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J. Biol. Chem., Vol. 277, Issue 6, 4104-4109, February 8, 2002
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From the Department of Pathology and Laboratory Medicine,
University of Cincinnati College of Medicine,
Cincinnati, Ohio 45267
Bile salt-stimulated carboxyl ester lipase (CEL),
also called cholesterol esterase, is one of the major proteins secreted by the pancreas. The physiological role of CEL was originally thought
to be its mediation of dietary cholesterol absorption. However, recent
studies showed no difference between wild type and CEL knockout mice in
the total amount of cholesterol absorbed in a single meal. The current
study tests the hypothesis that CEL in the intestinal lumen may
influence the type of lipoproteins produced. A lipid emulsion
containing 4 mM phospholipid, 13.33 mM
[3H]triolein, and 2.6 mM
[14C]cholesterol in 19 mM taurocholate was
infused into the duodenum of lymph fistula CEL(+/+) and CEL(
Bile Salt-stimulated Carboxyl Ester Lipase Influences Lipoprotein
Assembly and Secretion in Intestine
A PROCESS MEDIATED VIA CERAMIDE HYDROLYSIS*
/) mice
at a rate of 0.3 ml/h. Results showed no difference between CEL(+/+)
and CEL(/) mice in the rate of cholesterol and triglyceride
transport from the intestinal lumen to the lymph. However, CEL(/)
mice produced predominantly smaller lipoproteins, whereas the CEL(+/+)
mice produced primarily large chylomicrons and very low density
lipoprotein. The proximal intestine of CEL(/) mice was also found
to possess significantly less ceramide hydrolytic activity than that
present in CEL(+/+) mice. By using Caco2 cells grown on Transwell
membranes as a model, sphingomyelinase treatment inhibited the
secretion of larger chylomicron-like lipoproteins without affecting
total cholesterol secretion. In contrast, the addition of CEL to the apical medium increased the amount of large lipoproteins produced and
alleviated the inhibition induced by sphingomyelinase. Taken together,
this study identified a novel and physiologically significant role for
CEL, namely the promotion of large chylomicron production in the
intestine. The mechanism appears to be mediated through CEL hydrolysis
of ceramide generated during the lipid absorption process.
*
This work was supported by National Institutes of Health
Grants DK54504 and HL66246.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Pathology and
Laboratory Medicine, University of Cincinnati College of Medicine, 231 Albert Sabin Way, Cincinnati, OH 45267-0529. Tel.: 513-558-9152; Fax:
513-558-2141; E-mail: Huidy@email.uc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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