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

Clinical observations suggest that overt rhabdomyolysis may occur if severe hypophosphatemia is superimposed upon a pre-existing subclinical myopathy. To examine this possibility, a subclinical muscle cell injury was induced in 23 dogs by feeding them a phosphorus- and calorie-deficient diet until they lost 30% of their original weight. To induce acute, severe hypophosphatemia in the animals after partial starvation, 17 of the dogs were given large quantities of the same phosphorus-deficient diet in conjunction with an oral carbohydrate supplement, which together provided 140 kcal/kg per day. After phosphorus and caloric deprivation, serum phosphorus and creatine phosphokinase (CPK) activity were normal. Total muscle phosphorus content fell from 28.0+/-1.3 to 26.1+/-2.5 mmol/dg fat-free dry solids. Sodium, chloride, and water contents rose. These changes resembled those observed in patients with subclinical alcoholic myopathy. When studied after 3 days of hyperalimentation, the animals not receiving phosphorus showed weakness, tremulousness, and in some cases, seizures. Serum phosphorus fell, the average lowest value was 0.8 mg/dl (P <0.001). CPK activity rose from 66+/-357 to 695+/-1,288 IU/liter (P <0.001). Muscle phosphorus content fell further to 21.1+/-7.7 mmol/dg fat-free dry solids (P <0.001). Muscle Na and Cl contents became higher (P <0.01). Sections of gracilis muscle showed frank rhabdomyolysis.6 of the 23 phosphorus- and calorie-deprived dogs were also given 140 kal/kg per day but in addition, each received 147 mmol of elemental phosphorus. These dogs consumed their diet avidly and displayed no symptoms. They did not become hypophosphatemic, their CPK remained normal, and derangements of cellular Na, Cl, and H(2)O were rapidly corrected. The gracilis muscle appeared normal histologically in these animals. These data suggest that a subclinical myopathy may set the stage for rhabdomyolysis if acute, severe hypophosphatemia is superimposed. Neither acute hypophosphatemia nor rhabdomyolysis occur if abundant phosphorus is provided during hyperalimentation.
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PMID:Hypophosphatemia and rhabdomyolysis. 74 77

Carbohydrate metabolism was examined in different organs of rats with dietary potassium deprivation for 4 weeks. Thereafter, a 24- or 48-hour starvation period caused a significant decrease of skeletal muscle and liver glycogen content in K+-depleted (KD) rats, whereas kidney glycogen concentration increased and heart glycogen remained unchanged. In contrast, liver glucose concentration was significantly higher in starved KD animals without changes in muscle, heart, and kidney glucose concentrations. Potassium depletion caused a highly significant decrease of plasma and muscle potassium concentrations, metabolic alkalosis, reduced plasma insulin, and increased creatine phosphokinase levels. Blood lactate, pyruvate, and oxoglutarate levels were significantly enhanced in fasted KD rats, whereas blood citrate, beta-hydroxybutyrate, and glucose concentrations were unchanged. Blood acetoacetate level, however, was significantly reduced following potassium depletion. Therefore, beta-hydroxybutyrate/acetoacetate ratio increased significantly, whereas lactate/pyruvate ratio was not influenced. Our results clearly indicate impaired carbohydrate metabolism in potassium-depleted rats.
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PMID:Carbohydrate metabolism in potassium-depleted rats. 389 82

We studied a 23-year-old man with lipid storage myopathy. Five members of his family had hyperlipoproteinemia, and his consanguineous parents had elevated serum creatine kinase levels, although only the father showed clinical evidence of myopathy. The patient's intramuscular carnitine content was slightly reduced, but the reduction was not significant compared with the average value for reported cases with carnitine deficiency. Urinary excretion of carnitine showed good responses to starvation, long-chain fatty acid loading, and corticotropin administration. Therefore, his carnitine metabolism was normal. Administration of corticotropin or carnitine did not bring about any improvement of the symptoms. A connection between lipid storage myopathy and hyperlipoproteinemia was suggested.
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PMID:Lipid storage myopathy in familial hyperlipoproteinemia. 672 23

The pattern of change in activity of two enzymes in rat skeletal muscle during body storage after death has been determined. Myofibrillar protease activity was found to increase linearly with time of storage post mortem at room temperature but not at 4 degrees C. In contrast, creatine phosphokinase activity declines linearly with time, and again storage at 4 degrees C prevented the change in enzyme activity. Starvation of animals for 5 days or forced exercise prior to death did not markedly alter the rate of change in activity of the two enzymes, although creatine phosphokinase specific activity at time of death was higher in the starved and exercised rats as compared to control animals. A plot of the logarithm of protease/creatine phosphokinase specific activities ratio versus time post mortem yields a linear curve at room temperature. These observations offer a potential method for estimating time of death.
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PMID:Post-mortem changes in skeletal muscle protease and creatine phosphokinase activity--a possible marker for determination of time of death. 699 16

1. The palmitate oxidation by intact preparations of rat hemidaphragm, m.soleus and m.flexor digitorum brevis and by teased fibers of human m.pectoralis was studied. 2. The structural and metabolic viability of the in vitro preparations was shown by a low leakage of soluble creatine kinase, a constant rate of palmitate oxidation and only a small stimulatory effect of L-carnitine. 3. With hemidaphragm the palmitate oxidation rate increases with both the palmitate concentration (0-3 mM) and the palmitate/albumin molar ratio (0.5-5.0). 4. The apparent Km for palmitate oxidation was about 1.5 mM at 0.1 and 0.2 mM albumin and about 2.7 mM at 0.4 and 0.6 mM albumin, which correlates with the higher affinity of albumin for palmitate at lower palmitate/albumin molar ratios. 5. After prolonged starvation the apparent Km at 0.4 mM albumin is markedly lower. In whole homogenates of diaphragm the apparent Km at 0.4 mM albumin is only about 370 microM. 6. The calculated maximal oxidation rate was not significantly different for all albumin concentrations examined (23-32 nmol/min per g), did not change after starvation and appears to be of the same order of magnitude as the rate of endogenous fatty acid consumption (30-40 nmol/min per g). 7. Results suggest that substrate availability is a main factor for the oxidation rate of exogenous palmitate by hemidiaphragm in vitro and that the magnitude of the apparent Km is largely dependent upon the degree of label dilution with fatty acids of endogenous origin.
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PMID:Palmitate oxidation by intact preparations of skeletal muscle. 715 Jun 12

1. The muscle tension and the state of high-energy phosphate metabolism during contraction of the sartorius muscle in frogs (Rana catesbeiana) starved for 1-5 months was studied by in vivo 31P-NMR spectrometry. 2. Muscle tension began to decrease after 2-month starvation compared with the control group and decreased to about one-third of the control value after a 5-month starvation. 3. Muscle contraction induced by electrical stimulation or the use of anaerobic perfusion fluid did not decrease the concentration of creatine phosphate (PCr) or beta-ATP, and only negligibly changed the PCr/Pi ratio from starvation. 4. These results suggest a decrease in creatine kinase activity in the muscle of starved frogs.
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PMID:Phosphate metabolism during muscular contraction in starved frogs (Rana catesbeiana). 790 30

The enzymatic characterization of sarcoplasmic reticulum membrane fragments from rabbit skeletal muscle presented in this paper shows that glycogen phosphorylase, as well as other enzymes (e.g., creatine kinase, myokinase, phosphorylase kinase, glycosidase, AMP-deaminase, phosphoglucomutase) are associated with these membrane preparations. Amongst these enzymes, the highest activity associated with sarcoplasmic reticulum membranes is that of glycogen phosphorylase, which is mostly (at least 95%) in its b form (dephosphorylated form), since its activity in sarcoplasmic reticulum membranes is largely dependent upon AMP. A protocol is presented to quantify the amount of phosphorylase bound to sarcoplasmic reticulum membranes from fluorimetric measurements of the content of its coenzyme, pyridoxal 5'-phosphate. The content of phosphorylase ranged from 0.03 to 0.37 mg phosphorylase per mg of membrane protein, in sarcoplasmic reticulum membrane preparations made following several of the protocols most commonly used and also depending upon the length of the starvation period of the animal before killing. We also show that dilution of sarcoplasmic reticulum membranes to 0.1-0.2 mg protein per ml in a buffer containing 50 mM Tes-KOH (pH 7.4), 0.1 M KCl and 0.25 M sucrose removes at least 95% of glycogen phosphorylase from these membrane fragments, as well as other enzymes like myokinase and glycosidase. On these grounds, we suggest to introduce a final dilution step as indicated above in protocols of sarcoplasmic reticulum membrane preparations.
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PMID:Quantification and removal of glycogen phosphorylase and other enzymes associated with sarcoplasmic reticulum membrane preparations. 807 39

The creatine kinase activity in the skeletal muscles of one-day-old piglets is shown to be 1.3 times lower than that of five-day-old animals. The content of isoenzymes MM, MB and BB of creatine kinase in the skeletal muscles of one-and five-day-old piglets amounts to 25.8 and 30.4, 58.2 and 24.2%, of the total content of the enzyme, respectively. Insulin induces variations in the isoenzyme spectrum of creatine kinase in the skeletal muscles of piglets, which are more pronounced in one-day-old piglets, than in five-day-old animals. Cortisol seems to have no significant effect on the isoenzyme spectrum of creatine kinase in the skeletal muscles of piglets of both age groups. However, under conditions of starvation, the activity of creatine kinase in the skeletal muscles of piglets of both age groups falls, particularly in one-day-old animals.
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PMID:[The regulatory characteristics of creatine kinase activity in the skeletal muscle of piglets in the neonatal period]. 884 23

Seven female and three male common wombats (Vombatus ursinus) collected from forested areas of Victoria (Australia) over a 10 mo period, 10 April 1997 to 22 February 1998 had at least 30% of their skin affected by severe hyperkeratotic sarcoptic mange. Mangy wombats were grazing during the day, could be readily approached, were in poor body condition, and lacked subcutaneous fat. The anterolateral surface of the body was most heavily parasitised with Sarcoptes scabiei var wombati followed by the posterolateral surface, the dorsal region between the ears, the ears, ventral abdomen, medial aspect of the legs, axillary and inguinal areas, and the dorsal midline. Larvae were the most prevalent life-cycle stage followed by eggs, nymphs, females, and males. Mite numbers and the severity of clinical signs, namely thickness of scale crust and the degree of alopecia, were correlated and were symmetrical on each side of the body. Fissuring of crust and skin only occurred when scale crust was present. Bacterial infections occurred in three of 10 wombats within lymph nodes or the pleural cavity. Lymphoid depletion did not occur in lymph nodes or spleens and prescapular lymph nodes contained a greater amount of nuclear debris in germinal centres than non-mangy wombats. Seven wombats had fatty change in their livers. Gonads of mature wombats were not active or had minimal activity. Significant histopathological changes were not seen in the gastrointestinal tract, kidney, brain, myocardium, spleen, thyroid, reproductive tract, and gonads. Hematocrit, mean corpuscular volume, mean corpuscular hemoglobin, and concentrations of hemoglobin, lymphocytes, calcium, glucose, creatinine, total solids, total protein, albumin determined both colormetrically and electrophoretically, and globulins were significantly lower and concentrations of neutrophils, monocytes, phosphorus, urea, glutamate dehydrogenase, aspartate aminotransferase and creatine kinase were significantly higher in mangy versus captive wombats. Concentrations of erythrocytes, mean corpuscular hemoglobin, leucocytes, band neutrophils, eosinophils, nucleated erythrocytes, sodium, potassium, chloride, total bilirubin, alkaline phosphatase, and gamma glutamyltransferase for mangy wombats were not significantly different from that reported for captive wombats. Hematological and pathological changes in mangy wombats were consistent with anemia, inflammation, and changes seen with starvation.
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PMID:Distribution of life cycle stages of Sarcoptes scabiei var wombati and effects of severe mange on common wombats in Victoria. 1057 22

The contamination of water by metal compounds is a worldwide environmental problem. This study was undertaken to evaluate the impact of short-term cadmium exposure on metabolic patterns of the freshwater fish Oreochromis niloticus. The fish were exposed to 320, 640, 1,280 and 2,560 microg/l sublethal concentrations of Cd++ (CdCl2) in water for 7 days. The specific activities of the enzymes phosphofructo kinase (PFK-E.C.2.7.1.11.), lactate dehydrogenase (LDH-E.C.1.1.1.27.) and creatine kinase (CKE.C.2.7.3.2.) were decreased in white muscle after cadmium treatments, indicating decreases in the capacity of glycolysis in this tissue. Cadmium exposure induced increased glucose concentration in white muscle of fish. On the other hand, cadmium exposure at sublethal concentrations increased phosphofructo kinase and LDH in red muscle of fish. Cadmium significantly decreased total protein concentrations in liver and white muscle regardless of tissue glycogen levels. The data suggest that cadmium acts as a stressor, leading to metabolic alterations similar to those observed in starvation.
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PMID:Environmental cadium exposure and metabolic responses of the Nile tilapia, Oreochromis niloticus. 1150 39


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