Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026850 (muscular dystrophy)
 5,870 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of glutathione peroxidase, a selenium containing enzyme, was measured in the blood of horses to determine its usefulness as an indicator of selenium status. In 15 horses the enzyme activity was positively related to the blood selenium concentration (P less than .001, r-0.98) over the range of enzyme activities of 8.2 to 140 units (mumoles NADP-oxidised/min/gHb) and selenium concentrations of 0.24 to 2.74 mumol/l. In a group of 8 horses which 2 foals had died with lesions of muscular dystrophy the enzyme activity increased from a mean of 11.8 units before treatment with selenium to 34.5 units after 2 intravenous injections of sodium selenite given one month apart. Another group of 8 horses grazing paddocks adjacent to this affected group did not receive any selenium treatment and had a mean enzyme activity of 11.9 units. Blood glutathione peroxidase activity was measured in 50 pasture-fed horses and 180 stall-fed horses. The range of activities found (7 to 158 units) indicated that selenium intake in horses varied widely between localities. All pasture-fed horses grazing areas where muscular dystrophy had occurred in foals had low activities (less than 20 units). In stall-fed horses the enzyme activity was influenced by selenium treatment, and horses which had been treated usually had higher activities than horses in the same stable with no history of selenium treatment. It was concluded that blood glutathione peroxidase is a suitable indicator of selenium status in horses.
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PMID:Blood glutathione peroxidase activity in horses in relation to muscular dystrophy and selenium nutrition. 65 82

Four adolescent boys with Duchenne (progressive) muscular dystrophy (DMD) of 10-11 years duration and six normal boys of similar age were studied on a metabolism ward for 22 days. Sodium and potassium intake was as follows: Period I, Na 60 mEq, K 60 mEq; Period II, Na 10, K 60; Period III, Na 10, K 95-150; Period IV, Na 60, K 60. The differences between the DMD group and the group of normal boys for sodium and potassium in serum and urine and for urinary aldosterone were not significant. These findings show that the pathologically elevated sodium-potassium ratio in skeletal muscle of patients with DMD is not due to increased aldosterone or other causes of renal wastage of potassium.
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PMID:Urinary sodium, potassium and aldosterone in Duchenne muscular dystrophy. 83 56

Myopathy resembling nutritional muscular dystrophy occurred in a colony of 150 guinea pigs. Of 54 animals affected, 27 died. Major clinical signs were depression, conjunctivitis, and reluctance to move. Lesions were widespread throughout skeletal and cardiac musculature. Clinical signs and deaths ceased when the diet was changed to a different commercial ration. A single intramuscular injection of sodium selenite and alphatocopherol brought prompt remission of clinical signs in one group of 20 so treated.
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PMID:Myopathy in guinea pigs. 92 53

Antibody prepared against troponin-C, the calcium binding component of the troponin complex, was reacted with I band segments, and the distribution of antibody binding was assessed by immuno-electron microscopy. The I segments were isolated from glycerinated pectoral muscle which was prepared from normal adult chickens and from dystrophic chickens of strain 308. The antibody was deposited at 384 A +/- 7 A intervals along the thin filaments of the normal muscle. In contrast to the normal controls the dystrophic muscle did not exhibit a distinct periodicity when reacted with anti-troponin-C. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate revealed that although protein bands corresponding to troponin-C could be observed in the gels of the dystrophic preparations, the troponin-C band had migrated slower than that from normal thin filaments. It is concluded that avian muscular dystrophy produces an alteration of the structure of troponin-C resulting in (1) an inability of the protein to combine with its specific antibody and (2) a change in its electrophoretic behavior.
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PMID:An effect of avian hereditary muscular dystrophy on the reaction of troponin-C with its antibody. 92 78

Duchenne muscular dystrophy (DMD) is a rapidly progressive crippling disease of young boys that is inherited as an X-linked recessive trait. Previous studies have demonstrated the usefulness of erythrocyte studies in exploring membrane abnormalities in inheritied muscular dystrophy. Erythrocyte spectrin peak II protein (m.w. equivalent to 220,000) was more highly phosphorylated under initial rate conditions in DMD than in controls. The extent of peak II phosphorylation was greater in DMD erythrocytes and a Na+ stimulated peak II phosphorylation effect (Avruch and Fairbanks 1974) was not found to account for the differences between DMD and controls. The phosphorylated state of spectrin proteins in the membrane was evaluated and no differences in DMD could be measured. The maximal transfer of phosphate from differences in DMD could be measured. The maximal transfer of phosphate from [gamma-32P]ATP to spectrin peak II accounts for approximately 5-10% of the total phosphate content of spectrin.
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PMID:Erythrocyte spectrin peak II phosphorylation in Duchenne muscular dystrophy. 97 7

The early interest in selenium related primarily to its toxicity, but since 1957 the element has been recognized as a dietary essential. The dietary requirement for selenium by most species is about .1 ppm. Deficiencies of selenium in cattle and sheep have been confirmed under natural grazing conditions in many countries of the world. Overt signs of inadequacy such as white muscle disease (nutritional muscular dystrophy) occur primarily in young calves or lambs born to selenium deficient dams. Infertility has increased in ewes grazing pastures low in selenium. In general, signs of deficiency have not occurred in older animals such as finishing beef cattle and lactating dairy cows. Subclinical deficiencies of selenium are not determined easily, however, and thus an inadequacy of the element may be limiting maximum animal performance under certain circumstances of drylot feeding. The current nutritional status of ruminant animals in many geographical areas and involving various feeding programs with this element has not been established. The recent widespread deficiency problems with nonruminants suggest that such an assessment should be made. Concentration of selenium in tissue, particularly in the liver, has been used in establishing selenium status of the animal. With lambs glutathione peroxidase activity in certain tissues may be a more accurate indicator of selenium adequacy than is selenium content of the tissue. Supplemental sodium selenite and sodium selenate by either oral administration or parenteral injection have prevented clinical signs of selenium deficiency and animal losses in both ruminant and nonruminant animals. Heavy pellets containing elemental selenium for placement in the rumen have proved effective. In general, organic forms of selenium are absorbed more readily by animals than are inorganic compounds. The dietary requirements for selenium and its metabolism are influenced by many nutrient interrelationships, including its interactions with sulfur, lipids, vitamin E, proteins, amino acids, and several microelements. The Food and Drug Administration gave approval in 1974 for the oral administration of supplemental selenium as either sodium selenite or sodium selenate to certain classes of swine and poultry. Similar approval in the United States for ruminants will require additional information, particularly with regard to the influence of dietary intake on concentrations of selenium in tissue and milk in beef and dairy animals.
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PMID:Selenium in ruminant nutrition: a review. 110 75

We compared the morphologic characteristics of muscle fiber necrosis and subsequent regeneration after injury induced by intramuscular injections of bupivacaine hydrochloride (BPVC) and a variety of solutions at acid and alkaline pH (acetic anhydride, citric acid buffer, and sodium carbonate buffer). After BPVC injection the necrotic muscle fibers were rapidly invaded by phagocytic cells, followed by active regeneration and very little fibrous scar formation. The regenerating muscle fibers increased rapidly in size and attained complete fiber type differentiation and regained their initial fiber diameter within 1 month. Both alkaline and acid solutions induced muscle fiber necrosis followed by regeneration. Fiber necrosis induced by alkaline buffers and acetic anhydride solutions above pH 5.0 produced changes quite similar to that induced by BPVC. However, injection with 0.1 M acetic anhydride at pH below 4.0 resulted in coagulative necrosis of the injured muscle with very little phagocytic infiltration with poor regenerative activity and dense fibrous tissue scarring. Thus, pH 4.0 appears to be the critical pH determining the type of muscle injury and subsequent poor phagocytic and regenerative activities. This model of acidic acetic anhydride injury may lead to the identification of factors which interfere with regeneration and cause fibrous tissue scarring in human muscular dystrophy.
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PMID:Comparison of behavior in muscle fiber regeneration after bupivacaine hydrochloride- and acid anhydride-induced myonecrosis. 163 76

A 9 year old male previously diagnosed as progressive muscular dystrophy whose serum CPK5430IU.l-1 was very high received general anesthesia. Before anesthesia, dantrolene sodium 2 mg.kg-1 was given. Anesthesia was induced with thiamylal 100 mg and vecuronium bromide 3 mg. Anesthesia was maintained with sevoflurane (0.5%) in nitrous oxide (66%) and oxygen (33%). The course of anesthesia was uneventful. The operative time was 80 minutes. At the end of the operation, the patient recovered smoothly from anesthesia. A 46 year old female with dystrophia myotonia also received general anesthesia. The patient was diagnosed as having this disease 26 years previously. Preoperatively, the patient was suspected to have cardiac damage. Anesthesia was induced with thiamylal 100 mg, fentanyl 100 micrograms, midazolam 5 mg and vecuronium bromide 4 mg, and maintained with sevoflurane (1.0%) in nitrous oxide (66%) and oxygen (33%). Anesthesia was uneventful, but at the end of the operation, the patient could not breath fully by herself. She was placed on a ventilator and observed carefully. The endotracheal tube was removed 150 minutes after the induction of anesthesia. In these two cases, sevoflurane and vecuronium bromide were used safely.
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PMID:[General anesthesia with sevoflurane and vecuronium for patients with dystrophia myotonica and progressive muscular dystrophy]. 168

Histidine-rich calcium binding protein (HRC) is a luminal sarcoplasmic reticulum (SR) protein of 165 kDa identified by virtue of its ability to bind 125I-labeled low-density lipoprotein with high affinity after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Hofmann et al., J. Biol. Chem. 264: 8260-8270, 1989). Its role in SR function is unknown. In this report, the gene encoding human HRC was localized to human chromosome 19 and mouse chromosome 7 by hybridization of a human HRC cDNA fragment to a panel of somatic cell hybrids. Known synteny between a portion of human chromosome 19 and a portion of mouse chromosome 7 and in situ hybridization of a biotin-labeled HRC probe to human chromosomes suggest a localization to a region corresponding to 19q13.3. The locus for myotonic dystrophy resides in the region 19q13.2-13.3. Therefore, we considered HRC, a muscle-specific gene, to possibly represent a "candidate gene" for myotonic muscular dystrophy. As a first step toward localizing HRC in relation to the myotonic dystrophy locus, we report the cloning of the human HRC gene, its intron-exon organization, and characterization of several informative polymorphisms to be used in future linkage studies in families with myotonic dystrophy. Of particular interest is an Alu-associated poly-d(GA) sequence located in an intron in the middle of the gene, and two stretches of acidic amino acids in the coding region of exon 1 that vary in length among different individuals.
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PMID:cDNA and genomic cloning of HRC, a human sarcoplasmic reticulum protein, and localization of the gene to human chromosome 19 and mouse chromosome 7. 203 93

Oral and parenteral preparations of Se are used worldwide to prevent and treat nutritional muscular dystrophy and other Se deficiency syndromes. There are extensive published data on the effects of oral supplementation on Se residues in food animal products. Very little published data exist on the effects of parenteral administration on Se residues, even for cattle and swine in which parenteral preparations are used extensively. The distribution of Se into kidney and liver appears to be equivalent for both forms of supplementation. Elimination of Se in milk is greater after parenteral administration and correlates with high plasma Se levels, however the milk excretion drops quickly and after 4 d returns to control levels (Little et al. 1979). Of particular interest is the finding that up to 18% of Se in an oral diet may be excreted in milk (Maus et al. 1980). Use of Se supplements in poultry results in increased levels of Se in liver, kidney, and eggs. Distribution of Se into liver and kidney is much greater than into breast muscle indicating a greater capacity of these organs to accumulate Se. Excretion of Se into eggs results in Se levels equivalent to those in liver and kidney, indicating that eggs are an important route of Se excretion in laying hens (Ort and Latshaw 1978). When Se supplementation stops, the liver, kidney, and egg white and yolk residues decline quickly to control values within 1-2 wk. Breast muscle Se content changes little during supplementation and after withdrawal of supplementation. Oral and parenteral selenium supplementation in swine result in greater accumulation of Se in liver and kidney than in muscle. Oral selenium supplementation also increases the excretion of Se into milk. This method has been used to prevent Se deficiency disease in piglets (Mahan et al. 1975). Oral supplementation with 0.1 ppm Se, as sodium selenate, did not result in levels of Se in blood, meat, or viscera at slaughter (Jenkins and Winter 1973). Despite the large amount of data available on Se residues in food animals, additional information on the pharmacokinetics of parenterally administered Se preparations is needed, especially in sheep and goats which receive parenteral Se supplements. Information on the disappearance kinetics of Se residues in meat and milk is needed for all ruminants. The data currently available in the literature does not allow the calculation of pharmacokinetic parameters of Se in any species. Properly performed pharmacokinetic studies would contribute a great deal towards a better understanding of how food animals utilize supplemental selenium.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Effects of oral and parenteral selenium supplements on residues in meat, milk and eggs. 218 65


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