PMID- 27510818
OWN - NLM
STAT- MEDLINE
DCOM- 20170131
LR  - 20170131
IS  - 1872-7786 (Electronic)
IS  - 0009-2797 (Linking)
VI  - 257
DP  - 2016 Sep 25
TI  - The effect of HDL-bound and free PON1 on copper-induced LDL oxidation.
PG  - 141-6
LID - S0009-2797(16)30324-6 [pii]
LID - 10.1016/j.cbi.2016.08.007 [doi]
AB  - Oxidative modification of LDL plays an important role in the development of 
      atherosclerosis. High-density lipoprotein (HDL) confers protection against 
      atherosclerosis and the antioxidative properties of paraoxonase 1 (PON1) has been 
      suggested to contribute to this effect of HDL. The PON1 exist in two major 
      polymorphic forms (Q and R), which regulate the concentration and activity of the 
      enzyme and alter its ability to prevent lipid oxidation. However, the association 
      of Q192R polymorphism with PON1's capacity to protect against LDL 
      lipoperoxidation is controversial. The aim of this study was to evaluate the 
      effects of the purified PON1 Q192R and the partially purified HDL-bound PON1 
      Q192R isoenzymes (HDL-PON1 Q192R) on LDL oxidation, with respect to their 
      arylesterase/homocysteine thiolactonase (HTLase) activities. Cupric ion-induced 
      LDL oxidation was reduced up to 48% by purified PON1 Q192, but only 33% by an 
      equivalent activity of PON1 R192. HDL-PON1 Q192 isoenzyme caused a 65% reduction, 
      whereas HDL-PON1 R192 isoenzyme caused only 46% reduction in copper ion-induced 
      LDL oxidation. These findings reflect the fact that PON1 Q and PON1 R allozymes 
      may have different protective characteristics against LDL oxidation. The 
      protection against LDL oxidation provided by HDL-PON1 Q192R isoenzymes is more 
      prominent than the purified soluble enzymes. Inhibition of the Ca(+2)-dependent 
      PON1 Q192R arylesterase/HTLase by the metal chelator EDTA, did not alter PON1's 
      ability to inhibit LDL oxidation. These studies indicate that the active site 
      involvement of the purified enzyme is not similar to the HDL-bound one, in terms 
      of both PON1 arylesterase/HTLase activity and the protection of LDL from copper 
      ion-induced oxidation. Moreover, PON1's ability to protect LDL from oxidation 
      does not seem to require calcium.
CI  - Copyright (c) 2016 Elsevier Ireland Ltd. All rights reserved.
FAU - Bayrak, Ahmet
AU  - Bayrak A
AD  - Department of Biochemistry, Faculty of Medicine, Ordu University, Turkey. 
      Electronic address: abayrak@odu.edu.tr.
FAU - Bayrak, Tulin
AU  - Bayrak T
AD  - Department of Biochemistry, Faculty of Medicine, Ordu University, Turkey.
FAU - Bodur, Ebru
AU  - Bodur E
AD  - Department of Biochemistry, Faculty of Medicine, Hacettepe University, Turkey.
FAU - Kilinc, Kamer
AU  - Kilinc K
AD  - Department of Biochemistry, Faculty of Medicine, TOBB University of Economics and 
      Technology, Turkey.
FAU - Demirpence, Ediz
AU  - Demirpence E
AD  - Department of Biochemistry, Faculty of Medicine, TOBB University of Economics and 
      Technology, Turkey.
LA  - eng
PT  - Journal Article
DEP - 20160807
PL  - Ireland
TA  - Chem Biol Interact
JT  - Chemico-biological interactions
JID - 0227276
RN  - 0 (Isoenzymes)
RN  - 0 (Lipoproteins, HDL)
RN  - 0 (Lipoproteins, LDL)
RN  - 0 (oxidized low density lipoprotein)
RN  - 789U1901C5 (Copper)
RN  - EC 3.1.1.- (Carboxylic Ester Hydrolases)
RN  - EC 3.1.1.2 (arylesterase)
RN  - EC 3.1.8.1 (Aryldialkylphosphatase)
RN  - EC 3.1.8.1 (PON1 protein, human)
SB  - IM
MH  - Aryldialkylphosphatase/genetics/metabolism/*pharmacology
MH  - Carboxylic Ester Hydrolases/metabolism
MH  - Copper/pharmacology
MH  - Humans
MH  - Isoenzymes/pharmacology
MH  - Lipoproteins, HDL/*metabolism/pharmacology
MH  - Lipoproteins, LDL/drug effects/*metabolism
MH  - Oxidation-Reduction
MH  - Polymorphism, Single Nucleotide
MH  - Protein Binding
OTO - NOTNLM
OT  - High density lipoprotein
OT  - Low-density lipoprotein oxidation
OT  - PON1 polymorphism
OT  - Paraoxonase 1
OT  - Purification
EDAT- 2016/08/12 06:00
MHDA- 2017/02/01 06:00
CRDT- 2016/08/12 06:00
PHST- 2016/05/03 00:00 [received]
PHST- 2016/07/18 00:00 [revised]
PHST- 2016/08/05 00:00 [accepted]
PHST- 2016/08/12 06:00 [entrez]
PHST- 2016/08/12 06:00 [pubmed]
PHST- 2017/02/01 06:00 [medline]
AID - S0009-2797(16)30324-6 [pii]
AID - 10.1016/j.cbi.2016.08.007 [doi]
PST - ppublish
SO  - Chem Biol Interact. 2016 Sep 25;257:141-6. doi: 10.1016/j.cbi.2016.08.007. Epub 
      2016 Aug 7.