|
Journal of Lipid Research, Vol 31, 2029-2037, Copyright © 1990 by Lipid Research, Inc.
Metabolic fate of pancreas-derived cholesterol esterase in intestine: an in vitro study using Caco-2 cells
Y Huang and DY Hui
Department of Pathology and Laboratory Medicine, University of Cincinnati, College of Medicine, OH 45267-0529.
Bile salt-stimulated cholesterol esterase is synthesized in the pancreatic
acinar cells and is released into the intestinal lumen where it catalyzes
cholesterol absorption. In the current study, Caco-2 cells were used as an
in vitro model to study the interaction between the pancreatic cholesterol
esterase with intestinal cells. Results showed that addition of increasing
concentrations of cholesterol esterase in the incubation medium increased
the uptake of micellar cholesteryl oleate by Caco-2 cells. The cholesterol
esterase also increased the cellular uptake of the nonhydrolyzable
cholesteryl linoleoyl ether. However, maximum uptake of the cholesteryl
ether analog was 50% of that for cholesteryl oleate. The initial
interaction of cholesterol esterase with Caco-2 cells was mediated by
binding of the protein to a low affinity and high capacity binding site on
the cell surface. Cholesterol esterase bound to the cell surface could be
internalized via a monensin-sensitive mechanism. The cholesterol esterase
taken up by the cells had a short residence time and was either degraded or
was rapidly re-secreted from the cells. Chloroquine had no effect on the
degradation or re-secretion of cholesterol esterase by Caco-2 cells,
indicating that lysosomes were not involved with these processes. The
cholesterol esterase taken up by the cells was not available to mediate
further cholesterol uptake. These results indicated that the bile salt-
stimulated cholesterol esterase secreted from pancreas could facilitate
intestinal lipid absorption only transiently. The data suggest that the
regulation of cholesterol esterase synthesis and secretion by the pancreas
may be important for regulation of cholesterol absorption.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
N. Bruneau, S. Richard, F. Silvy, A. Verine, and D. Lombardo
Lectin-like Ox-LDL Receptor Is Expressed in Human INT-407 Intestinal Cells: Involvement in the Transcytosis of Pancreatic Bile Salt-dependent Lipase
Mol. Biol. Cell,
July 1, 2003;
14(7):
2861 - 2875.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. Y. Hui and P. N. Howles
Carboxyl ester lipase: structure-function relationship and physiological role in lipoprotein metabolism and atherosclerosis
J. Lipid Res.,
December 1, 2002;
43(12):
2017 - 2030.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
R. J. Kirby, S. Zheng, P. Tso, P. N. Howles, and D. Y. Hui
Bile Salt-stimulated Carboxyl Ester Lipase Influences Lipoprotein Assembly and Secretion in Intestine. A PROCESS MEDIATED VIA CERAMIDE HYDROLYSIS
J. Biol. Chem.,
February 1, 2002;
277(6):
4104 - 4109.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
N. Bruneau, D. Lombardo, and M. Bendayan
The Affinity Binding Sites of Pancreatic Bile Salt-Dependent Lipase in Pancreatic and Intestinal Tissues
J. Histochem. Cytochem.,
February 1, 2000;
48(2):
267 - 276.
[Abstract]
[Full Text]
|
 |
|

|
 |

|
 |
 
N Bruneau, D Lombardo, and M Bendayan
Participation of GRP94-related protein in secretion of pancreatic bile salt-dependent lipase and in its internalization by the intestinal epithelium
J. Cell Sci.,
January 9, 1998;
111(17):
2665 - 2679.
[Abstract]
[PDF]
|
 |
|

|
 |

|
 |
 
K. Mackay, J. R. Starr, R. M. Lawn, and J. L. Ellsworth
Phosphatidylcholine Hydrolysis Is Required for Pancreatic Cholesterol Esterase- and Phospholipase A2-facilitated Cholesterol Uptake into Intestinal Caco-2 Cells
J. Biol. Chem.,
May 16, 1997;
272(20):
13380 - 13389.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
P. N. Howles, C. P. Carter, and D. Y. Hui
Dietary Free and Esterified Cholesterol Absorption in Cholesterol Esterase (Bile Salt-stimulated Lipase) Gene-targeted Mice
J. Biol. Chem.,
March 22, 1996;
271(12):
7196 - 7202.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 1990 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|