In vitro inhibitory effects of palonosetron hydrochloride, bevacizumab and cyclophosphamide on purified paraoxonase-I (hPON1) from human serum

被引：50

作者：

Turkes, Cuneyt ^{[1
]}

Soyut, Hakan ^{[2
]}

Beydemir, Sukru ^{[1
]}

机构：

[1] Ataturk Univ, Dept Chem, Fac Sci, TR-25240 Erzurum, Turkey

[2] Bayburt Univ, Dept Primary Educ, Fac Educ, TR-69000 Bayburt, Turkey

来源：

ENVIRONMENTAL TOXICOLOGY AND PHARMACOLOGY | 2016年 / 42卷

关键词：

Paraoxonase; Inhibition; Palonosetron hydrochloride; Bevacizumab; Cyclophosphamide; OXIDATIVE STRESS; PON1; ACTIVITY; POLYMORPHISMS; PURIFICATION; DRUGS; BROMOPHENOLS; CHOLESTEROL; ERYTHROCYTE; POPULATION; PLASMA;

D O I：

10.1016/j.etap.2015.11.024

中图分类号：

X [环境科学、安全科学];

学科分类号：

08 ; 0830 ;

摘要：

In this study, we investigated the effects of the drugs, palonosetron hydrochloride, bevacizumab and cyclophosphamide, on human serum paraoxonase-I (hPON1) enzyme activity in in vitro conditions. The enzyme was purified similar to 231-fold with 34.2% yield by using ammonium sulphate precipitation, DEAE-Sephadex A-50 ion-exchange chromatography and Sephadex G-200 gel-filtration chromatography from human serum. hPON1 exhibited a single protein band on the SDS polyacrylamide gel electrophoresis. The inhibition studies were performed on paraoxonase activity of palonosetron hydrochloride, bevacizumab and cyclophosphamide. K-i constants were found as 0.033 +/- 0.001, 0.0544 +/- 0.003 mM and 3.419 +/- 0.518 mM, respectively. Compared to the inhibition rates of the drugs, palonosetron hydrochloride has the maximum inhibition rate. However, inhibition mechanisms of the drugs were determined as noncompetitive by Lineweaver-Burk curves. (C) 2016 Elsevier B.V. All rights reserved.

引用

页码：252 / 257

页数：6

共 41 条

[1] Synthesis and paroxonase activities of novel bromophenols [J].

Akbaba, Yusuf ;

Turkes, Cuneyt ;

Polat, Leyla ;

Soyut, Hakan ;

Sahin, Ertan ;

Menzek, Abdullah ;

Goksu, Suleyman ;

Beydemir, Sukru .

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2013, 28 (05) :1073-1079

[2] Intravenous anesthetics inhibit human paraoxonase-1 (PON1) activity in vitro and in vivo [J].

Alici, Haci Ahmed ;

Ekinci, Deniz ;

Beydemir, Suekrue .

CLINICAL BIOCHEMISTRY, 2008, 41 (16-17) :1384-1390

[3] CYP17, GSTP1, PON1 and GLO1 gene polymorphisms as risk factors for breast cancer: an Italian case-control study [J].

Antognelli, Cinzia ;

Del Buono, Chiara ;

Ludovini, Vienna ;

Gori, Stefania ;

Talesa, Vincenzo N. ;

Crino, Lucio ;

Barberini, Francesco ;

Rulli, Antonio .

BMC CANCER, 2009, 9

[4]

Arpaci A, 2009, IN VIVO, V23, P421

[5] Paraoxonases 1, 2, and 3, oxidative stress, and macrophage foam cell formation during atherosclerosis development [J].

Aviram, M ;

Rosenblat, M .

FREE RADICAL BIOLOGY AND MEDICINE, 2004, 37 (09) :1304-1316

[6] Synthesis and carbonic anhydrase inhibitory properties of novel bromophenols including natural products [J].

Balaydin, Halis Turker ;

Soyut, Hakan ;

Ekinci, Deniz ;

Goksu, Suleyman ;

Beydemir, Sukru ;

Menzek, Abdullah ;

Sahin, Ertan .

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2012, 27 (01) :43-50

[7] Aspirin use is associated with higher serum concentrations of the anti-oxidant enzyme, paraoxonase-1 [J].

Blatter-Garin, MC ;

Kalix, B ;

De Pree, S ;

James, RW .

DIABETOLOGIA, 2003, 46 (04) :593-594

[8]

Ciftci M, 2008, ASIAN J CHEM, V20, P2189

[9] Structural organization of the human PON1 gene [J].

Clendenning, JB ;

Humbert, R ;

Green, ED ;

Wood, C ;

Traver, D ;

Furlong, CE .

GENOMICS, 1996, 35 (03) :586-589

[10]

Çoban TA, 2008, J ENZYM INHIB MED CH, V23, P266, DOI [10.1080/14756360701474780 , 10.1080/14756360701474780]

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