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1 Department of Pharmacology and Physiology, New Jersey School of Medicine and Dentistry, Newark 07103; 2 Department of Animal Science, Cook College, Rutgers University, New Brunswick 08903; 3 Pathology and Laboratory Medicine Service, Veterans Affairs Medical Center and New Jersey School of Dentistry and Medicine, Newark, New Jersey 07103; and 4 United States Department of Agriculture/Agricultural Research Service Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine and Texas Children's Hospital, Houston, Texas 77030
The in vivo effects of
protein malnutrition and protein rehabilitation on lactase phlorizin
hydrolase (LPH) synthesis were examined. Five-day-old pigs were
fed isocaloric diets containing 10% (deficient, n = 12) or 24% (sufficient, n = 12) protein. After 4 wk,
one-half of the animals in each dietary group were infused intravenously with [13C1]leucine for 6 h, and the jejunum was analyzed for enzyme activity, mRNA abundance,
and LPH polypeptide isotopic enrichment. The remaining animals were fed
the protein-sufficient diet for 1 wk, and the jejunum was analyzed.
Jejunal mass and lactase enzyme activity per jejunum were significantly
lower in protein-deficient vs. control animals but returned to normal
with rehabilitation. Protein malnutrition did not affect LPH mRNA
abundance relative to elongation factor-1
, but
rehabilitation resulted in a significant increase in LPH mRNA relative
abundance. Protein malnutrition significantly lowered the LPH
fractional synthesis rate (FSR; %/day), whereas the FSR of LPH in
rehabilitated and control animals was similar. These results suggest
that protein malnutrition decreases LPH synthesis by altering
posttranslational events, whereas the jejunum responds to
rehabilitation by increasing LPH mRNA relative abundance, suggesting
pretranslational regulation.
small intestine; messenger ribonucleic acid; fractional and total synthesis rates; gas chromatography-mass spectroscopy
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