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Am J Physiol Gastrointest Liver Physiol 266: G568-G575, 1994;
0193-1857/94 $5.00
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AJP - Gastrointestinal and Liver Physiology, Vol 266, Issue 4 568-G575, Copyright © 1994 by American Physiological Society

ARTICLES

Precocious and reversible expression of sucrase-isomaltase unrelated to intestinal cell turnover

E. Nsi-Emvo, C. Foltzer-Jourdainne, F. Raul, F. Gosse, I. Duluc, B. Koch and J. N. Freund
Institut National de la Sante et de la Recherche Medicale, Universite Louis Pasteur, Strasbourg, France.

The effect of starvation and refeeding on the developmental pattern of intestinal sucrase-isomaltase (SI) was analyzed in preweaned rats. Starvation at postnatal day 12 caused a precocious expression of SI activity and mRNA. Alkaline phosphatase activity was slightly reduced, and no significant change was observed for aminopeptidase and lactase activities. Immunostaining showed that SI molecules appear in cells at the base of the villus. Sucrase expression was further increased by prolonged food deprivation, whereas enzyme activity as well as the amount of SI mRNA dropped to reach the low level found in control sucklings when 48 h-starved pups were refed by returning them to their dams. During the refeeding period, the enterocytes that were committed to produce SI by starvation continued to express the enzyme while migrating up the villi. However, the new epithelial cells arising from the crypts no longer synthesized the disaccharidase. The starvation-evoked appearance of SI was preceded by a transient burst of expression of the protooncogene c-fos, an event that may be correlated to the ontogenic rise of c-fos mRNA observed before weaning. However, in contrast to the normal weaning condition, SI induction by starvation occurred without obvious increase of epithelial cell proliferation and turnover. During the starvation and refeeding period, patterns of sucrase activity and SI mRNA paralleled the serum level of glucocorticoids.(ABSTRACT TRUNCATED AT 250 WORDS)


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