Carboxylesterases in lipid metabolism: from mouse to human

ABSTRACT Mammalian carboxylesterases hydrolyze a wide range of xenobiotic and endogenous compounds, including lipid esters. Physiological functions of carboxylesterases in lipid metabolism and energy homeostasis in vivo have been demonstrated by genetic manipulations and chemical inhibition in mice,...

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Main Authors: Jihong Lian, Randal Nelson, Richard Lehner
Format: Article
Language:English
Published: Oxford University Press 2017-07-01
Series:Protein & Cell
Subjects:
Online Access:http://link.springer.com/article/10.1007/s13238-017-0437-z
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author Jihong Lian
Randal Nelson
Richard Lehner
author_facet Jihong Lian
Randal Nelson
Richard Lehner
author_sort Jihong Lian
collection DOAJ
description ABSTRACT Mammalian carboxylesterases hydrolyze a wide range of xenobiotic and endogenous compounds, including lipid esters. Physiological functions of carboxylesterases in lipid metabolism and energy homeostasis in vivo have been demonstrated by genetic manipulations and chemical inhibition in mice, and in vitro through (over)expression, knockdown of expression, and chemical inhibition in a variety of cells. Recent research advances have revealed the relevance of carboxylesterases to metabolic diseases such as obesity and fatty liver disease, suggesting these enzymes might be potential targets for treatment of metabolic disorders. In order to translate pre-clinical studies in cellular and mouse models to humans, differences and similarities of carboxylesterases between mice and human need to be elucidated. This review presents and discusses the research progress in structure and function of mouse and human carboxylesterases, and the role of these enzymes in lipid metabolism and metabolic disorders.
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spelling doaj.art-0a50138711574388ad9f5bfd123128aa2023-09-02T09:00:27ZengOxford University PressProtein & Cell1674-800X1674-80182017-07-019217819510.1007/s13238-017-0437-zCarboxylesterases in lipid metabolism: from mouse to humanJihong Lian0Randal Nelson1Richard Lehner2Group on Molecular and Cell Biology of Lipids, University of AlbertaGroup on Molecular and Cell Biology of Lipids, University of AlbertaGroup on Molecular and Cell Biology of Lipids, University of AlbertaABSTRACT Mammalian carboxylesterases hydrolyze a wide range of xenobiotic and endogenous compounds, including lipid esters. Physiological functions of carboxylesterases in lipid metabolism and energy homeostasis in vivo have been demonstrated by genetic manipulations and chemical inhibition in mice, and in vitro through (over)expression, knockdown of expression, and chemical inhibition in a variety of cells. Recent research advances have revealed the relevance of carboxylesterases to metabolic diseases such as obesity and fatty liver disease, suggesting these enzymes might be potential targets for treatment of metabolic disorders. In order to translate pre-clinical studies in cellular and mouse models to humans, differences and similarities of carboxylesterases between mice and human need to be elucidated. This review presents and discusses the research progress in structure and function of mouse and human carboxylesterases, and the role of these enzymes in lipid metabolism and metabolic disorders.http://link.springer.com/article/10.1007/s13238-017-0437-zcarboxylesteraselipaselipidlipoproteinliveradipose
spellingShingle Jihong Lian
Randal Nelson
Richard Lehner
Carboxylesterases in lipid metabolism: from mouse to human
Protein & Cell
carboxylesterase
lipase
lipid
lipoprotein
liver
adipose
title Carboxylesterases in lipid metabolism: from mouse to human
title_full Carboxylesterases in lipid metabolism: from mouse to human
title_fullStr Carboxylesterases in lipid metabolism: from mouse to human
title_full_unstemmed Carboxylesterases in lipid metabolism: from mouse to human
title_short Carboxylesterases in lipid metabolism: from mouse to human
title_sort carboxylesterases in lipid metabolism from mouse to human
topic carboxylesterase
lipase
lipid
lipoprotein
liver
adipose
url http://link.springer.com/article/10.1007/s13238-017-0437-z
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AT randalnelson carboxylesterasesinlipidmetabolismfrommousetohuman
AT richardlehner carboxylesterasesinlipidmetabolismfrommousetohuman