On the primary site of control in the spontaneous development of small‐intestinal sucrase‐isomaltase after birth

Sebastio, Gianfranco; Hunziker, Walter; Ballabio, Andrea; Auricchio, Salvatore; Semenza, Giorgio

doi:10.1016/0014-5793(86)81069-9

Cited by 30 publications

(7 citation statements)

References 30 publications

(11 reference statements)

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“…4B), although less well than laetase with its mRNA. This is germane to what we have reported on the site of control of sucrase-isomaltase biosynthesis in rive in fetal life (in man [37]) or during weaning (in rabbits [38]). As pointed out in a previous section, we unexpectedly find in addition a post-translational mechanism that reduces sucrase activity in the proximal third of the small intestine (Fig.…”

Section: Resultsmentioning

confidence: 50%

The levels of lactase and of sucrase‐isomaltase along the rabbit small intestine are regulated both at the mRNA level and post‐translationally

et al. 1992

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We determined along the small intestine of young and adult rabbits the activities of lactase (LPH) and sucrase (Sl), the levels of their cognate mRNA~, and examined the in vitro biosynthesis of LPH and pro.Sl. Lactate activity is low in the proximal 1/3 of the intestine, whereas the mRNA levels are high. However, the rates of biosynthesis of the LPH forma correlated well with the steady-state levels of LPH mRNA in all see~nents, indicating that factor(s) acting post-translationally produce a decline in brush border LPH in the proximal small intestine. These factor(s) are not involved in the processing of pro-LPH to mat ure LPH, since the relative amounts ol'the various l'onns of LPH are almost the same :dong the small intestine. Unexpectedly, we find that also for SI the ratio of activity to mRNA is low in proximal intestine. The biosynthesis ol'pro-Sl ~rrclates with the steady-state levels of its mRNA. Hence, the steady-state levels o1" LPI-I and Sl along the small intestine arc regulated both by mRNA level5 attd by posttranslational factor(s).

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Section: Resultsmentioning

confidence: 50%

The levels of lactase and of sucrase‐isomaltase along the rabbit small intestine are regulated both at the mRNA level and post‐translationally

et al. 1992

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“…Many different patterns, however, are found. (1) A steady increase after weaning at 14-17 days of life was found with sucrase-isomaltase [4] and IF [5]. (2) A rapid increase at birth, followed by no change until adulthood was seen with the FABPs [6], Although the mRNA levels of the liver FABP rise rapidly at day 1 and are steady for 30 or more days, the tissue levels rise steadily up to 20 days of life [7], Thus, control of liver FABP production, for exam ple, is exercised at the translational level, as well as pre-translationally.…”

Section: Pre-translational Mechanismsmentioning

confidence: 99%

Pre-Translational, Translational, and Post-Translational Mechanisms in Adaptation of Intestinal Proteins

Alpers

1990

Digestion

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The enterocyte exhibits remarkable short-term adaptation to a meal, complementing the well recognized adaptation of the stomach and pancreas. The mechanisms utilized include increased protein synthesis by pre-translational and translational events, and post-translational alterations in protein degradation and secretion. All of these events occur within a few hours after the meal. These adaptations are compared with the more long-term events in post-natal development that occur over a period of days, at least in the rat. They contrast even more with the macroscopic changes that also occur over days and weeks following intestinal resection, the model most commonly associated with the concept of intestinal adaptation. The demonstration of cellular and molecular adaptation within a few hours of a meal represents an expansion of the definition of intestinal adaptation and may provide clues to the explanation of more delayed events.

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“…Recent studies centred on SI and lactase expression during pre-and post-natal development, during crypt-to-villus cell differentiation in adult animals and in Caco-2 and cells have provided evidence for both transcriptional and posttranslational control sites. In the case of SI, its mRNA and enzyme activity were first detectable, and subsequently increased in parallel during spontaneous or precociously-induced appearance, in newborn rabbits [18] and rats [19] and in human embryos [20], providing evidence for a transcriptional level of regulation. However, Leeper & Henning [19] have suggested that in rats older than 24 days other mechanisms may also be important.…”

Section: Introductionmentioning

confidence: 99%

Clonal analysis of sucrase-isomaltase expression in the human colon adenocarcinoma Caco-2 cells

Beaulieu

Quaroni

1991

Biochemical Journal

145

146

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To investigate the biosynthetic basis for the mosaic expression of brush border enzymes in confluent Caco-2 cells, a human colon carcinoma cell line exhibiting characteristics of adult small intestinal enterocytes, we have obtained a series of clones differing markedly in their growth rates, amounts of transforming growth factor-a/epidermal growth factor-like activity released into the culture medium, and sucrase-isomaltase (SI) activity. Other intestinal markers (aminopeptidase N, dipeptidylpeptidase IV, lactase, alkaline phosphatase and 'crypt cell antigen') displayed a much more limited variability in expression, suggesting that the Caco-2 cell clones we have obtained did not differ in their overall ability to differentiate.Immunofluorescence staining, metabolic labelling with radioactive methionine and hybridization analysis of SI mRNA abundance were used to investigate SI synthesis and its regulation in clones endowed with low, intermediate or high sucrase activity. The results obtained have demonstrated heterogeneous SI expression, even in clonal cell lines, and a negative correlation between SI expression and growth factor concentrations in the culture medium, suggesting an autocrine regulation of cell proliferation and differentiation in confluent Caco-2 cells. Pulse-chase experiments using the two clones endowed with the lowest and highest levels of SI activity, followed by immunoprecipitation of labelled SI with epitope-specific antibodies and SDS/PAGE analysis, suggested that both transcriptional and post-translational mechanisms play a role in the regulation of SI expression in intestinal cells.

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On the primary site of control in the spontaneous development of small‐intestinal sucrase‐isomaltase after birth

Cited by 30 publications

References 30 publications

The levels of lactase and of sucrase‐isomaltase along the rabbit small intestine are regulated both at the mRNA level and post‐translationally

The levels of lactase and of sucrase‐isomaltase along the rabbit small intestine are regulated both at the mRNA level and post‐translationally

Pre-Translational, Translational, and Post-Translational Mechanisms in Adaptation of Intestinal Proteins

Clonal analysis of sucrase-isomaltase expression in the human colon adenocarcinoma Caco-2 cells

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