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Biomedical subjects

F Raul

Publications and source records attributed to F Raul.

At least 19 recordsLinked to original sources
PubMed1992

Dietary control of the lactase mRNA distribution along the rat small intestine.

At weaning, the lactase-phlorizin hydrolase (LPH) mRNA was shown to disappear specifically from the distal part of ileum while remaining abundant in the more proximal segments of the small intestine. The purpose of this study was to analyze the longitudinal distribution of this transcript in rats whose intestinal lumen content was modified before and after weaning. Preweaned animals force-fed with an artificial diet retained a high amount of LPH mRNA in the jejunum, whereas this transcript precociously decreased in the distal ileum. Conversely, prolonged nursing delayed the specific decay of the LPH mRNA in the latter segment. Food deprivation in preweaned animals did not alter the longitudinal distribution of this transcript in that it remained abundant in the distal ileum. In adult rats, rearranging the order of the small intestinal segments with regard to the intraluminal flow of nutrients did not modify the typical distribution of the LPH mRNA. These results suggest that switching over from milk to the adult-type diet at weaning contributes to the modification of the longitudinal distribution of the LPH mRNA that normally occurs at this stage. However, once the adult pattern of expression of this transcript is established, it cannot be significantly altered by changing the position of each intestinal segment as well as its luminal content.

Aging↗
PubMed1991

Adaptation of intestinal hydrolases to starvation in rats: effect of thyroid function.

The effects of long-term starvation on the activities of sucrase, lactase, and aminopeptidase, and on their respective mRNA were determined in the small intestine of thyroidectomized and sham-operated adult rats. Thyroidectomy reduced the protein loss at the level of the intestinal brush border membranes during starvation. Prolonged fasting caused a significant decrease in sucrase activity, but thyroidectomy partly prevented this effect. However, the amount of the corresponding mRNA dropped during long term starvation without incidence of thyroidectomy. Lactase activity in the brush border membranes was increased by starvation, and thyroidectomy caused a further elevation of the enzyme activity. Simultaneously, lactase mRNA content rose only slightly compared to the enzyme activity. Aminopeptidase activity and mRNA content decreased during starvation and thyroidectomy did not prevent this process. These results indicate that intestinal hydrolases respond non-coordinately to long-term food deprivation. In addition, the thyroid status of the animals has a direct influence on the adaptation of several brush border hydrolases to starvation. This suggests that the drop in plasma thyroid hormones during fasting allows a better maintenance of protein content and of hydrolase activities in the brush border membranes of the small intestine. These adaptive processes seemed to be partly controlled at a post-transcriptional level.

Adaptation, Physiological↗
PubMed1991

Lactase expression is controlled differently in the jejunum and ileum during development in rats.

This study shows the distribution of the messenger RNA for lactase-phlorizin hydrolase during postnatal development and along the longitudinal axis of the rat small intestine. At birth, this messenger RNA was present along the whole length of small intestine, and its concentration remained elevated during the suckling period despite the concomitant decrease in enzyme activity. At weaning, the amount of lactase messenger RNA dropped specifically in the distal ileum. This decrease in lactase messenger RNA was initiated at the ileocecal junction, progressed gradually towards the jejunum, and followed the decrease in lactase activity several days later. Starvation and refeeding were also found to cause modifications of lactase activity and messenger RNA expression that were prominent in the distal part of small intestine. These data support that posttranscriptional and pretranslational levels of regulation are required to define the spatial and temporal expression of lactase in the rat small intestine.

Animals↗
PubMed1991

Ileal compensation for age-dependent loss of jejunal function in rats.

Adaptive responses of brush border hydrolases and crypt cell proliferation were measured in the jejunum and ileum of 4-mo-old adult and 28-mo-old senescent male Wistar rats. Responses were measured after rats were deprived of food and then refed with a normoprotein diet (17% protein) or an isoenergetic high protein diet (70% protein). The young rats deprived of food then refed for 18 h with the high protein diet showed better body weight recovery than did old animals. Withholding food for 48 h induced a more pronounced drop of sucrase activity in the intestine of the old rats relative to young rats. Refeeding the high protein diet caused a better recovery of sucrase activity in the jejunum of young rats relative to senescent rats. In the aged animals, sucrase activity in the jejunum remained significantly lower after refeeding both diets. Compared with nourished controls, aged rats showed enzyme activity to be completely restored in the ileum. The high protein diet increased aminopeptidase activity in the jejunum and ileum of young rats, in contrast to the senescent rats in which the increase of enzyme activity was restricted to the ileum. In the jejunum of aged rats, the cell migration rate from crypt base to villus tip was reduced after refeeding, but no age-related changes were observed in the ileum. Our results indicate that the jejunum of senescent rats exhibits reduced adaptive capacities that may be partly compensated by enhanced ileal functions.

Adaptation, Physiological↗
PubMed1991

Derivatives of plant beta-glucans are hydrolyzed by intestinal lactase-phlorizin hydrolase of mammals.

Laminaribiose and gentiobiose, two O-beta-linked disaccharides deriving from plant beta-glucans, were found to be hydrolyzed in the rat small intestine by an enzyme anchored into the brush border membrane of the enterocytes. Immunological and biochemical data, together with the developmental pattern of expression, support that this activity is carried out by the bifunctional enzyme involved in the hydrolysis of lactose and glycosylceramides: the lactase-phlorizin hydrolase complex.

Animals↗
PubMed1991

Rat lactase activity and mRNA expression in relation to the thyroid and corticoid status.

The effect of glucocorticoids and thyroid hormones on lactase expression was investigated along the small intestine of rats. In sucklings thyroxine injections promoted a precocious drop of enzyme activity but not of mRNA. Hydrocortisone did neither modify lactase activity nor its mRNA expression. In adults decreasing the amount of thyroid hormones led to a slight and reversible increase of the lactase mRNA content whereas lactase activity rised more dramatically. Thus, thyroid hormones in contrast to corticoids, are involved in the posttranscriptional control of lactase during the suckling period. Yet, none of these hormones might induced the modification of the longitudinal distribution of the lactase mRNA that occurred at weaning.

Animals↗
PubMed1990

Specific expression of lactase in the jejunum and colon during postnatal development and hormone treatments in the rat.

The expression of lactase was compared in the jejunum and colon of the rat at the levels of enzyme activity and protein and RNA content. We found that the enzyme proteins and the corresponding mRNAs share common features and are encoded by a single gene in both intestinal segments. In the jejunum, large amounts of lactase mRNA and proteins were detected during postnatal development as well as in adult rats, despite the 10-fold decline in lactase specific activity which occurs at weaning. In contrast, in the colon the expression of lactase was restricted to early postnatal development. In the colon, the enzymic activity of lactase and the amounts of protein and mRNA followed parallel development profiles with a peak at day 4 after birth. Injections of thryoxine or epidermal growth factor into neonates led to small modifications in the expression of lactase in the jejunum. On the other hand, these treatments caused a large decline in lactase activity in the colon that paralleled a decrease in the amount of lactase protein and mRNA. These data indicate that the expression of lactase is mainly regulated at the post-transcriptional level in the jejunum, whereas it is controlled at the pretranslational level in the colon.

Animals↗
PubMed1990

Effect of epidermal growth factor on the expression of digestive hydrolases in the jejunum and colon of newborn rats.

The regulatory effect of epidermal growth factor (EGF) on the developmental pattern of brush border hydrolases was studied in the proximal jejunum and colon of the newborn rat. In the proximal colon, daily administration of EGF for 1, 3, or 5 days postpartum inhibited the postnatal increase in lactase, maltase, and aminopeptidase specific activities. In contrast, in the jejunum EGF did not influence lactase activity, inconsistently increased maltase activity, and partly prevented the early postnatal decrease in aminopeptidase activity. In the proximal colon, EGF showed additive effects with T4 and hydrocortisone on the inhibition of lactase activity. In the jejunum, EGF potentiated the effect of hydrocortisone and T4 on the expression of sucrase activity and had only a slight effect when injected alone. The incorporation rate of [3H]thymidine in the proximal colon and jejunum was not different in control and treated rats, indicating the absence of an effect of EGF on DNA synthesis. These results show that EGF may play an important physiological role in the enzymatic differentiation of the developing intestine during early postnatal development. Alone or acting with T4 or glucocorticoids, EGF may induce the decline of digestive hydrolases in the proximal colon. In the small intestine EGF may play a major role in the triggering of sucrase expression.

Aminopeptidases↗
PubMed1990

[Different expression of the mRNA detected by the cDNA for fetal rat lactase in the jejunum and colon].

To study the genetical expression of lactase-phlorizin hydrolase in the jejunum and colon of developing rats we cloned the corresponding cDNA in a cDNA library constructed from the intestinal RNA of fetal rats. The structure of this 6.1 kb-long cDNA was similar to that of the cDNA of adult rabbits and humans, indicating that the enzyme was synthesized as a precursor organized into repeated homologous domains. The mRNA for lactase-phlorizin hydrolase accumulated at a constant level throughout the development in the jejunum despite the decline in lactase activity occurring at weaning. In the colon, the cDNA for lactase-phlorizin hydrolase hybridized to a transcript that was similar in size to the jejunal mRNA. This mRNA was transiently found during the first week after birth. Its rate of accumulation defined the level of lactase activity measured at this stage. We conclude that the expression of lactase-phlorizin hydrolase during the development is essentially regulated at the post-transcriptional level in the jejunum, in contrast to the colon where it is regulated at the pretranslational level.

Animals↗
PubMed1990

Comparative expression of the mRNA for three intestinal hydrolases during postnatal development in the rat.

The distribution of the mRNA for intestinal aminopeptidase-N, lactase-phlorizin hydrolase and sucrase-isomaltase was compared during rat postnatal development as well as along the longitudinal axis of the intestinal tract including small-intestine and colon. We found out that each mRNA exhibited a specific pattern of accumulation, suggesting proper regulation steps for the expression of the corresponding digestive enzymes.

Aminopeptidases↗
PubMed1989

Discrepancy between the intestinal lactase enzymatic activity and mRNA accumulation in sucklings and adults. Effect of starvation and thyroxine treatment.

The accumulation profile of intestinal lactase mRNA was investigated in suckling and adult rats and pigs. We found no correlation between the lactase enzymatic activity and the accumulation of the messenger at both developmental stages. Modulation of lactase activity by starvation or thyroxine treatment had no effect on lactase mRNA accumulation in the rat intestine. These results confirm that thyroxine modulates lactase expression essentially at the post-transcriptional level.

Age Factors↗
PubMed1989

Age influence on sucrose hydrolysis and on monosaccharide absorption along the small intestine of rat.

The consequences of aging on the hydrolysis and absorption of hexoses was assessed in vitro using everted intestinal segments. Glucose and fructose were given either as a mixture of free monosaccharides or as a disaccharide solution (sucrose). The jejuno-ileum of 3- and 24-month-old rats was everted and divided into four equal segments. For each segment, the mucosal medium contained either sucrose (140 mM) or an equimolar mixture of glucose and fructose (70 mM). Monosaccharide concentrations in the mucosal ans serosal media were measured after 1 h of incubation at 37 degrees C. In the young adult, glucose absorption was enhanced when given as sucrose. In contrast, in the aged rat, free glucose or glucose released from sucrose hydrolysis were similarly absorbed. Independently of age, fructose was better absorbed when provided in a mixture of free monosaccharides. The intestinal segments (and especially the ileum), of the aged animals exhibited higher abilities to hydrolyse sucrose and to absorb monosaccharides indicating a normal or increased intestinal hydrolytic activity and absorptive capacity for dietary sugars.

Aging↗
PubMed1989

Perinatal expression of brush-border hydrolases in rat colon: hormonal and tissue regulations.

The evolution pattern of brush-border digestive hydrolases and their hormonal regulation were studied in the proximal colon of newborn rats. The potentiality of the colon to express a small intestinal enzymatic pattern was also examined in associations made up of colonic endoderm and small intestinal mesenchyme, developed as either intracelomic grafts in 3-day-old chick embryos or as intrarenal grafts in adult rats. A transient increase of lactase- and aminopeptidase-specific activities occurred in the colon from the 19th day of gestation to 14 days after birth, but sucrase activity could never be detected. Immunocytochemical studies with antibodies specific for rat lactase, aminopeptidase, and sucrase confirmed these results. However, the levels of hydrolase activities were lower in the colon than in the jejunum at the same age. Thyroxine or hydrocortisone treatment during the first 4 days postpartum decreased lactase activity by 70 and 30%, respectively, but did not affect aminopeptidase activity. A slight but significant induction of sucrase activity was obtained with both hormones. In contrast, in the jejunum, only thyroxine decreased lactase activity with a lesser effect (30%), but both hormones increased aminopeptidase activity and induced the marked well-known appearance of sucrase activity. The fetal small intestinal mesenchyme was not able to induce the colonic endoderm to achieve a small intestinal-like differentiation. But the exposure of the developed hybrid intestines to glucocorticoids in organ culture allowed expression of sucrase in one-third of the cases. These results demonstrate the presence of brush-border hydrolases in the proximal colon of newborn rats, normally expressed in the small intestine, but never in the adult colon.(ABSTRACT TRUNCATED AT 250 WORDS)

Aging↗
PubMed1989

The gene for intestinal sucrase-isomaltase as member of a gene family.

The synthetic oligonucleotide MF59, derived from the rabbit sucrase-isomaltase cDNA sequence, hybridizes to two classes of mRNA in the rat and pig intestinal epithelium as well as to various restriction fragments within the human genome. These results strongly support the hypothesis that the sucrase-isomaltase gene belongs to a gene family. The cloning of a human cosmid containing such a sequence similar to MF59 has allowed us to identify a new member of this gene family which detects a single 6.5 Kb intestinal mRNA in the adult pig.

Amino Acid Sequence↗
PubMed1988

Adaptation of intestinal enzymes to seasonal and dietary changes in a hibernator: the European hamster (Cricetus cricetus).

Effects of diet, hibernation and seasonal variations on hydrolase activities were determined in mucosa and purified brush border membranes of the small intestine of European hamsters. Wild hamsters captured in April and fed for several weeks with an equilibrated laboratory chow (20% protein, 50% carbohydrates) exhibited a rise in disaccharidase activities (sucrase, isomaltase, lactase) but no changes in aminopeptidase N activity. During deep hibernation, in contrast to sucrase and isomaltase activities which showed only minor changes, lactase activity was significantly enhanced along the jejunoileum, and aminopeptidase N activity was maximum in the ileum. After a short period (48 h) of wakefulness and feeding following 10 days of starvation during the hibernation period, the activities of the disaccharidases and of aminopeptidase N returned to values measured in active animals. In contrast to the nutritional state, which has an important impact on the activities of intestinal enzymes, season has little effect on the intestine of the active animal under a controlled environment. The pattern of enzyme activities which occurs along the small intestine in the hibernating animal may be a prerequisite for optimum digestion during the short phases of waking during the hibernation period of the European hamster.

Adaptation, Physiological↗
PubMed1988

Age related increase of brush border enzyme activities along the small intestine.

Intestinal morphology and brush border hydrolase activities were determined along the small intestine of young adult (three months, n = 10), mature (12 months, n = 10), and senescent (29 months, n = 15) rats. The intestinal segments of the senescent rats contained higher mucosal mass and protein content (p less than 0.05) compared with the young and mature animals. A significant reduction of villus height and crypt depth (p less than 0.05) was found in the proximal intestine during aging. A 35% increase in villus height (p less than 0.05) without changes in crypt depth, was observed in the distal ileum in senescent rats. The activities of sucrase and isomaltase were significantly increased during aging in the duodenum and jejunum (p less than 0.05). Lactase and aminopeptidase activities which showed only minor changes between young and mature animals were significantly enhanced in senescent animals (p less than 0.05) with aminopeptidase exhibiting a three-fold increase in activity in the proximal ileum. The results when combined with those of previous studies suggest that in the aged animal, the increased level of intestinal hydrolase activities may be the consequence of prolonged cellular maturation along the villi in the proximal intestine, and of adaptation to increased concentrations of intraluminal substrates in the distal intestine.

Aging↗