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

Cross-sectional areas and succinate dehydrogenase (SDH) activities of muscle fibers in the rat levator ani (LA) and bulbocavernosus (BC) were determined and compared with those of the soleus (SOL) and superficial (TAs) and deep (TAd) portions of the tibialis anterior (TA). In addition, cell body sizes and SDH activities of spinal motoneurons innervating the LA and BC were examined. Histochemical myofibrillar adenosine triphosphatase (mATPase) staining reactions following alkaline and acid preincubations revealed that all the muscle fibers in the LA and BC were type IIB. Gel electrophoresis, however, showed that the LA and BC contained 2.9 and 2.4% type IIx myosin heavy chain (MHC) isoform, respectively. Immunohistochemical analyses using MHC antibodies showed that the muscle fibers in the LA and BC had types IIx / IIa (approximately 3%) or type IIb MHC isoforms. The mean fiber cross-sectional areas in the LA and BC were significantly smaller than those in the SOL, TAs, or TAd. The mean fiber SDH activities in the LA and BC were significantly lower than those in the SOL or TAd, and similar to TAs. The population of alpha motoneurons innervating the LA and BC had similar SDH activities, irrespective of their cell body sizes. These data indicate that the LA and BC are comprised of a relatively homogeneous population of small, fast and low oxidative fibers innervated by a relatively homogeneous population of spinal motoneurons. These characteristics of the muscle fibers and motoneurons are consistent with their function in short, high-intensity activities.
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PMID:Perineal muscles and their innervation: metabolic and functional significance of the motor unit. 957 66

The histochemical composition of the levator auris longus (LAL) muscle has been investigated in adult NMRi mice. Histochemical reaction for myofibrillar adenosine triphosphatase (ATPase) after preincubation in alkaline and acidic media, nicotine amideadenine-dinucleotide dehidrogenase (NADH-dehydrogenase), and alpha-glycerophosphate dehydrogenase were performed on cryosections of LAL muscle. Expression of myosin heavy chain (MyHC) isoforms was detected with the immunoperoxidase method applying monoclonal antibodies against MyHC isoforms -1, -2a, -2x/d, and -2b, as well as by sodium dodecylsulfate (SDS) glycerol gel electrophoresis. The muscle was proven to be a pure fast-twitch muscle. The most numerous fibers in LAL muscles contained MyHC-2b and some MyHC-2a. Histochemically, pure IIA fibers with oxidative metabolism and pure IIB fibers with glycolytic metabolism were detected. In contrast to the majority of mature control muscles, numerous hybrid fibers coexpressing MyHC-2x/d with MyHC-2a or MyHC-2b were present. Both hybrids were oxidative-glycolytic; additionally, some hybrids containing MyHC-2a were oxidative. In one out of six muscles, traces of MyHC-1 were detected both with immunoperoxidase staining and with SDS glycerol gel electrophoresis. Rare fibers that exceptionally expressed small amounts of MyHC-1 always coexpressed MyHC-2a, which is an additional proof that pure type I fibers do not exist in LAL. Due to these histochemical characteristics and to its previously described morphological features, the use of the LAL muscle as a model for various studies, particularly muscle and nerve interactions, is emphasized.
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PMID:Fiber types in the mouse levator auris longus muscle: a convenient preparation to study muscle and nerve plasticity. 1068 98

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.
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PMID:Thyroid hormone receptor-beta-selective agonist GC-24 spares skeletal muscle type I to II fiber shift. 1594 69