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J. Biol. Chem., Vol. 277, Issue 9, 7170-7177, March 1, 2002
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From the In vitro, pancreatic triglyceride
lipase requires colipase to restore activity in the presence of
inhibitors, like bile acids. Presumably, colipase performs the same
function in vivo, but little data supports that notion.
Other studies suggest that colipase or its proform, procolipase, may
have additional functions in appetite regulation or in fat digestion
during the newborn period when pancreatic triglyceride lipase is not
expressed. To identify the physiological role of procolipase, we
created a mouse model of procolipase deficiency. The
Clps
Decreased Postnatal Survival and Altered Body Weight Regulation
in Procolipase-deficient Mice*
,§,,, and
Departments of Pediatrics and Molecular
Biology and Pharmacology, Washington University School of Medicine and
St. Louis Children's Hospital, St. Louis, Missouri 63110 and the
¶ Department of Cell and Molecular Biology, Lund University,
Biomedical Center, B11, S-221 84 Lund, Sweden
/ mice appeared normal at birth, but
unexpectedly 60% died within the first 2 weeks of life. The survivors
had fat malabsorption as newborns and as adults, but only when fed a
high fat diet. On a low fat diet, the Clps/
mice did not have steatorrhea. The Clps/
pups had impaired weight gain and weighed 30% less than
Clps+/+ or Clps+/
littermates. After weaning, the Clps/ mice
had normal rate of weight gain, but they maintained a reduced body
weight compared with normal littermates even on a low fat diet. Despite
the reduced body weight, the Clps/ mice had
a normal body temperature. To maintain their weight gain in the
presence of steatorrhea, the Clps/ mice had
hyperphagia on a high fat diet. Clps/ mice
had normal intake on a low fat diet. We conclude that, in addition to
its critical role in fat digestion, procolipase has essential functions
in postnatal development and in regulating body weight set point.
*
This work was supported by National Institutes of Health
Grants DK53100, DK52574, and DK56341.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: Washington
University School of Medicine, 660 South Euclid Ave., Campus Box 8208, St. Louis, MO 63110. Tel.: 314-286-2857; Fax: 314-286-2894; E-mail: Lowe@kids.wustl.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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