Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To study the aging of muscle fibres in red skeletal muscle, fibre number, fibre diameter and fibre type composition in the soleus muscle of male rats of 3, 12 and 24 months old were examined. The total number of muscle fibres remained unchanged, while average diameter increased slightly with increasing age. The staining intensity of myosin adenosine triphosphatase (ATPase) activity in the fibres decreased with advancing age. Therefore, observation on the basis of myosin ATPase histochemistry alone is not adequate to study the aging of muscle fibres. In the muscles of 24 month-old animals, four fibre types were recognized; 1) many (52%) type I-O fibres showing weak ATPase and succinate dehydrogenase (SDH) reactions with slight subsarcolemmal aggregates of diformazan (SAD); 2) some (33%) type M fibres showing weak ATPase and intense SDH reactions with marked SAD; 3) a few (12%) type O fibres showing weak ATPase and intense SDH reactions without SAD; and 4) very few (4%) type IIA fibres. Histochemical and morphometric results suggest that type I-O, type M and type O fibres are derived from type I, type I and type IIA fibres, respectively. Furthermore, no transitional fibres from type IIA to type I were observed. Therefore, age-related changes in fibre type composition in the muscle cannot be explained by the simple idea that most type IIA fibres are transformed into type I fibres.
 ...
PMID:Age-related changes in fibre number, fibre size, fibre type composition and adenosine triphosphatase activity in rat soleus muscle. 797 39

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.
 ...
PMID:Glycosylation pattern and enzyme activities in atrophic, angulated skeletal muscle fibres from ageing rats. 818 92

Integrin-linked kinase (ILK) participates with beta1 integrin to mediate extracellular matrix interactions, such as extracellular matrix reorganization. Thus, ILK is hypothesized to influence wound contraction and scar contracture and, as such, would be a target molecule to manipulate pharmacologically in expediting wound contraction or possibly preventing scar contracture. The expression of ILK messenger ribonucleic acid, along with ILK-protein expression, was found in fibroblasts. The localization of ILK in human skin and rat granulation tissue was documented by immunohistology. ILK was present in human dermal fibroblasts, but was not found in human epidermal cells in skin. Cells were transfected with wild-type ILK or kinase-deficient ILK (E359K) and were assayed for collagen lattice contraction, migration, and myosin adenosine triphosphatase (ATPase) activity. Cells overexpressing E359K were poorer at collagen lattice contraction than control cells, whereas cells overexpressing wild-type ILK were equal to control cells at lattice contraction. ILK overexpression enhanced cell migration, but E359K overexpression did not affect cell migration. Neither ILK nor E359K overexpression altered myosin ATPase activity. Hence, ILK action within fibroblasts appears unrelated to myosin ATPase control of microfilament-generated forces. ILK appears to be a target molecule for pharmacologic manipulation to expedite wound contraction or to prevent scar contracture.
 ...
PMID:Integrin-linked kinase: a possible role in scar contracture. 1474 74

Triiodothyronine (T3) is known to play a key role in the function of several tissues/organs via the thyroid hormone receptor isoforms alpha (TRalpha) and beta (TRbeta). We have investigated the effects of GC-24, a novel synthetic TRbeta-selective compound, on skeletal muscle fiber-type determination, cross-sectional area, and gene expression in rat skeletal muscles. For fiber typing, cross sections of soleus and extensor digitorum longus (EDL) muscles were stained for myosin ATPase activity at various pHs. Serum T3, T4, and cholesterol levels were also determined. Analysis of highly T3-responsive genes, viz., myosin heavy chain IIa (MHCIIa) and sarcoendoplasmic reticulum adenosine triphosphatase (SERCA1), was performed by quantitative real-time polymerase chain reaction. Equimolar doses of T3 and GC-24 had a similar cholesterol-lowering effect. T3, but not GC-24, decreased fiber type I and increased fiber type II abundance in soleus and EDL muscles. Conversely, in EDL, both T3 and GC-24 decreased the mean cross-sectional area of type I fibers. MHCIIa gene expression was reduced (approximately 50%) by T3 and unchanged by GC-24. SERCA1 gene expression was strongly induced by T3 (approximately 20-fold) and mildly induced by GC-24 (approximately two-fold). These results show that GC-24 does not significantly alter the composition of skeletal muscle fiber type and further strengthens the putative use of GC compounds as therapeutic agents.
 ...
PMID:Thyroid hormone receptor-beta-selective agonist GC-24 spares skeletal muscle type I to II fiber shift. 1594 69


<< Previous 1 2 3