Triacylglycerol hydrolase: role in intracellular lipid metabolism

被引：101

作者：

Dolinsky, VW

Gilham, D

Alam, M

Vance, DE

Lehner, R ^{[1
]}

机构：

[1] Univ Alberta, Heritage Med Res Ctr 328, Dept Pediat, CIHR Grp Mol & Cell Biol Lipids, Edmonton, AB T6G 2S2, Canada

[2] Univ Alberta, Heritage Med Res Ctr 328, Dept Cell Biol, CIHR Grp Mol & Cell Biol Lipids, Edmonton, AB T6G 2S2, Canada

[3] Univ Alberta, Heritage Med Res Ctr 328, Dept Biochem, CIHR Grp Mol & Cell Biol Lipids, Edmonton, AB T6G 2S2, Canada

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2004年 / 61卷 / 13期

关键词：

lipase; carboxylesterase; triacylglycerol; VLDL; liver; adipose; atherosclerosis;

D O I：

10.1007/s00018-004-3426-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent scientific advances have revealed the identity of several enzymes involved in the synthesis, storage and catabolism of intracellular neutral lipid storage droplets. An enzyme that hydrolyzes stored triacylglycerol (TG), triacylglycerol hydrolase (TGH), was purified from porcine, human and murine liver microsomes. In rodents, TGH is highly expressed in liver as well as heart, kidney, small intestine and adipose tissues, while in humans TGH is mainly expressed in the liver, adipose and small intestine. TGH localizes to the endoplasmic reticulum and lipid droplets. The TGH genes are located within a cluster of carboxylesterase genes on human and mouse chromosomes 16 and 8, respectively. TGH hydrolyzes stored TG, and in the liver, the lipolytic products are made available for VLDL-TG synthesis. Inhibition of TGH activity also inhibits TG and apolipoprotein B secretion by primary hepatocytes. A role for TGH in basal TG lipolysis in adipocytes has been proposed. TGH expression and activity is both developmentally and hormonally regulated. A model for the function of TGH is presented and discussed with respect to tissue specific functions.

引用

页码：1633 / 1651

页数：19

共 155 条

[11] Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: From binding promiscuity to selective inhibition [J].

Bencharit, S ;

Morton, CL ;

Hyatt, JL ;

Kuhn, P ;

Danks, MK ;

Potter, PM ;

Redinbo, MR .

CHEMISTRY & BIOLOGY, 2003, 10 (04) :341-349

[12]

BLANCHETTEMACKIE EJ, 1995, J LIPID RES, V36, P1211

[13]

BORCHARDT RA, 1987, J BIOL CHEM, V262, P16394

[14]

BOREN J, 1994, J BIOL CHEM, V269, P25879

[15] Apo B100-containing lipoproteins are secreted by the heart [J].

Borén, J ;

Véniant, MM ;

Young, SG .

JOURNAL OF CLINICAL INVESTIGATION, 1998, 101 (06) :1197-1202

[16] Perilipin A increases triacylglycerol storage by decreasing the rate of triacylglycerol hydrolysis [J].

Brasaemle, DL ;

Rubin, B ;

Harten, IA ;

Gruia-Gray, J ;

Kimmel, AR ;

Londos, C .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (49) :38486-38493

[17] PURIFICATION AND CHARACTERIZATION OF A HUMAN LIVER COCAINE CARBOXYLESTERASE THAT CATALYZES THE PRODUCTION OF BENZOYLECGONINE AND THE FORMATION OF COCAETHYLENE FROM ALCOHOL AND COCAINE [J].

BRZEZINSKI, MR ;

ABRAHAM, TL ;

STONE, CL ;

DEAN, RA ;

BOSRON, WF .

BIOCHEMICAL PHARMACOLOGY, 1994, 48 (09) :1747-1755

[18] Mammalian acyl-CoA: cholesterol acyltransferases [J].

Buhman, KF ;

Accad, M ;

Farese, RV .

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, 2000, 1529 (1-3) :142-154

[19] INTRACELLULAR EVENTS IN THE ASSEMBLY OF VERY-LOW-DENSITY-LIPOPROTEIN LIPIDS WITH APOLIPOPROTEIN-B IN ISOLATED RABBIT HEPATOCYTES [J].

CARTWRIGHT, IJ ;

HIGGINS, JA .

BIOCHEMICAL JOURNAL, 1995, 310 :897-907

[20] Translocation of hormone-sensitive lipase and perilipin upon lipolytic stimulation of rat adipocytes [J].

Clifford, GM ;

Londos, C ;

Kraemer, FB ;

Vernon, RG ;

Yeaman, SJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (07) :5011-5015

← 1 2 3 4 5 6 7 8 9 10 →