Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The activity and the molecular characteristics of butyrylcholinesterase were studied in the epithelial cells of the following intestinal segments: duodenum, jejunum, ileum, caecum and colon of starved and refed rats. 2. After starvation, the specific activity of the enzyme is found to increase in the jejunum. The same level of activity was maintained after refeeding. No notable changes were observed in the other intestinal segments after either starvation or refeeding. 3. The behaviour of aminopeptidase, a well-characterized intestinal enzyme, is comparable to that of butyrylcholinesterase, except in the duodenum where the aminopeptidase activity is increased after refeeding. 4. In this cell type, BuChE is found only in its globular forms (G1, G2 and G4). Starvation resulted in a higher value of the sedimentation coefficient of the ileal G2 form, suggesting the existence of a complex between the enzyme and non-cholinesterase components. 5. After refeeding, the sedimentation profile was similar to that of control.
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PMID:Behaviour of butyrylcholinesterase in the intestinal epithelial cells of starved and refed rats. 173 92

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.
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PMID:Adaptation of intestinal hydrolases to starvation in rats: effect of thyroid function. 193 43

To compare the tropic effect of different dietary nutrients on mucosal adaptation in the jejunum and ileum, adult rats were submitted to a 96-h period of starvation and refed isocaloric liquid diets (1.5 kcal ml-1) containing either protein (casein), carbohydrate (starch) or lipids. In the jejunum, 4 days of starvation caused mucosal hypoplasia, villus and crypt shortening and a decrease in the total activity of disaccharidases with the exception of lactase which was markedly enhanced. In contrast, mucosal hypoplasia was incomplete in the ileum which exhibited an increase in crypt depth and in the specific and total activities of disaccharidases and of aminopeptidase. Compared with protein and carbohydrates, lipids exerted the strongest stimulatory effect for mucosal regeneration. In the jejunum as well as in the ileum, mucosal mass parameters, villus length, crypt depth and lactase activity did reverse towards their initial value within 1-3 days of refeeding lipids, even though the animals received only one-third of their normal daily caloric intake. Our results indicate that the pattern of response to fasting differs between the proximal and distal small intestine, and that the intestinal changes induced by starvation are rapidly reversed by refeeding small amounts of a diet rich in fat.
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PMID:Refeeding after starvation in the rat: comparative effects of lipids, proteins and carbohydrates on jejunal and ileal mucosal adaptation. 212 4

The effects of starvation (72 h) and refeeding with three liquid diets, differing only in the molecular form of the nitrogen source (whole whey proteins, WP; tryptic whey protein hydrolysate, WPH; and amino acid mixture, AAM), on the jejunal mucosal morphology and brush border enzyme activities (sucrase, S; maltase, M; and neutral aminopeptidase, NA) of male Wistar rats were studied. All three diets produced repair of the fasting-induced mucosal atrophy; the WP diet gave the most rapid growth with maximum villus height (VH) and protein content after 48 h (p less than 0.01). AAM gave the fastest and greatest stimulation of sucrase and maltase activities (p less than 0.01). There were no significant differences in NA activity. In control rats the WPH and AAM diets produced significantly greater villus height and disaccharidase activities than did the WP diet. Jejunal morphology and disaccharidase activities can be modified by the molecular form of alimentary protein and nutritional status interferes with these modifications.
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PMID:Dietary whey proteins and their peptides or amino acids: effects on the jejunal mucosa of starved rats. 264 93

Vacuoles prepared from yeast cells of Candida albicans were enriched in proteinase ycaB (EC 3.4.21.48) but not in aminopeptidase or beta-glucosidase. Proteinase ycaB, assayed in situ, increased 1.5-fold during starvation whereas aminopeptidase activity decreased by 25%. Proteinase ycaB increased a further 1.5-fold during germ-tube formation.
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PMID:The cellular location of proteases in Candida albicans. 330 84

Strains of Escherichia coli K12 were isolated in which the lac structural genes were fused to the promoter for the aminopeptidasee N structural gene (pepN). Although this enzyme is constitutively produced, the differential rate of synthesis is increased about 4-fold upon phosphate starvation. The pepN-lac fusions were shown to respond to phosphate specific regulatory signals. A plaque forming lambda transducing phage bearing the pepN-lac fusion was isolated. This phage was used to prove genetically the fusion of lac genes to the promoter for the aminopeptidase. These results demonstrate a control at the transcriptional level of aminopeptidase synthesis.
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PMID:Fusion of the lac genes to the promoter for the aminopeptidase N gene of Escherichia coli. 612 64

The specific activity of X-prolyl-dipeptidyl aminopeptidase in Saccharomyces cerevisiae grown on glucose-containing medium remains constant during exponential growth and increases less than twofold when cells reach the stationary phase. In cells harvested from exponential growth on glucose-containing medium the specific activity of the enzyme is found to be 20-30% lower than the specific activity observed in media without glucose, containing acetate or ethanol as the carbon source. X-Prolyl-dipeptidyl aminopeptidase is not inactivated after the addition of glucose to stationary phase cells. Growth of the yeast on poor nitrogen sources or under nitrogen-starvation results in a three- to fourfold increase in the level of the enzyme.
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PMID:Studies on the regulation of X-prolyl dipeptidyl aminopeptidase activity. 614 Dec 15

A mutant strain of Salmonella typhimurium that lacks two proline-specific peptidases (peptidases P and Q) could not complete the degradation of proline peptides formed as intermediates in starvation-induced protein breakdown. The wild-type strain produced free proline as the product of degradation of proline-labeled proteins. The pepP pepQ mutant, however, produced a mixture of small proline peptides. In the absence of peptidase Q only, peptidase P could complete the degradation of most of the proline peptide intermediates formed. In the absence of peptidase P only, about 50% of the proline-labeled, acid-soluble products were proline peptides. These results are consistent with in vitro specificity data indicating that peptidase Q hydrolyzes X-Pro dipeptides only, whereas peptidase P attacks both X-Pro dipeptides and longer peptides with X-Pro at their N-termini. A mutant strain lacking four broad-specificity peptidases (peptidases N, A, B, and D), but containing peptidases P and Q, also produced proline peptides as products of protein breakdown. This observation suggests that broad-specificity peptidases are required to generate the X-Pro substrates of peptidases P and Q. A strain lacking six peptidases (N, A, B, D, P, and Q) was constructed and produced less free proline from protein breakdown than either the pepP pepQ strain or the pepN pepA pepB pepD strain. These observations suggest that the degradation of peptide intermediates involves the sequential removal of N-terminal amino acids and requires both broad-specificity aminopeptidases (peptidases N, A, and B) and the X-Pro-specific aminopeptidase, peptidase P.
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PMID:Degradation of proline peptides in peptidase-deficient strains of Salmonella typhimurium. 633 37

The activities of microvillus aminopeptidase (microsomal, EC 3.4.11.2), dipeptidyl peptidase IV (EC 3.4.14.-), glycyl-leucine dipeptidase (EC 3.4.13.11), proline dipeptidase (EC 3.4.13.9), sucrase (EC 3.2.1.48) and gamma-glutamyl transpeptidase (EC 2.3.2.2) were measured in peroral intestinal biopsies taken from patients with coeliac disease in the acute phase and in remission. A comparison with the amounts of corresponding activities from a reference group showed that all the measured activities were significantly decreased in the acute phase of the disease. In patients in remission only microvillus aminopeptidase and dipeptidyl dipeptidase IV displayed a substantial depression as compared to the reference group. It is suggested that a primary mucosal digestion defect will result in lack of substrate for other intestinal enzymes. This is a situation comparable to starvation and may explain the variation in the grade of restitution for the different enzymes.
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PMID:Intestinal peptidases and sucrase in coeliac disease. 700 82

Aminopeptidase, lactase and sucrase activities have been followed during 5 days in the jejunum and in the ileum of starved adult rats. Enzyme activities have been determined in the mucosal homogenates as well as in the purified brush border membranes and expressed as activities per intestinal length (segmental activities) or as activities per milligram of protein (specific activities). The segmental and specific activity of aminopeptidase was increased in the ileum during the first 2 days of starvation, suggesting that aminopeptidase may have during the first days of starvation a conservative role by preventing an important loss of tissue protein. In all conditions, lactase activity was strikingly enhanced by starvation whereas sucrase activity showed no changes or decreased activity. Lactase stimulation was initiated during the first 24 h of starvation reaching its maximum after 2 days. The various experimental conditions leading to a specific or to a nonspecific stimulation of intestinal lactase activity have been discussed.
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PMID:Modifications of brush border enzyme activities during starvation in the jejunum and ileum of adult rats. 715 74


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