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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The influence of starvation has been studied on tissue and serum G-6Pase F-D-Pase and alkaline phosphatase activities and on the muscle and liver glycogen content of the freshwater catfish H. fossilis (Bloch). A marked increase in G-6Pase and F-D-Pase activities and a fall in the muscle and liver glycogen content recorded during 40 day starvation. The rise in gluconeogenic enzymes during starvation may be due to glucocorticoid stimulation. Alkaline phosphatase activity was found to decline markedly during starvation. The decline in enzyme activity is attributed to some factors like a fall in the rate of synthesis caused by lowered metabolic demands and to electrolyte imbalance caused by tissue overhydration. The fall in glycogen content may be related to the starved condition of the fish. Elevation in glycogen content and alkaline phosphatase activity and a fall in gluconeogenic enzymes were noted when feeding had been resumed.
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PMID:Effect of starvation on tissue and serum gluconeogenic enzymes, alkaline phosphatase and tissue glycogen in the freshwater catfish, Heteropneustes fossilis (Bloch). 23 11

Glucose dehydrogenase and alkaline phosphatase activities have been studied for various conditions of sporulation of Bacillus megaterium KM (carbon, nitrogen, phosphate starvation). Glucose dehydrogenase appears in all conditions of sporulation, even with excess of glucose or gluconate. Alkaline phosphatase, usually dereprimed in phosphate starvation, does not increase during sporulation of Bacillus megaterium when phosphate is present.
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PMID:[Variations in enzyme activities in different sporulation conditions of Bacillus megaterium]. 81 46

Alkaline phosphatase (APase) expression can be induced in Bacillus subtilis by phosphate starvation or by sporulation. We have recently shown that there are multiple APase structural genes contributing to the total alkaline phosphatase expression in B. subtilis. The expression of the alkaline phosphatase III gene (phoAIII) was analysed under both phosphate-starvation induction and sporulation induction conditions. phoAII is transcribed from two promoter regions, PV and PS. The PV promoter initiated transcription 37 bp before the translation initiation codon and was used to transcribe phoAIII during phosphate-starvation induction in vegetative cells. The PS promoter initiated transcription 119 bp before the translation initiation codon and was used during sporulation induction. Genes which have previously been shown to affect total vegatative APase, pho regulon genes phoP, phoR and phoS, affected expression of phoAIII during phosphate starvation. Genes known to affect expression of total sporulation APase, i.e. spoIIA, spoIIG and spoIIE, affected phoAIII expression during sporulation induction. Our data show that one member of the APase multigene family, phoAIII, contributes to the total APase expression both during phosphate-starvation induction and sporulation induction, and that the mechanism of regulation includes two promoters, each requiring different regulatory genes.
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PMID:Separate promoters direct expression of phoAIII, a member of the Bacillus subtilis alkaline phosphatase multigene family, during phosphate starvation and sporulation. 176 85

Alkaline phosphatase (ALP, EC 3.1.3.1), acid phosphatase (ACP, EC 3.1.3.2), aspartate aminotransferase (ASAT, EC 2.6.1.1) and alanine aminotransferase (ALAT, EC 2.6.1.2) were measured in the mucosal homogenates of the duodenum, jejunum and caecum of full-fed (control), starved and refed White Rock Cockerels. Starvation caused a significant (p less than or equal to 0.05) increase in the activity of ACP in all three segments of the intestine. Subsequent re-feeding brought the activity back to the control level. In contrast ALP activity fell in the duodenum during starvation and was partially restored by refeeding. In the jejunum and caecum the ALP activity decreased during starvation and was fully restored by re-feeding only in the caecum. ASAT activity increased (p less than or equal to 0.05) during the entire period of starvation in all three segments. Re-feeding failed to decrease the enzyme activity within 48 hours. Starvation caused a reduction (p less than or equal to 0.05) in the activity of ALAT and re-feeding did not increase the activity in the duodenum and jejunum. The caecum showed no change in the activity during fasting.
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PMID:The activities of phosphatases and aminotransferases in the epithelium of the small intestine and caecum of white rock cockerels during starvation. 255 Nov 9

Cell envelope composition and selected physiological traits of Vibrio parahaemolyticus were studied in regard to the Kanagawa phenomenon and growth conditions. Cell envelopes were prepared from cells cultured in Proteose Peptone-beef extract (Difco Laboratories, Detroit, Mich.) medium or filtered estuarine water. Protein, phospholipid, and lipopolysaccharide contents varied with culture conditions. The phospholipids present in the cell envelopes were identified as phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin. Phosphatidylethanolamine decreased and phosphatidylglycerol increased in cells grown in estuarine water. Profiles of proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated numerous protein species, with four to six predominant proteins ranging from 26,000 to 120,000 in molecular weight. The profile of V. parahaemolyticus cell envelope proteins was unique and might be useful in the identification of the organism. Alkaline phosphatase activity was slightly higher in Kanagawa-negative strains and was higher in cells grown in estuarine water than in cells grown in rich laboratory medium. The DNA levels in estuarine water-grown cells increased, while RNA levels and cell volume decreased. Bacteriophage sensitivity typing demonstrated a close intraspecies relationship. Results indicated that Kanagawa-positive and -negative strains were closely related, but they could be grouped separately and may have undergone starvation-related physiological changes when cultured in estuarine water.
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PMID:Comparison of Vibrio parahaemolyticus grown in estuarine water and rich medium. 278 69

The effect of starvation and sampling time on plasma alkaline phosphatase activity, total plasma calcium concentration and whole blood ionized calcium concentration was determined in the rat. Starvation caused a significant fall in total and ionized calcium concentrations as well as in alkaline phosphatase activity. These changes were accompanied by a fall in whole blood pH and an increase in the anion gap and a decrease in urinary excretion of calcium. These indices were restored to normal following refeeding. There was no change in serum 25-OH vitamin D concentrations following starvation for 3 days. Alkaline phosphatase activity showed a pattern compatible with the presence of a circadian rhythm when sampling took place between 0800 and 1800 h. Total and ionized calcium concentrations did not show such a rhythm when animals were fed the present diet.
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PMID:Effect of starvation and sampling time on plasma alkaline phosphatase activity and calcium homeostasis in the rat. 278 12

We previously have shown that aging alters the expression of several intestinal enzymes during cell migration from the crypt base to the villus tip. The activities of many mucosal enzymes are dramatically altered by starvation and refeeding. We compared the effects of starvation and refeeding on the activities of selected intestinal enzymes in young and aging Fischer 344 rats. Gut mass fell during starvation and rose during refeeding to a similar extent in both groups. Sucrase and maltase specific activities in control aging rats were lower than in young controls and, during starvation, enzyme activities declined at approximately similar rates in both groups. Total duodenal enzyme activities fell by about two-thirds in young animals and by greater than 80% in aged animals. Alkaline phosphatase and adenosine deaminase activities also were lower in aging than young animals. During refeeding, enzyme activities rose more in aging rats than in the young. In fact, the specific activities of sucrase and maltase in aging rats refed for 1 day exceeded the values found in fed aging controls. The adaptive responses of duodenal enzymes exceeded those in the jejunum. In conclusion, the aging intestine responds appropriately to starvation and refeeding. However, the fluctuations in brush-border enzyme activities are much greater in aging than in young rats. Such alterations may be an important influence of aging on gut differentiation and might have an adverse impact upon nutritional maintenance in aging animals.
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PMID:Adaptive changes of intestinal enzymes to nutritional intake in the aging rat. 359 66

Seventy-two hour starvation in neonatal rabbits was studied. Fasted animals received no feeds, only water every 8 h for 72 h. Fed animals were suckled by the dam. There was no difference in birth weight, serum albumin, blood urea nitrogen, electrolytes, or urine specific gravity between fed and fasted animals. Weight at 72 hr was less in fasted (p less than 0.01) than fed rabbits. Serum cortisol (p less than 0.05) and corticosterone (p less than 0.01) levels were higher in the fasted group. Proximal and distal small bowel homogenates had less DNA and protein (p less than 0.01) in the fasted group, but the protein/DNA ratio was the same in the proximal and distal small bowel homogenates from both groups. Sucrase (E.C.3.2.1.26) specific activity was significantly increased in proximal small bowel homogenates from the fasted group (p less than 0.01) but was the same in distal small bowel homogenates from both groups. Sucrase total activity per proximal segment was the same in fed and fasted animals but was significantly less per segment in distal small bowel homogenates from fasted animals. Alkaline phosphatase (E.C.3.1.3) total and specific activity was decreased in proximal (p less than 0.01) and distal (p less than 0.05) small bowel homogenates from the fasted group. Lactase (E.C.3.2.1.23) total activity was decreased in proximal and distal (p less than 0.01) small bowel homogenates from the fasted group but lactase specific activity was unchanged. Thus, a brief period of malnutrition in neonatal animals can result in a variety of regional functional changes in the gastrointestinal mucosa.
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PMID:Short-term malnutrition in neonatal rabbits. I. Brush border enzymes. 368 82

Alkaline phosphatase is induced in excess phosphate media by starvation either for pyrimidines or for guanine. Induction is observed both during starvation, after a lag period, and following a period of starvation. Induction is not caused by a lowering of the internal orthophosphate pool, but is linked to alterations in the levels of the nucleotide pools. Experiments with purine-requiring mutants suggest that phosphatase is induced in wild-type strains by an adenine nucleotide. Mutations in the phoR gene can produce differential responses to the different starvation regimes.
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PMID:Physiological factors in the regulation of alkaline phosphatase synthesis in Escherichia coli. 455 39

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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PMID:Precocious and reversible expression of sucrase-isomaltase unrelated to intestinal cell turnover. 817 95


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