Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of this study was to determine whether skeletal muscle mass, myofibrillar adenosinetriphosphatase activity, and the expression of myosin heavy (MHC) and light chain subunits are differentially affected in juvenile (4 wk) and young adult (12 wk) rats by a hypertrophic growth stimulus. Hypertrophy of the plantaris or soleus was studied 4 wk after ablation of either two [gastrocnemius (GTN) and soleus or plantaris] or one (GTN) synergistic muscle(s). There was no difference in the relative magnitude of hypertrophy because of age. Plantaris myofibrillar adenosinetriphosphatase activity was decreased 21 and 12% in juvenile and adult rats, respectively, as a result of ablation of both the GTN and soleus. Slow myosin light chain isoforms (1s and 2s) were expressed to a greater extent in hypertrophied plantaris muscles of both ages, but the increase in 1s was greater in juvenile rats. The relative expression of slow beta-MHC in hypertrophied plantaris muscles increased by 470 and 350%, whereas MHC IIb decreased by 70 and 33% in juvenile and adult rats, respectively. The relative expression of MHC IIa increased (56%) in the plantaris after ablation in juvenile rats only. These shifts in myosin subunit expression and the increases in mass were generally about one-half the magnitude when only the GTN was removed. There were no detectable myosin shifts in hypertrophied soleus muscles. Although the extent of muscle hypertrophy is similar, the shifts in myosin subunits were greater in juvenile than in young adult rats.
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PMID:Age effects on myosin subunit and biochemical alterations with skeletal muscle hypertrophy. 153 98

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

Samples of semitendinosus muscle from 28 male cattle (18 Salers and 10 Limousins) were taken at 10 months (biopsy) and at 16 months of age (at slaughter). The animals had received the same diet and were slaughtered after the same duration of fattening. The activities of isocitrate dehydrogenase and lactate dehydrogenase were measured in the muscle samples. The five lactate dehydrogenase isoenzymes were separated by electrophoresis under non-denaturing conditions and assayed by densitometry. Fibres were identified by histochemistry by myofibrillar ATPase and succinate dehydrogenase activities as SO (slow oxidative), FOG (fast oxidative glycolytic) or FG (fast glycolytic), and by immunohistochemistry by their reaction to monoclonal antibodies specific to slow and fast myosin heavy chain reactions in I, IIC, IIA, IIAB and IIB type fibres. The isocitrate dehydrogenase activity was not modified between 10 and 16 months of age; the lactate dehydrogenase activity decreased and was correlated with an increase in the proportion of the H isozyme to the detriment of the proportion of the M form. This period was characterized by an increase in fibre size, increased expression of MHC IIa, resulting in more IIA fibres, less IIB fibres, and an increase in the percentage of type IIAB fibres, however the proportions of SO, FOG and FG, when analysed statistically, were not modified between 10 and 16 months of age.
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PMID:Changes in the metabolic and contractile characteristics of muscle in male cattle between 10 and 16 months of age. 1041 83

The purpose of this study was to examine myosin heavy chain (MHC) and myosin light chain (MLC) isoforms following 12 wk of progressive resistance training (PRT). A needle biopsy was taken from the vastus lateralis to determine fiber-type expression [ATPase (pH 4.54) and MHC/MLC] in seven healthy men (age = 74.0 +/- 1.8 yr). Subjects were also tested for 1-repetition maximum (1-RM), pre- and posttraining. The progressive knee extensor protocol consisted of three sets at 80% of 1-RM 3 days/wk for 12 wk. Freeze-dried, single muscle fibers were dissected for MHC and MLC analysis and then subjected to SDS-PAGE and silver staining, pre- and posttraining. MHC expression increased in the I (10.4%; P < 0.05) and decreased in I/IIa (9.0%; P < 0.05), I/IIa/x (0.9%; P < 0.05), and IIa/x (8.9%; P < 0.05) isoforms, with no change in the IIa and IIx isoforms, pre- vs. posttraining (total fibers = 3,059). The MLC(3f)-to-MLC(2) ratio did not change with the PRT in either the MHC I or MHC IIa isoforms (total fibers = 902), pre- to posttraining. ATPase fiber distribution did not significantly differ following training (I: 50. 4 +/- 6.7 vs. 51.9 +/- 7.9, IIa: 36.8 +/- 5.3 vs. 41.1 +/- 7.0, IIb: 12.8 +/- 5.6 vs. 7.0 +/- 4.0%; pre- vs. posttraining, respectively). 1-RM increased (51.9%; P < 0.05) from pre- to posttraining. The PRT provide a stimulus for alterations in MHC isoforms, which demonstrated a decrease in all hybrid isoforms and an increase in MHC I expression (not found in the ATPase results), unlike the MLC ratio (3:2), which was not altered with training.
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PMID:Progressive resistance training reduces myosin heavy chain coexpression in single muscle fibers from older men. 1065 30

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

The effects of spinal cord injury (SCI) on the profile of sarco(endo) plasmic reticulum calcium-ATPase (SERCA) and myosin heavy chain (MHC) isoforms in individual vastus lateralis (VL) muscle fibers were determined. Biopsies from the VL were obtained from SCI subjects 6 and 24 wk postinjury (n = 6). Biopsies from nondisabled (ND) subjects were obtained at two time points 18 wk apart (n = 4). In ND subjects, the proportions of VL fibers containing MHC I, MHC IIa, and MHC IIx were 46 +/- 3, 53 +/- 3, and 1 +/- 1%, respectively. Most MHC I fibers contained SERCA2. Most MHC IIa fibers contained SERCA1. All MHC IIx fibers contained SERCA1 exclusively. SCI resulted in significant increases in fibers with MHC IIx (14 +/- 4% at 6 wk and 16 +/- 2% at 24 wk). In addition, SCI resulted in high proportions of MHC I and MHC IIa fibers with both SERCA isoforms (29% at 6 wk and 54% at 24 wk for MHC I fibers and 16% at 6 wk and 38% at 24 wk for MHC IIa fibers). Thus high proportions of VL fibers were mismatched for SERCA and MHC isoforms after SCI (19 +/- 3% at 6 wk and 36 +/- 9% at 24 wk) compared with only ~5% in ND subjects. These data suggest that, in the early time period following SCI, fast fiber isoforms of both SERCA and MHC are elevated disproportionately, resulting in fibers that are mismatched for SERCA and MHC isoforms. Thus the adaptations in SERCA and MHC isoforms appear to occur independently.
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PMID:Phenotypic adaptations in human muscle fibers 6 and 24 wk after spinal cord injury. 1174 54

In order to obtain broader insights into the equine musculoskeletal system, we studied the fibre type composition of 2 locomotory muscles in biopsies from Dutch Warmblood foals taken at 3 different ages in the first year postpartum. The muscle fibre types were determined histochemically as well as immunohistochemically. ATPase-characterised IIB fibres appear to express either IId or type lIa plus IId myosin heavy chain (MHC). A high percentage of fibres classified as IIA with ATPase expressed both fast types of MHC. The type I classification by the 2 methods matched almost completely. There was an increase with age of fibres expressing I and IIa MHC in the gluteus medius. At the same time, there was a decrease of fibres expressing IId MHC and fibres co-expressing MHC IIa and IId. MHC expression of the semitendinosus muscle did not change over time at first, but from age 22-48 weeks there was a decrease in the percentage of type IId fibres. In general, the gluteus medius contained more type I fibres but fewer type IId fibres compared to the semitendinosus. At most ages the fibre type compositions of both muscles correlated with one another. To examine the effect of exercise, one-third of the foals were given box rest, one-third received training and one-third kept at pasture during the first 22 weeks of life. The 3 exercise groups differed in their fibre type composition; however, these differences could not be attributed to the effect of exercise.
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PMID:Changes in fibre type composition of gluteus medius and semitendinosus muscles of Dutch Warmblood foals and the effect of exercise during the first year postpartum. 1190 60

The purpose of this study was to characterize the myosin heavy chain (MHC) composition of single muscle fibers from the gastrocnemius of male collegiate distance (DIST; n = 7), middle-distance (MID; n = 6), and recreational runners (REC; n = 6). Additionally, mATPase histochemistry was used to serve as a comparison to previous studies and the single fiber MHC technique. SDS-PAGE of single muscle fibers revealed a higher proportion of MHC I in DIST compared to MID and REC (74.9 +/- 4.3 vs 54.4 +/- 2.8 vs 56.2 +/- 2.9 %, respectively; p < 0.05), less MHC IIa/IIx in DIST compared to MID and REC (0.0 +/- 0.0 vs 6.0 +/- 2.4 vs 15.9 +/- 4.2 %, respectively; p < 0.05), and more total hybrids (I/IIa+IIa/IIx+I/IIa/IIx) in REC than both run groups, DIST and MID (23.0 +/- 3.3 vs 6.2 +/- 1.1 vs 13.2 +/- 2.6 %, respectively; p < 0.05). ATPase histochemistry (pH 4.54) revealed a higher percentage of type I fibers in DIST compared to MID and REC (71.1 +/- 3.1 vs 56.3 +/- 2.5 vs 59.8 +/- 2.3 %, respectively; p < 0.05), a higher percentage of type IIa in MID compared to DIST and REC (43.3 +/- 2.7 vs 28.5 +/- 3.1 vs. 30.2 +/- 3.1 %, p < 0.05), and a higher distribution of type IIb in REC than both run groups (10.0 +/- 2.7 vs 0.4 +/- 0.2 vs 0.4 +/- 0.2 %, p < 0.05). These results suggest that distance running leads to an increase in MHC I expression, training for mid-distance events leads to a prevalence of MHC IIa, and run training leads to a decrease in hybrid fibers.
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PMID:Myosin heavy chain composition of single muscle fibers in male distance runners. 1240 79

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

Biopsy samples were taken from the vastus lateralis of 18- to 84-yr-old male sprinters (n = 91). Fiber-type distribution, cross-sectional area, and myosin heavy chain (MHC) isoform content were identified using ATPase histochemistry and SDS-PAGE. Specific tension and maximum shortening velocity (V(o)) were determined in 144 single skinned fibers from younger (18-33 yr, n = 8) and older (53-77 yr, n = 9) runners. Force-time characteristics of the knee extensors were determined by using isometric contraction. The cross-sectional area of type I fibers was unchanged with age, whereas that of type II fibers was reduced (P < 0.001). With age there was an increased MHC I (P < 0.01) and reduced MHC IIx isoform content (P < 0.05) but no differences in MHC IIa. Specific tension of type I and IIa MHC fibers did not differ between younger and older subjects. V(o) of fibers expressing type I MHC was lower (P < 0.05) in older than in younger subjects, but there was no difference in V(o) of type IIa MHC fibers. An aging-related decline of maximal isometric force (P < 0.001) and normalized rate of force development (P < 0.05) of knee extensors was observed. Normalized rate of force development was positively associated with MHC II (P < 0.05). The sprint-trained athletes experienced the typical aging-related reduction in the size of fast fibers, a shift toward a slower MHC isoform profile, and a lower V(o) of type I MHC fibers, which played a role in the decline in explosive force production. However, the muscle characteristics were preserved at a high level in the oldest runners, underlining the favorable impact of sprint exercise on aging muscle.
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PMID:Aging, muscle fiber type, and contractile function in sprint-trained athletes. 1669 Jul 91


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