<i>In vitro</i> efficacy of some cattle drugs on bovine serum paraoxonase 1 (PON1) activity

Arslan, Mikail; Gençer, Nahit; Arslan, Oktay; Guler, Ozen Ozensoy

doi:10.3109/14756366.2011.611135

Cited by 19 publications

(9 citation statements)

References 43 publications

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“…The IC 50 values obtained varied markedly from 0.014 to 507.72 mg/mL. According to these findings, most potent and significant inhibition was displayed by dexamethasone, atropine sulfate, and furosemid 54 .…”

Section: Resultsmentioning

confidence: 81%

“…PON is also a drug target [40][41][42][43] . We have performed a number of studies regarding the interactions of different inhibitors with several such enzymes, including PON1 [44][45][46][47][48][49][50] . Sinan et al showed that gentamycin sulfate and cefazolin sodium salt inhibited human serum PON1 dose and time dependently, with IC 50 values of 0.887 and 0.0084 mM, respectively, but did not affect liver PON1 activity in human hepatoma HepG2 cells 16 .…”

Section: Resultsmentioning

confidence: 99%

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An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

Demir

Gençer

Arslan

2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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In this study, an alternative purification method for human paraoxonase 1 (hPON1) enzyme was developed using two-step procedures, namely, ammonium sulfate precipitation and Sepharose-4B-L-tyrosine-3-aminophenantrene hydrophobic interaction chromatography. SDS-polyacrylamide gel electrophoresis of the enzyme indicates a single band with an apparent M(W) of 43 kDa. The enzyme was purified 219-fold with a final specific activity of 4,408,400 U/mg and a yield of 10%. Furthermore, we examined the in vitro effects of some anabolic compounds, such as zeranol, 17 β-estradiol, diethylstilbestrol, oxytocin, and trenbolone on the enzyme activity to understand the better inhibitory properties of these molecules. The five anabolic compounds dose dependently decreased the activity of hPON1 with inhibition constants in the millimolar-micromolar range. The results show that these compounds exhibit inhibitory effects on hPON1 at low concentrations with IC50 values ranging from 0.064 to 16.900 µM.

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Section: Resultsmentioning

confidence: 81%

Section: Resultsmentioning

confidence: 99%

An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

Demir

Gençer

Arslan

2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Pharmacological studies, including enzyme-drug interaction analyses, are becoming increasingly vital important [25][26][27][28][29] . In a study, it was shown that a lactam derivative namely 2-hydroxyquinoline inhibited PON1 effectively 30 .…”

Section: Resultsmentioning

confidence: 99%

In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)

Gökçe

Gençer

Arslan

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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Human serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. In this study, in vitro effect of some hydroxy and dihydroxy ionic coumarin derivatives (1-20) on purified PON1 activity was investigated. Among these compounds, derivatives 11-20 are water soluble. In investigated compounds, compounds 6 and 13 were found the most active (IC 50 ¼ 35 and 34 mM) for PON1, respectively. The present study has demonstrated that PON1 activity is very highly sensitive to studied coumarin derivatives.

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“…Enzyme inhibition is an important issue for drug design and biochemical applications [45][46][47] . In this study, we have showed that human PON1 was inhibited effectively by some coumarin or benzoxazinone derivatives.…”

Section: Resultsmentioning

confidence: 99%

Some coumarins and benzoxazinones as potent paraoxonase 1 inhibitors

Karataş

Uslu

Alıcı

et al. 2016

Journal of Enzyme Inhibition and Medicinal Chemistry

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In this study, we aimed to investigate the effect of some coumarin and benzoxazinone derivatives on the activity of human PON1. Human serum paraoxonase 1 was purified from fresh human serum blood by two-step procedures that are ammonium sulfate precipitation (60-80%) and then hydrophobic interaction chromatography (Sepharose 4B, L-tyrosine and 1-napthylamine). The enzyme was purified 232-fold with a final specific activity of 27.1 U/mg. In vitro effects of some previously synthesized ionic coumarin or benzoxazinone derivatives (1-21) on purified PON1 activity were investigated. Compound 14 (1-(2,3,4,5,6)-pentamethylbenzyl-3-(6,8-dimethyl-2H-chromen-2-one-4-yl))benzimidazolium chloride was found out as the strongest inhibitor (IC 50 ¼ 7.84 mM) for PON1 among the compounds. Kinetic investigation and molecular docking study were evaluated for one of the most active compounds (compound 12) and obtained data showed that this compound is competitive inhibitor of PON1 and interact with Leu262 and Ser263 in the active site of PON1. Moreover, coumarin derivatives were found out as the more potent inhibitors for PON1 than benzoxazinone derivatives.

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In vitro efficacy of some cattle drugs on bovine serum paraoxonase 1 (PON1) activity

Cited by 19 publications

References 43 publications

An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)

Some coumarins and benzoxazinones as potent paraoxonase 1 inhibitors

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