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J. Biol. Chem., Vol. 277, Issue 39, 36617-36623, September 27, 2002
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From the Cellular retinol-binding protein II (CRBP II) is
a member of the cellular retinol-binding protein family, which is
expressed primarily in the small intestine. To investigate the
physiological role of CRBP II, the gene encoding CRBP II was
inactivated. The saturable component of intestinal retinol uptake is
impaired in CRBP II
Increased Neonatal Mortality in Mice Lacking Cellular
Retinol-binding Protein II*
,,,
, and**
Department of Medicine, Washington
University, St. Louis School of Medicine, St. Louis, Missouri
63110, Specialty Care, St. Louis Veterans Affairs to
Administration Medical Center, St. Louis, Missouri 63106, ** Department of Biochemistry and Molecular Biophysics,
Washington University-St. Louis School of Medicine, St. Louis, Missouri
63110, § Department of Pathology, University of Cincinnati
Medical Center, Cincinnati, Ohio 45267, and the ¶ Department of
Medicine, Columbia University, College of Physicians and Surgeons,
New York, New York 10032
/ mice. The knockout
mice, while maintained on a vitamin A-enriched diet, have reduced
(40%) hepatic vitamin A stores but grow and reproduce normally.
However, reducing maternal dietary vitamin A to marginal levels during
the latter half of gestation results in 100% mortality/litter within
24 h after birth in the CRBP II/ line
but no mortality in the wild type line. The neonatal mortality in
heterozygote offspring of CRBP II/ dams
(79 ± 21% deaths/litter) was increased as compared with the
neonatal mortality in heterozygote offspring of wild type dams (29 ± 25% deaths per litter, p < 0.05). Maternal CRBP
II was localized by immunostaining in the placenta at 18 days
postcoitum as well as in the small intestine. These studies suggest
that both fetal as well as maternal CRBP II are required to ensure adequate delivery of vitamin A to the developing fetus when dietary vitamin A is limiting.
*
This work was supported by National Institutes of Health
Grant DK40172 (to E. L.), Grant DK50446 (to M. S. L.), Grant DK52444 (to W. S. B.), the Washington University Digestive Diseases
Research Core Center (Grant DK 52574) and Clinical Nutrition Research
Unit (Grant DK 56341).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: Div. of
Gastroenterology, Washington University School of Medicine, Campus Box 8124, 660 South Euclid Ave, St. Louis, MO 63110. Tel.: 314-362-1072; Fax: 314-362-8959; E-mail address: eli@im.wustl.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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