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)

To study the diastolic properties of the heart includes examining active relaxation, passive ventricular stiffness and atrial contraction. (i) The main determinant of active relaxation is the adenosine triphosphate (ATP) concentration. Relaxation needs to occur so that the ATP content of the cell can be decreased by activation of the myosin ATPase, which in turn depends upon an intracellular messenger, elevation of the calcium transient. In a model of cardiac hypertrophy active relaxation is always slower. This slowing accompanies a slowing of the calcium transient, a diminution in the activity of the Na+/Ca2+ exchanger, a change in the properties of Na+, K+ ATPase and a decreased concentration of Ca2+ ATPase in the sarcoplasmic reticulum. (ii) Chamber stiffness is likely to be increased only in relation to the degree of ventricular hypertrophy. The main, if not unique, determinant of ventricular diastolic tissue stiffness is the structure and concentration of the collagen. Consequently tissue stiffness is augmented in cardiac hypertrophy in which the ventricular collagen concentration is elevated. It is important that both clinically and experimentally cases of cardiac hypertrophy, even those resulting from pressure overload in which myocardial stiffness and cardiac collagen concentration remain unchanged, have been documented. A good example of this is the DOCA-salt model of arterial hypertension. (iii) Atrial contraction is normally more rapid than ventricular contraction, the biological basis for which is the difference in isomyosin content.(ABSTRACT TRUNCATED AT 250 WORDS)
Eur Heart J 1992 Sep
PMID:Biological basis of diastolic dysfunction of the hypertensive heart. 139 55

The aim of the present study was to further subdivide the type II fibers of the human thyroarytenoid and posterior cricoarytenoid muscles by means of a modified myosin ATPase reaction. In order to understand the functioning of these highly strained muscles better, it is important to know the respective percentage of fatigue-resistant type IIA fibers and fatigable type IIB fibers. The material comprised the larynges of seven laryngectomized males aged between 45 and 70 years and four laryngectomized females aged between 39 and 72 years. After having been frozen in nitrogen, 10-microns-thick sections were cut from the laryngeal muscles in a cryostat. The pH-lability of the enzyme that can be utilized in a classical myosin ATPase reaction permits a differentiation between fiber types I, IIA and IIB. Evidently, this is not possible with every human muscle. The fiber types IIA and IIB of the thyroarytenoid and the posterior cricoarytenoid muscles could be clearly distinguished by means of the inhibition reactivation myofibrillar ATPase technique. Using this method, the myosin ATPase enzyme was initially inhibited by hydroxymercuribenzoate and subsequently reactivated by cysteine. Regarding the incidence of type I and IIA fibers, there was a statistically significant difference between the thyroarytenoid and the posterior cricoarytenoid muscles. The type IIA fiber content was statistically significantly higher in the arytenoid muscle than in the posterior cricoarytenoid muscle. The percentage of type IIB fibers was low, not only in the thyroarytenoid muscle and the posterior cricoarytenoid muscle but also in the other laryngeal muscles.(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Embryol (Berl) 1992 Sep
PMID:Fiber differentiation of the human laryngeal muscles using the inhibition reactivation myofibrillar ATPase technique. 141 83

1. Skeletal muscle samples were obtained by needle biopsy from one of two depths of the m. gluteus medius in a group of twenty race-trained thoroughbred horses. 2. The content of carnosine was determined in each muscle sample, part of which was used for histochemical analysis. Fibres were classified as type I, type IIA or type IIB on the basis of the pH dependent lability of the myosin ATPase reaction. 3. Muscle samples with a higher type II fibre section area (FSA) have a higher carnosine content than those with a higher type I FSA. 4. Multiple linear regression analysis was used to estimate the mean carnosine content of individual fibre types. The results estimated a mean carnosine content in type I fibres of 54 mmol (kg dry muscle (DM))-1, in type IIA fibres 85 mmol (kg DM)-1 and in type IIB fibres 180 mmol (kg DM)-1. 5. Based on the estimated values of single fibre carnosine content, there was close concordance between the estimated and the measured carnosine content of mixed fibre samples. 6. It would appear from this and other studies that carnosine has an important role as a physico-chemical buffer in equine middle gluteal muscle and that this is greatest in type IIB fibres, where it may account for up to 50% of physico-chemical buffering of H+ produced by muscle in the pH range 7.1-6.5.
J Physiol 1992 Sep
PMID:Estimation of the carnosine content of different fibre types in the middle gluteal muscle of the thoroughbred horse. 148 59

Do muscle fiber properties commonly associated with fiber types in adult animals and the population distribution of these properties require normal activation patterns to develop? To address this issue, the activity of an oxidative [succinic dehydrogenase (SDH)] and a glycolytic [alpha-glycerophosphate dehydrogenase (GPD)] marker enzyme, the characteristics of myosin adenosinetriphosphatase (myosin ATPase, alkaline preincubation), and the cross-sectional area of single fibers were studied. The soleus and medial gastrocnemius of normal adult cats were compared with cats that 6 mo earlier had been spinally transected at T12-T13 at 2 wk of age. In control cats, SDH activity was higher in dark than light ATPase fibers in the soleus and higher in light than dark ATPase fibers in the medial gastrocnemius. After transection, SDH activity was similar to control in both muscles. GPD activity appeared to be elevated in some fibers in each fiber type in both muscles after transection. The cross-sectional areas most affected by spinal transection were light ATPase fibers of the soleus and dark ATPase fibers of the medial gastrocnemius, the predominant fiber type in each muscle. These data demonstrate that although the muscle fibers of cats spinalized at 2 wk of age presumably were never exposed to normal levels of activation, the activity of an oxidative marker enzyme was maintained or elevated 6 mo after spinal transection. Furthermore, although the absolute enzyme activities in some fibers were elevated by transection, three functional protein systems commonly associated with fiber types, i.e., hydrolysis of ATP by myosin ATPase and glycolytic (GPD) and oxidative (SHD) metabolism, developed in a coordinated manner typical of normal adult muscles.
J Appl Physiol (1985) 1990 Sep
PMID:Enzyme profiles of single muscle fibers never exposed to normal neuromuscular activity. 170 Sep 75

Capillary supply, the proportion of oxidative fibres and blood flow were studied in fast rat muscles (tibialis anterior, TA, and extensor digitorum, EDL) made ischaemic by ligation of the common iliac artery, in chronically stimulated muscles and in ischaemic chronically stimulated muscles. Stimulation was carried out for 6 h/day at 10 Hz (three periods of 2 h with 90-120-min intervals between stimulations) for 10-12 days using electrodes implanted in the vicinity of the lateral popliteal nerve. Blood flow (measured by radioactive microspheres) was 3.62 +/- 0.52 ml.100 g-1.min-1 at rest and 78.4 +/- 14.6 ml.100 g-1.min-1 (mean +/- SEM) during isometric contractions at 4 Hz. Ischaemic muscles had significantly lower blood flow at rest as well as during contractions (72 +/- 14% and 25 +/- 4% of the values in contralateral muscles respectively). Stimulated muscles had significantly higher flow than contralateral control muscles during contractions; stimulated ischaemic muscles had normal blood flow at rest, but the increase in flow during contractions was limited to a similar extent to that in ischaemic muscles alone. Of all anatomically present capillaries (staining for alkaline phosphatase in frozen sections) the capillary/fibre ratio increased by 36% in stimulated tibialis anterior, but was not significantly different from control muscles in stimulated ischaemic TA and was even lower than in control muscles in stimulated ischaemic EDL. The proportion of fast oxidative fibres (estimated on the basis of histochemical staining for myosin ATPase and succinate dehydrogenase) increased from 53.2 +/- 3.2% in normal EDL to 82.0 +/- 2.3% in chronically stimulated EDL and to 100% in chronically stimulated ischaemic muscles.(ABSTRACT TRUNCATED AT 250 WORDS)
Pflugers Arch 1990 Sep
PMID:The role of blood flow and/or muscle hypoxia in capillary growth in chronically stimulated fast muscles. 170

To determine the effects of maternal exercise training during pregnancy on skeletal muscle metabolism of the progeny, eleven female Sprague-Dawley rats were divided into an exercise and a control group. The maternal training group (6) ran on a rodent treadmill for 4 weeks prior to pregnancy and daily throughout gestation (21 days) at 26.8 m/min, 1 hour/day, 5 days per week. The measurements were taken 28 days postpartum. No differences were noted between the sedentary and trained maternal animals for succinic dehydrogenase (SDH), phosphofructokinase (PFK), and myosin ATPase activities of the soleus, plantaris and gastrocnemius muscles. Maternal gastrocnemius SDH and soleus PFK levels were significantly (p less than 0.05) lower than levels found in the offspring. The liver glycogen of trained maternal animals was significantly higher than that found in all other groups. As well it was shown that maternal exercise had no effect on any of the aforementioned physiological parameters measured in the pups. The results indicate that exercise training during pregnancy does not modify the skeletal muscle metabolism of the offspring as observed 28 days after birth.
J Sports Med Phys Fitness 1991 Sep
PMID:Skeletal muscle metabolism in the offspring of trained rats. 179 11

The metabolic plasticity of single fibers in adult cat medial gastrocnemius (MG) 6 mo after complete spinal cord transection (Sp) at T12-T13 was studied. Some Sp cats were trained to weight support (Sp-WS) 30 min/day beginning 1 mo posttransection. Cross-sectional area, succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD), and myofibrillar adenosinetriphosphatase (ATPase) activities were determined in fibers identified in frozen serial sections. Fibers were categorized as light or dark based on myosin ATPase staining, alkaline preincubation. The percentage of dark ATPase fibers was higher in Sp and Sp-WS (approximately 85%) than in control (approximately 60%). All dark ATPase fibers reacted positively to a fast myosin heavy chain monoclonal antibody. In both spinal groups, a higher percentage of dark ATPase fibers reacted to both fast and slow myosin heavy chain antibodies than in controls. Neither Sp nor Sp-WS cats showed fiber atrophy. Compared with control, SDH activity was decreased in both fiber types of Sp cats. Daily weight-support training ameliorated this adaptation. There were no differences among the three groups in mean GPD and ATPase activities for either fiber type. There was a slight tendency, however, for spinal cats to have higher GPD and ATPase activities (independent of type) than control, probably reflecting the larger proportion of dark ATPase fibers in these cats. These observations indicate that 6 mo after spinalization in adult cats, some of the fibers of a fast muscle became "faster" and developed oxidative and glycolytic enzyme profiles that normally are exhibited in fast fatigable motor units.(ABSTRACT TRUNCATED AT 250 WORDS)
Am J Physiol 1990 Sep
PMID:Enzymatic plasticity of medial gastrocnemius fibers in the adult chronic spinal cat. 214 12

Postural muscles have many type I myofibers, which reacted strongly for acid-stable myosin ATPase and were unreactive for alkali-stable myosin ATPase (Ariano et al., J. Histochem. Cytochem., 21:51-55, 1973; Armstrong et al., Am. J. Anat., 163:87-98, 1982; Smith et al., J. Neurophysiol., 40:503-513, 1977). House shrews (Suncus murinus) keep abducting their limbs in locomotion and hardly lift their trunk off the ground. The limb muscles of Suncus were examined by histochemical methods to determine whether the locomotory and postural behavior is related to the proportion of type I myofibers. The observation of whole cross sections from the triceps surae, flexor digitorum superficialis, quadriceps femoris, and caudally situated muscles in the thigh showed that all myofibers of these muscles were unreactive for acid-stable myosin ATPase and strongly reactive for alkali-stable myosin ATPase: Those were classified as type II myofibers. Type II myofibers showed a weak (type IIB), moderate (type IIAB), or strong (type IIA) reaction for NADH tetrazolium reductase. Part of type IIA myofibers reacted weakly to moderately for menadione-linked glycerol-3-phosphate dehydrogenase (m-GPD), which predominated in the soleus muscle. Type IIAB, type IIB, and the remainder of type IIA myofibers reacted strongly for m-GPD. The limb muscles contained subtypes of type II myofibers but no type I myofibers. In Suncus murinus, type I myofibers specialized for a postural maintenance may not be required because all myofibers function exclusively for propulsion.
Anat Rec 1990 Sep
PMID:Composition of myofiber types in limb muscles of the house shrew (Suncus murinus): lack of type I myofibers. 214 5

Postoperative pulmonary complication and respiratory failure, frequently seen in undernourished patients such as those with esophageal cancer, were suspected to be due to respiratory muscle wasting caused by nutritional depletion. Based on this idea, the respiratory muscles obtained by biopsies during operation from diaphragm, external intercostal muscle, and rectus abdominis muscle were assessed histochemically in 32 patients. The specimens were stained for myosin ATPase to differentiate the types of muscle fibers, and then the size and distribution of the muscle fibers of each type were measured. In diaphragm muscle, cross-sectional areas of type 1 & 2 and the ratio of the area occupied by each fiber were usually the same; in external intercostal muscle, however, type 1 fibers were dominant and in rectus abdominis muscle, type 2 fibers were dominant. The cross-sectional area of each respiratory muscle fiber well correlated with certain anthropometrical indexes, and the nutritionally depleted cases, the muscle fibers were of a smaller size suggesting less respiratory muscle strength. The ratio of the area occupied by type 1 fibers in diaphragm muscle was linearly related to serum albumin, total cholesterol, and PNI (prognostic nutritional index). Type 2 fibers were dominant in malnourished patients, suggesting greater fatigue compared to well-nourished cases. Opposite findings were obtained in external intercostal muscle and rectus abdominis muscle, and the ratio of the area occupied by type 2 fibers was smaller in the undernourished cases, suggesting reduced maximum strength of these muscles.(ABSTRACT TRUNCATED AT 250 WORDS)
Nihon Kyobu Geka Gakkai Zasshi 1990 Sep
PMID:[Histochemical analysis of respiratory muscles of patients with esophageal cancer--with special reference to the preoperative nutritional state]. 214 8

The heptapeptide Ile-Arg-Ile-Cys-Arg-Lys-Gly-OEt is the analog of the S-site, one of the actin-binding sites in myosin [Suzuki et al. (1987) J. Biol. Chem. 262, 11410-11412]. Various substituted heptapeptides were synthesized, and the dissociation constants of each acto-heptapeptide complex was measured. Comparison of the dissociation constants indicated that the hydrophobic side chain of Ile-1 was critical for the binding with F-actin, but not that of Ile-3. The positive charge and the side chain length of Arg-2 were also important. The presence of a sulfur atom in the Cys-4 was also necessary. The affinity of the N-terminal Ile-Arg-Ile part for F-actin was influenced by the kind of residues in the C-terminal tetrapeptide part. Based on these results, the side chains of Ile(702), Arg(703), and Cys(SH1)(705) in myosin subfragment-1 heavy chain were assigned to be critical for the binding with F-actin. The amino acid sequence of S-1 heavy chain containing these critical residues for the S-site from residue number 700 to 717 can be predicted as an analogue of the segment B of the ATP-binding site [Walker et al. (1982) EMBO J. 1, 945-951]. The actin-binding S-site possibly shares a part of the ATP-binding site in myosin. We discuss the possibility that the S-site is an inhibitory site of myosin ATPase and the so-called actin-activation of myosin ATPase is a deinhibition induced by transient binding of F-actin to the S-site.
J Biochem 1990 Sep
PMID:Roles of the amino acid side chains in the actin-binding S-site of myosin heavy chain. 214 38


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