کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7557164 | 1491308 | 2017 | 32 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Development of amide-based fluorescent probes for selective measurement of carboxylesterase 1 activity in tissue extracts
ترجمه فارسی عنوان
توسعه پروب های فلورسنت مبتنی بر آمید برای اندازه گیری انتخابی فعالیت کربوکسی استراز 1 در عصاره های بافت
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کلمات کلیدی
4-NPA4-nitrophenyl acetatePON2PON1maglCarboxylesterase 1FAAHhCE1Carboxylesterase 2AADACPON3arylacetamide deacetylase - آرییلات آمید دیازتیلازAminopyridines - آمینوپیریدین هاAChE - آهیAcetylcholinesterase - استیل کولین استرازFatty acid amide hydrolase - اسید آمینه هیدرولاز اسید چربFluorescent substrate - بستر فلورسنتELISA - تست الیزاEnzyme-linked immunosorbent assay - تست الیزاmonoacylglycerol lipase - لیپاز monoacylglycerol لیپازParaoxonase 1 - پاراکسوناز 1Paraoxonase 2 - پاراکسوناز 2
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی
Carboxylesterases are well known for their role in the metabolism of xenobiotics. However, recent studies have also implicated carboxylesterases in regulating a number of physiological processes including metabolic homeostasis and macrophage development, underlying the need to quantify them individually. Unfortunately, current methods for selectively measuring the catalytic activity of individual carboxylesterases are not sufficiently sensitive to support many biological studies. In order to develop a more sensitive and selective method to measure the activity of human carboxylesterase 1 (hCE1), we generated and tested novel substrates with a fluorescent aminopyridine leaving group. hCE1 showed at least a 10-fold higher preference for the optimized substrate 4-MOMMP than the 13 other esterases tested. Because of the high stability of 4-MOMMP and its hydrolysis product, this substrate can be used to measure esterase activity over extended incubation periods yielding a low picogram (femtomol) limit of detection. This sensitivity is comparable to current ELISA methods; however, the new assay quantifies only the catalytically active enzyme facilitating direct correlation to biological processes. The method described herein may allow hCE1 activity to be used as a biomarker for predicting drug pharmacokinetics, early detection of hepatocellular carcinoma, and other disease states where the activity of hCE1 is altered.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 539, 15 December 2017, Pages 81-89
Journal: Analytical Biochemistry - Volume 539, 15 December 2017, Pages 81-89
نویسندگان
Sean D. Kodani, Morgane Barthélemy, Shizuo G. Kamita, Bruce Hammock, Christophe Morisseau,