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Query: UMLS:C0026850 (muscular dystrophy)
 5,870 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A number of workers have reported that avian muscular dystrophy causes alterations in the levels of certain enzyme activities in "fast-twitch" muscle fibers but has little effect on enzyme activities in "slow-twitch" muscle fibers. In the present work, the effects of this disease on the content and relative rates of synthesis of a number of glycolytic enzymes and the skeletal muscle-specific MM isoenzyme of creatine kinase in chicken muscles was investigated. It was shown that (i) the approximate 50% reductions in steady-state concentrations of three glycolytic enzymes (aldolase, enolase, and glyceraldehyde-3-P dehydrogenase) in dystrophic breast (fast-twitch) muscle result predominantly from decreases in relative rates of synthesis, rather than accelerations in relative rates of degradation, of these proteins in the diseased tissue; (ii) in contrast to the situation with the glycolytic enzymes, muscular dystrophy has only minor effects (25% or less) on the content and relative rate of synthesis of MM creatine kinase in breast muscle fibers; (iii) the muscular dystrophy-associated alterations in content and synthesis of the glycolytic enzymes in breast muscle fibers become apparent only during postembryonic maturation of this tissue; and (iv) as expected, muscular dystrophy has no significant effect on the content or relative rates of synthesis of glycolytic enzymes in slow-twitch lateral adductor muscles of the chicken. These results are discussed in terms of the apparent similarities between the effects of muscular dystrophy and surgical denervation on the protein synthetic programs expressed by mature fast-twitch muscle fibers.
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PMID:Content and synthesis of glycolytic enzymes and creatine kinase in skeletal muscles and normal and dystrophic chickens. 397 May 44

A sandwich enzyme immunoassay method for measurement of beta subunit of muscle enolase in human serum was developed by use of purified antibodies to enolase beta subunit and beta-D-galactosidase from Escherichia coli as label. The assay was specific to the beta subunit with no cross-reaction with the alpha and gamma subunits of human enolase. The measurable range was from 10 pg to 10 ng per assay tube or 1 to 1000 ng/ml serum. Coefficients of variation within-run and between-run for the assay of serum beta subunit were less than 14%. Normal adult sera contained about 6 ng/ml of the beta subunit, and the levels were significantly elevated in sera of patients with muscular dystrophy and those with myocardial infarction. Serum levels of the beta subunit correlated well with those of creatine phosphokinase, but poorly with those of myoglobin in the same samples. The specific distribution of beta subunit in skeletal muscle and heart was confirmed by measuring the levels in various tissue extracts.
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PMID:Immunoassay of human muscle enolase subunit in serum: a novel marker antigen for muscle diseases. 634 61

In both 2- and 3-month-old 129 ReJ mice, the catalytic activity levels of three enzymes involved in glycogen breakdown (phosphorylase, enolase, and aldolase) were found to be 35-50% lower in hind limb muscles of dystrophic mice as compared with normal mice. The reduced activities of these enzymes in the diseased tissue was directly due to corresponding reductions in the number of enzyme molecules rather than being due to inactivation of the enzymes in the dystrophic muscle. Results of short term double isotope incorporation experiments conducted with muscle explants in vitro suggested that the rates of synthesis of these enzymes, and of most other abundant cytosolic proteins, relative to each other, were similar in hind limb muscles of normal and dystrophic mice. The present work on murine muscular dystrophy is discussed in terms of our previous studies into the influence of avian muscular dystrophy on the content and synthesis of abundant glycolytic enzymes in chicken skeletal muscles.
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PMID:Content and synthesis of several abundant glycolytic enzymes in skeletal muscles of normal and dystrophic mice. 669 88

The term limb-girdle muscular dystrophies (LGMD) identify about two dozens of distinct genetic disorders. Additional genes must play a role, since there are LGMD families excluded from any known locus. The aim of our work is to test a number of candidate genes in unclassified LGMD patient and control DNA samples. We selected the following 11 candidate genes: myozenin 1, 2 and 3, gamma-filamin, kinectin-1, enolase-3 beta, ZASP, TRIM 11 and TRIM 17, OZZ and zeta-sarcoglycan. These candidates were chosen for a combination of different reasons: chromosomal position, sequence homology, interaction properties or muscular dystrophy phenotypes in animal models. The exon and flanking intron sequences were subjected to molecular testing by comparative mutation scanning by HT-DHPLC of LGMD patients versus control. We identified a large number of variations in any of the genes in both patients and controls. Correlations with disease or possible modifying effects on the LGMD phenotype remain to be investigated.
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PMID:Candidate-gene testing for orphan limb-girdle muscular dystrophies. 1947 18