2011
DOI: 10.1016/j.bbalip.2010.10.002
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Mouse serum paraoxonase-1 lactonase activity is specific for medium-chain length fatty acid lactones

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Cited by 6 publications
(3 citation statements)
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“…The remaining two isozymes, PON1 and PON3, found in the liver and blood, show lower activity toward HSLs. Their primary substrates seem to be ␦-lactones and/or ␥-lactones with lipophilic side chains (49,50,55).…”
Section: Serum Paraoxonasesmentioning
confidence: 99%
“…The remaining two isozymes, PON1 and PON3, found in the liver and blood, show lower activity toward HSLs. Their primary substrates seem to be ␦-lactones and/or ␥-lactones with lipophilic side chains (49,50,55).…”
Section: Serum Paraoxonasesmentioning
confidence: 99%
“…They hydrolyze a wide range of ␦-and ␥-lactones with lipophilic side chains (fatty acid lactones or lipolactones; Fig. 1 (4,21). PON1 and PON3 also hydrolyze the quorum-sensing lactone 3OC12-HSL, yet with much lower efficiency (17).…”
mentioning
confidence: 99%
“…Paraoxonase 1 (PON1) is a calcium-dependent esterase synthesized in the liver and circulating in the blood attached to high-density lipoproteins (HDL). PON1 protects plasma lipoproteins including low-density lipoproteins (LDL) and HDL themselves from oxidative modification by decomposing lipid peroxidation products such as fatty acid lactones [ 6 ]. In addition, PON1 hydrolyzes homocysteine (Hcy) thiolactone both in vitro [ 7 ] and in vivo [ 8 , 9 ].…”
Section: Introductionmentioning
confidence: 99%