000			naa a22 7ar4500
005			20151027110733.0
008			150528t xxu||||| |||| 00| 0 tu d
001			265907
016			_a000313663400016
022			_a1475-6366
040			_aNEU
041			_aeng
050	0	4	_aQU4
100	1		_9574751 _aKulaksiz-Erkmen, Gulnihal.
245	1	0	_aAmitriptyline may have a supportive role in cancer treatment by inhibiting glutathione S-transferase pi (GST-pi) and alpha (GST-alpha) _cGülnihal Kulaksiz-Erkmen, Özlem Dalmizrak, Gamze Dincsoy-Tuna, Arın Doğan, I. Hamdi Oğuş, Nazmi Özer
260			_bInforma Healthcare, _c2013.
520			_aA tricyclic anti-depressant, amitriptyline, is a highly prescribed drug for cancer patients for mood elevation but there are limited studies about the interaction of amitriptyline with glutathione S-transferases pi (GST-pi) and glutathione S-transferases alpha (GST-alpha). GST isozymes have been implicated in chemotherapeutic drug resistance. We demonstrated that the concentration dependent inhibition of GST-pi and GST-alpha by amitriptyline followed inverse hyperbolic inhibition curves with IC50 values of 5.54 and 8.32 mM, respectively. When the varied substrate was GSH, amitriptyline inhibited both isozymes competitively and similar K-i values were found for GST-pi (K-i = 1.61 +/- 0.17 mM) and GST-alpha (K-i = 1.45 +/- 0.20 mM). On the other hand, when the varied substrate was CDNB, the inhibition types were non-competitive for GST-pi (K-i = 1.98 +/- 0.31 mM) and competitive for GST-alpha (K-i = 1.57 +/- 0.16 mM). Amitriptyline, in addition to its antidepressant effect, might also have a minor supportive role on the effectiveness of the anticancer drugs by decreasing their elimination through inhibiting GST-pi and GST-alpha.
650		0	_9572720 _aNear East University Article
650		0	_9572723 _aYakın Doğu Üniversitesi Makale
650			_9117600 _aBiochemistry
650			_9574753 _aanticancer drugs;
650			_9574754 _aGST-alpha;
650			_9574755 _aSerotonın
650			_9574756 _aTransporters
773			_gFeb 2013, Volume: 28, Issue:1, Pages: 131-136 _tJournal Of Enzyme Inhıbıtıon And Medıcınal Chemıstry _x14756366
856			_uhttp://library.neu.edu.tr:2048/login?url=http://dx.doi.org/10.3109/14756366.2011.639017
942			_x1000005 _kQU0000004A452013 _cOED
999			_c242593