Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We compared the localizations of lectin binding and activity for myosin ATPase and succinic dehydrogenase in sections of the gracilis, soleus, and masseter muscles from 10- and 60-day-old rats. In the 60-day-old rats, incubation of the muscle sections with the lectins ConA, GS-II, HPA, and jacalin gave rise to a mosaic staining pattern, especially in the gracilis muscle, in which the same fibers were strongly stained for ConA, GS-II, and HPA, whereas the staining with jacalin in these fibers was weak, and vice versa. There was no correspondence in the staining patterns for the enzymes and the lectins. In the masseter muscle only GS-II gave rise to distinct differences in the staining intensity between muscle fibers. In 10-day-old rats all fibers in the muscles were moderately stained with ConA, HPA, and jacalin, whereas a chessboard staining pattern could be observed after incubation with GS-II. In an extract of hindleg muscle from 60-day-old rats there was strong affinity for ConA and HPA and weak affinity for GS-II and jacalin, as shown by dot-blotting. After electrophoresis and blotting to nitrocellulose membranes, three muscle protein bands with apparent molecular weights of 100,000, 90,000, and 43,000 showed affinity for ConA, HPA, and GS-II, whereas no bands were jacalin positive. The complex lectin staining pattern in skeletal muscle might be related to development, specialization, and function of the muscles.
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PMID:Mosaic lectin and enzyme staining patterns in rat skeletal muscle. 138 89

In this study enzyme activities and lectin binding patterns in skeletal muscle from very old rats were investigated in order to evaluate changes in enzyme activity or carbohydrate expression in senile muscle. Activities for adenosine triphosphatase (ATPase), succinic dehydrogenase, non-specific esterase and the binding pattern for 31 lectins were investigated in the soleus muscles from very old (36 months) and young (3 months) rats. In ageing muscles atrophic, angulated muscle fibres are frequent. In cryostat sections these fibres were mostly but not always type II defined by the myosin ATPase reaction; few showed a strong esterase activity. Some showed strong activity for succinic dehydrogenase while others were weakly reacting. A number of lectins strongly bound to the sarcoplasm in angulated fibres while the binding to normal fibres in both old and young rat muscle was much weaker or even absent. Preferential binding to the ageing, angulated fibres was seen with Aleuria aurentia, Galantus nivalis, Caragana abborecens, Triticum vulgaris, Maackia amurensis, Sambucus nigra, Phaseolus vulgaris erythroagglutinin, and Phaseolus coccineus. Samples of homogenized and centrifuged muscles were run by electrophoresis and the gels blotted to nitrocellulose paper. Subsequent lectin staining of the blots detected that two glycoproteins with molecular weights around 25,000 and 21,000 daltons were present in old muscle, but not in young. Aberrant or elevated expression of sarcoplasmic glycoconjugates is involved in ageing muscle atrophy.
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PMID:Glycosylation pattern and enzyme activities in atrophic, angulated skeletal muscle fibres from ageing rats. 818 92

Complex-type oligosaccharides were detected in the sarcoplasm of muscle fibres from cat and human biceps using lectins and anticarbohydrate antibodies. The lectin Datura stramonium agglutinin strongly stained type II A fibres as identified by myosin ATPase activity after alkaline and acid preincubation. In contrast, all muscle fibres showed a moderate coarse granular staining after incubation with Tetracarpidum conophorum agglutinin and Telfairia occidentalis agglutinin which recognize tri-antennary complex glycans poorly bound by D. stramonium agglutinin. Strong sarcoplasmic staining in all muscle fibres was obtained after incubation with an antibody against branched N-acetyllactosamine structure while an antibody against binary 2 --> 3 sialyllactosamine glycans failed to detect the muscle fibres. Treatment of the muscle sections with sialidase prior to incubation with D. stramonium agglutinin did not influence the lectin staining pattern. Staining of blots from electrophoretically separated muscle proteins obtained by homogenization, solubilization and centrifugation of small muscle pieces showed D. stramonium agglutinin binding to a number of bands ranging from 200 kDa to 30 kDa. No D. stramonium agglutinin positive bands were observed in blots from separated mitochondrial proteins while blots from sarcoplasmic reticulum separated by electrophoresis stained many bands in the range from 200 kDa to 30 kDa. It may be concluded that all muscle fibres in human and cat biceps hold intracellular non-sialylated complex-type oligosaccharides and further, that a specific tri-antennary complex-type glycoform is strongly expressed in type II A fibres as recognized by D. stramonium agglutinin. These results indicate a different glycosylation of certain myofibrillar-associated proteins in muscle fibre types.
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PMID:The complex-type oligosaccharide binding lectin Datura stramonium agglutinin detects type II A muscle fibres in the branchial biceps from man and cat. 914 91