ro¨k,Bala´zs Do¨me,´ kos Ve´gva´ri,Lena Gustavsson,Thomas E. Feh 대한약학회 2015 Archives of Pharmacal Research Vol.38 No.9
MALDI mass spectrometry imaging (MSI)provides a technology platform that allows the accuratevisualization of unlabeled small molecules within the twodimensionalspaces of tissue samples. MSI has proven to bea powerful tool-box concept in the development of newdrugs. MSI allows unlabeled drug compounds and drugmetabolites to be detected and identified and quantifiedaccording to their mass-to-charge ratios (m/z) at high resolutionin complex tissue environments. Such drug characterizationin situ, by both spatial and temporal behaviorswithin tissue compartments, provide new understandings ofthe dynamic processes impacting drug uptake and metabolismat the local sites targeted by therapy. Further, MSIin combination with histology and immunohistochemistry,provides the added value of defining the context of cellbiology present at the sites of drug localization thus providinginvaluable information relating to treatment efficacy. In this report we provide mass spectrometry imagingdata within various cancers such as malignant melanoma inpatients administered with vemurafenib, a protein kinaseinhibitor that is targeting BRAF mutated proteins and thathas shown significant efficacy in restraining disease progression. We also provide an overview of other examplesof the new generation of targeted drugs, and demonstratethe data on personalized medicine drugs localization withintumor compartments within in vivo models. In these cancermodels we provide detailed data on drug and target proteinco-localization of YCG185 and sunitinib. These drugs aretargeting VEGFR2 within the angiogenesis mechanism. Our ability to resolve drug uptake at targeted sites ofdirected therapy provides important opportunities forincreasing our understanding about the mode of action ofdrug activity within the environment of disease.
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