Author

Shuqi Xie

Advisor

Ross, Matt K.

Committee Member

Crow, Allen

Committee Member

Chambers, Janice E.

Committee Member

Ross, Matthew K.

Date of Degree

1-1-2009

Document Type

Graduate Thesis - Open Access

Degree Name

Master of Science

College

College of Veterinary Medicine

Department

Department of Basic Sciences

Abstract

Carboxylesterases (CEs) are nonspecific hydrolytic enzymes and responsible for the metabolism of xenobiotics and endobiotics that contain ester bonds. There are two human CE isoforms found in liver, CES1 and CES2. In this study it is shown that the mere abundance of CES1 protein expression in human liver does not predict its biochemical activity. The human interindividual variation in CES1 activities may attribute to several mechanisms. One possibility is the presence of endogenous inhibitors in liver, arachidonic acid (AA) and 27-hydroxycholesterol (27-HC). CES1 is also expressed in human monocytes/macrophages and is proposed to catalyze the rate-limiting step of cholesterol ester mobilization in macrophages. It is of interest to determine whether CES1 can degrade the lipid mediators, 2-arachidonoylglycerol (2-AG), prostaglandin E2-1-glyceryl ester (PGE2-G), and prostaglandin F2α-1-glyceryl ester (PGF2α-G), in monocytes/macrophages and to determine if this metabolism is inhibited by organophosphate pesticide exposure.

URI

https://hdl.handle.net/11668/17065

Comments

Organophosphates||Interindividual variation||Carboxylesterases||CES1||Lipid mediators||Endogenous inhibitors

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