کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
11001775 | 1051446 | 2018 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Identification of biologically active δ-lactone eicosanoids as paraoxonase substrates
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کلمات کلیدی
GFPHEKPONHBSSAEBSFEicosanoid4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloridePAPc - PAPCEsterase - استرسPolyunsaturated fatty acid - اسید چرب غیر اشباعPUFA - اسید چرب چند غیراشباعIsoprostanes - ایزوپروتامین هاLactone - لاکتونParaoxonase - پاراکسونازgreen fluorescent protein - پروتئین فلورسنت سبزhuman embryonic kidney 293 - کلیه جنینی انسان 293
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The mammalian paraoxonases (PONs 1, 2 and 3) are a family of esterases that are highly conserved within and between species. They exhibit antioxidant and anti-inflammatory activities. However, their physiological function(s) and native substrates are uncertain. Previous structure-activity relationship studies demonstrate that PONs have a high specificity for lipophilic lactones, suggesting that such compounds may be representative of native substrates. This report describes the ability of PONs to hydrolyze two bioactive δ-lactones derived from arachidonic acid, 5,6-dihydroxy-eicosatrienoic acid lactone (5,6-DHTL) and cyclo-epoxycyclopentenone (cyclo-EC). Both lactones were very efficiently hydrolyzed by purified PON3. PON1 efficiently hydrolyzed 5,6-DHTL, but with a specific activity about 15-fold lower than PON3. 5,6-DHTL was a poor substrate for PON2. Cyclo-EC was a poor substrate for PON1 and not hydrolyzed by PON2. Studies with the PON inhibitor EDTA and a serine esterase inhibitor indicated that the PONs are the main contributors to hydrolysis of the lactones in human and mouse liver homogenates. Studies with homogenates from PON3 knockout mouse livers indicated that >80% of the 5,6-DHTL and cyclo-EC lactonase activities were attributed to PON3. The findings provide further insight into the structural requirements for PONs substrates and support the hypothesis that PONs, particularly PON1 and PON3, evolved to hydrolyze and regulate a class of lactone lipid mediators derived from polyunsaturated fatty acids.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 505, Issue 1, 20 October 2018, Pages 87-92
Journal: Biochemical and Biophysical Research Communications - Volume 505, Issue 1, 20 October 2018, Pages 87-92
نویسندگان
John F. Teiber, Junhui Xiao, Gerald L. Kramer, Seiji Ogawa, Christian Ebner, Helene Wolleb, Erick M. Carreira, Diana M. Shih, Robert W. Haley,