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)

In 24 normal and 24 obese subjects of both sexes circulating substrates (blood sugar, free fatty acids, ketone bodies) and hormones (insulin, growth hormone, pancreatic glucagon) were determined during 6 days of total fast. In normals the blood sugar fell to lower levels than in the obese. Plasma free fatty acids and ketone concentrations rose faster in normal than in obese subjects, and faster in females than in males. Plasma insulin concentrations declined to a greater extent in obese than in normal subjects. In all groups studied a significant increase of the pancreatic glucagon level within 1-3 days of fasting was observed, however, its rise occurred faster in normal females than in males. Growth hormone (GH) rose significantly in normal males but not in obese males. Following high overnight fasting values in some normal females showed no significant increase in GH levels but significantly higher GH values than obese females after 1-6 days of fasting. After summarizing starvation-induced metabolic changes common to all study groups the respective differences found between males and females and between normal and obese subjects are discussed.
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PMID:[Metabolic differences between males and females and between normal and obese subjects during total fast]. 93 57

Prolonged starvation is known to induce significant alterations in several cardiac lysosomal enzymes, particularly the acid proteinase cathepsin D. To determine what specific factors might mediate these changes, fetal mouse hearts in organ culture were maintained in media designed to simulate selected hormonal or nutritional substrate changes that accompany starvation. Reduced concentrations of glucose caused an increase in the activity of beta-acetylglucosaminidase but had no effect on cathepsin D or acid phosphatase activites (i.e., effects opposite from those of starvation). Also, high concentrations of free fatty acid, acetoacetate, and beta-OH-butyrate induced an increase in cathepsin D (+18%) and a simultaneous decrease in glucosaminidase (-19%), with little change in acid phosphatase. Furthermore, glucagon had no effect on any of the enzymes, whereas growth hormone caused a small (6%) increase in cathepsin D activity. In addition, insulin deprivation caused significant increases (7-25%) in the activities of all three enzymes. Insulin deprivation and excess ketones, but not the other interventions, increased the proportion of enzyme activity which was nonsedimentable. These results suggest the possibility that lysosomal alterations during starvation may be related in part to prolonged insulin deficiency and exposure to high concentrations of ketones and free fatty acids.
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PMID:Hormonal and nutritional substrate control of cardiac lysosomal enzyme activities. 95 75

We studied nine patients with anorexia nervosa: five were "undernourished" and four were "well-nourished". The undernourished patients had significantly higher plasma growth hormone (GH) levels in a fasting state and higher GH rebounds following glucose administration. In four of these patients, GH levels decreased to normal after weight restoration. Decreased urinary follicle stimulating hormone (FSH) in three and plasma luteinizing hormone in six patients were not related to nutritional status; however, positive correlation was found between duration of illness and urinary FSH. Other results included decreased plasma testosterone in the one male, elevated plasma cortisol in five, and decreased 17-ketosteroid excretion in five patients. The results support elevated GH as secondary to starvation of anorexia nervosa and not an independent hypothalamic-pituitary disturbance. Other endocrine findings indicate hypothalamic-pituitary malfunction is not confined to GH.
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PMID:Hypothalamic-pituitary function in anorexia nervosa. 113 Sep 37

1. To study the role of group-specific protease in enzyme degradation, alternation of its activity under various physiological conditions was examined. 2. Studies on the distribution of group-specific protease in various organs of rats showed high activity in skeletal muscle and the muscle layer of small intestine, and rather low activity in liver. The activity varied in different muscles, but red muscle tended to have higher activity than white muscle. Activity was much lower in the muscles of the stomach and colon than in those of the small intestine. 3. Group-specific protease in skeletal muscle increased under various dietary conditions (starvation, protein-free diet or high protein diet), but the activities in the muscle layer of the small intestine and liver were not greatly influenced by dietary conditions. None of the hormones tested (i.e. hydrocortisone, glucagon, insulin, growth hormone and estrogen) influenced the activity of group-specific protease in liver. 4. The level of group-specific protease in skeletal muscle was increased markedly fifteen days after denervation, with a reciprocal decrease in the level of muscle phosphorylase, which is a good substrate of the protease. 5. Liver protease activity appeared in the late suckling period. The activity in skeletal muscle was high at the time of birth and attained the adult level 3 weeks after birth. The activity in the muscle layer of the small intestine did not change after birth. Thus the mechanism for evoking these three specific proteases during development are apparently different. The activity of liver protease began to decrease approximately 12 h after partial hepatectomy and reached a minimum after about 72 h. Recovery of the protease activity was very slow and activity had not returned to the normal value 7 days after the operation. This observation seems to be consistent with the fact that there is little or no protease activity in liver in the neonatal period.
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PMID:Studies on new intracellular proteases in various organs of rat. 3. Control of group-specific protease under physiological conditions. 116 15

Growth hormone concentration has been assayed in 105 children (45 girls and 60 boys) during starvation and following its stimulation with clonidine and insulin and during the sleep. A significant difference between growth hormone concentration during fasting and after stimulation has been noted. No statistically significant difference between growth hormone concentrations during the sleep and following insulin has been found. The most intensive growth hormone release has been observed during the sleep. Test with clonidine is technically simple and may be performed also in the out-patient clinics.
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PMID:[Growth hormone concentration following various factors stimulating its release]. 130 18

Male and female wild Norway rats (Rattus norvegicus Erxleben) and males and female albino outbred rats (Ipf:RIZ) were crossbred. The resulting animals (F1 hybrids) were the control, noninbred group (0% inbred). By systematic full-sib mating, two experimental groups (50 and 91% of inbred) were produced. Half of each group (both males and females) was exposed to physical stress (3 days of starvation and 3 hr of swimming). The other half of each group was anesthetized using ether to collect blood. The anterior pituitary hormone concentrations of prolactin (PRL), corticotropin (ACTH), and growth hormone (rGH) in blood serum were determined by the radioimmunoassay method. Significant relationships between the PRL, ACTH, and rGH concentrations in blood serum and the inbreeding coefficient were observed: A significant PRL content decrease in blood serum occurred (linear function) and the rGH and ACTH content diminished significantly rapidly (quadratic function). These changes were affected by an increase in homozygosity. Stress significantly influenced PRL, ACTH, and rGH concentrations as well. The sex of rats significantly determined PRL and ACTH content only. Hormone levels were also influenced by interactions between the factors studied (inbred level, sex, stress).
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PMID:The effect of genetic variability (degree of homozygosity) on serum levels of the anterior pituitary hormones prolactin, corticotropin, and growth hormone in rats. 133 58

Structural heterogeneity has been demonstrated for growth hormone (GH) receptors from a number of species, and both high and low affinity art receptors have been characterised by ligand binding studies. In the present study, we have transfected Chinese hamster ovary (CHO-K1) cells with a cDNA clone encoding a full-length transmembrane ovine (o) GH receptor, under the regulatory control of the human metallothionein IIA promoter. A stably transfected cell line was established (GHR9.5) which expresses on the cell surface a single class of receptor which binds 220,000 [125I]oGH molecules at high affinity (Kd = 0.30 nM) which is comparable to the affinity established for endogenous oGH receptors in postnatal sheep liver microsomes (Kd = 0.27 nM, Freemark et al. (1987) Endocrinology 120, 1865-1872). The expressed receptor also binds ovine placental lactogen (oPL, 205,000 binding sites per cell) with high affinity (Kd = 0.76 nM). The presence of two species of oGH receptor was detected in GHR9.5 cells using affinity cross-linking analysis (M(r) 148,000 and M(r) 73,000) and given that the oGH receptor cDNA codes for a non-glycosylated receptor of M(r) 69,914, it is likely that these cross-linked species correspond to homodimeric and monomeric forms of the oGH receptor, each binding to a single molecule of GH. Parallel cross-linking studies with sheep liver microsomes also demonstrated two oGH receptor species (M(r) 133,000 and M(r) 58,000), the difference in relative molecular weights between the transfected and endogenous receptors presumably resulting from tissue-specific post-translational modifications. In the presence of oGH, the GHR9.5 cells respond by increasing total cellular protein synthesis by 27% relative to non-GH-exposed GHR9.5 cells, indicating the functionality of the expressed receptor. We also demonstrate unequivocally that oPL, through a specific interaction with the transfected oGH receptor, is able to mediate a similar cellular response (38% protein synthesis induction). Responsiveness to oGH and oPL in the GHR9.5 cells is dependent on serum starvation prior to oGH exposure and occurs only with prolonged exposure (greater than 2 h) to oGH. This cellular stimulation occurs independently of c-fos transcription which has previously been shown to be one of the earliest events associated with GH action in tissues expressing endogenous GH receptors (Doglio et al. (1989) Proc. Natl. Acad. Sci. USA 86, 1148-1152; Slootweg et al. (1990) J. Mol. Endocrinol. 4, 265-274).
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PMID:Functional expression of an ovine growth hormone receptor in transfected Chinese hamster ovary cells. 151 79

To understand the roles of four highly homologous rat hepatic serine protease inhibitor genes (Spi 2.1, Spi 2.2, Spi 2.3, and alpha 1-antitrypsin), we measured the hepatic content of their specific mRNAs under several physiological conditions. Spi 2.1 and 2.3 mRNAs, which are regulated by growth hormone, paralleled serum growth hormone levels developmentally. Only Spi 2.1 mRNA decreased with starvation, while Spi 2.2, 2.3, and alpha 1-antitrypsin mRNAs did not change. Despite the close homology of the Spi genes to mouse contrapsin, which is regulated by testosterone, none of the serine protease inhibitor mRNAs examined here was dependent on androgens for expression. Spi 2.2 mRNA displayed a unique ontogenetic regulation, with a rise in hepatic content at day 19 to levels five times that of any other age group. These studies confirm the importance of growth hormone in the regulation of Spi 2.1 and 2.3 mRNAs and suggest that Spi 2.2 mRNA may be regulated by metabolic alterations occurring in the weaning period.
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PMID:Discoordinate hormonal and ontogenetic regulation of four rat serpin genes. 159 Mar 55

Adult fed and starved Warren chickens, 2 yr of age, and approaching the end of the second laying year, were injected iv with 1 of the following products: 10 micrograms of thyrotropin releasing hormone (TRH); 100 micrograms of bovine thyrotropin (bTSH); 100 micrograms of ovine growth hormone (oGH); saline. The influence on plasma concentrations of thyroxine (T4), triiodothyronine (T3) or chicken GH (cGH) were followed. Prior to injection, it was clear from the control values that starvation for 3 d decreased plasma levels of T3 and increased cGH, whereas 7 d of fasting increased T4 and cGH. The plasma levels of cGH were elevated greater than 10-fold at 15 min following the TRH challenge in food-deprived chickens compared to a less than 4-fold increase in normal fed hens. This increase was followed by a rise in T3 after 1 h, which was also more pronounced in the starved animals, whereas T4 decreased or remained unaffected. Increases in T4 can, however, be obtained with 100 micrograms TSH in normal fed (2-fold) or starved animals (greater than 3-fold). Following injection of 100 micrograms oGH, a significant increase in T3 levels was observed which in fed animals was already present at 30 min, but the higher levels persisted for 1 and 2 h in fed and starved hens. At the same time, a decrease in T4 was observed in both groups of GH-treated chickens. It is concluded that TRH at the dose used is not thyrotropic but has a somatotropic effect and is responsible for the peripheral conversion of T4 into T3.
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PMID:Thyrotropin-releasing hormone (TRH) is not thyrotropic but somatotropic in fed and starved adult chickens. 174 1

From an endocrinological aspect, metabolic changes of humoral factors were examined in a female patient deprived of food for 18 days. On admission, serum acetoacetate (AcAc) and 3-hydroxybutyrate (3-OHB) levels markedly increased. The serum free triiodothyronine (T3) level decreased, whereas serum thyroxine (T4) concentrations were within normal range. Diurnal variations of serum cortisol levels were not observed. At day six after admission, the effects of intravenously administered thyrotropin releasing hormone (TRH) on pituitary thyroid stimulating hormone (TSH) was suppressed, whereas growth hormone (GH) was hyper-responsive. Re-feeding gradually normalized the decreased free T3 level following the reduction of serum ketone bodies. The diurnal rhythmicity of cortisol secretion was restored. At day 17, the TSH response to TRH was restored, while the GH hyperreaction was attenuated. The present case provided evidence that starvation elicits lowered TSH response and GH hypersecretion to intravenously administered TRH, and distorts diurnal rhythmicity of adrenal cortisol secretion in a healthy subject without any psychogenic disorders.
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PMID:Altered hormonal status in a female deprived of food for 18 days. 177 Mar 28


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