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)

Muscle biopsies for histochemical and ultrastructural analysis were obtained from seven critically ill patients admitted to the Intensive Care Unit of the "Domingo Luciani" Hospital, Caracas, Venezuela. The sample included two patients with sepsis of abdominal origin, and five that presented sepsis/MOFS, with renal, hepatic, and respiratory disturbances and muscular weakness. Sections were examined for myosin adenosine triphosphatase (ATPase) after pre-incubation with both acid buffer (pH 4.37 and 4.6) and alkaline buffer (pH 10.3), for reduced nicotinamide dinucleotide diaphorase (NADHd), and for alpha-glycerophosphate dehydrogenase (alpha-GPDH). Sections were stained with hematoxilin and eosin to look for pathological changes and examined with a transmission electron microscope. Skeletal muscle of patients in early stage of sepsis showed a normal aspect with light microscopy, but at the ultrastructural level some of the fibres showed atrophy and some capillaries looked altered. Patients with sepsis/MOFS exhibited an evident muscle disorder with oedema, infiltrate, atrophy and segmental necrosis. All fibre types showed decrease in diameter; specially fibre types IIA and IIB. Intramuscular capillaries were thickened and occluded, indexes of capillarity were slightly reduced, and fibre oxidative activity was decreased. At ultrastructural level fibres showed severe atrophy, contractile system disorganization and segmental necrosis. Capillaries were also altered and the mononuclear cell infiltrate was abundant and represented by macrophages, lymphocytes and mastocytes.
 ...
PMID:Histochemical and ultrastructural study of skeletal muscle in patients with sepsis and multiple organ failure syndrome (MOFS). 947 42

To better evaluate the role of a possible mitochondrial alteration in the pathogenesis of cleft lip, we obtained and examined 38 orbicularis oris muscle specimens taken from the cleft margin of both cleft and noncleft sides of 10 unilateral cleft lip infants at the time of primary closure. Part of each sample was frozen in liquid nitrogen/cooled isopentane, while the remainder was fixed in 2.5% glutaraldehyde, postfixed in osmium tetroxide, and embedded in Araldyte resin. Ten-micrometer-thick sections were obtained from the frozen samples and stained for histologic (Gomori trichrome) and histochemical (adenosine triphosphatase, nicotinamide adenine dinucleotide-tetrazolium reductase, cytochrome c-oxidase, succinate dehydrogenase) techniques. Ultra-thin sections (70 to 100 nm) of the resin-embedded specimens were stained with uranyl acetate and lead cytrate and were examined with a Zeiss 109 transmission electron microscope operating at 80 kV. Muscular fiber-type ratio was found to be 19.2 percent type 1 and 80.8 percent type 2 fibers on the cleft side and 26.3 percent type 1 and 73.7 percent type 2 fibers on the noncleft side. We detected aspecific structural alterations, such as variations in the fiber size without fiber group atrophy or fiber-type grouping with the ATPase reaction, in all biopsies. Although Gomori trichrome revealed a dark staining and red granularity of the fibers, suggesting an increase in mitochondria activity, no ragged-red fibers or cytochrome c-oxidase-negative/succinate dehydrogenase-positive fibers were found. At the ultrastructural level, the mitochondrial morphology was always preserved, without inclusions or variations in size and/or shape. On the other hand, we invariably noticed an increase of the number of mitochondria, associated with abnormal glycogen deposits, in some areas of every specimen. Both of these two latter findings were regularly localized at the periphery of the sarcolemma, resembling the so-called lobulated fibers, an aspecific sign of muscular flogosis. Our findings, although excluding an inherent metabolic myopathy of orbicularis oris muscle in unilateral cleft lip patients, evinced both an increased oxidative metabolism and a generic inflammatory condition of that muscle, the nature of which must still be defined.
 ...
PMID:Mitochondrial activity of orbicularis oris muscle in unilateral cleft lip patients. 973 10

The diagnosis of nemaline rod myopathy (NM) is based on the presence of numerous pathognomonic rods within a fresh frozen muscle biopsy specimen. Three forms of congenital NM have been described in humans, and rods have been found to occur in various other conditions. A similar myopathy was described in 1986 in a family of cats. In this report, we describe a case of congenital NM in a 10-month-old Border Collie, an adult-onset NM in an 11-year-old Schipperke, and 2 acquired myopathies with nemaline rods in adult dogs associated with hypothyroidism and Cushing's syndrome. Common clinical features included exercise intolerance, abnormal electromyography, and the presence of nemaline rods in fresh, frozen, and glutaraldehyde-fixed biopsies from proximal appendicular limb muscles. Staining of cryostat sections of muscle biopsy specimens by the modified Gomori trichrome technique disclosed numerous rod bodies that were localized to type 1 fibers by the histochemical adenosine triphosphatase reaction. Accumulation of rods also was demonstrated by electron microscopy in 2 of the cases with localized enlargement and streaming of Z lines. Documentation of NM in a young Border Collie and the adult-onset form in the Schipperke alerts clinicians to the existence of this disorder in these breeds.
 ...
PMID:Nemaline rods in canine myopathies: 4 case reports and literature review. 985 34

We investigated the changes of muscle proteins in acute quadriplegic myopathy (AQM) using immunohistochemistry and stoichiometry. Cases of AQM were observed in which it was difficult to type muscle fibers with adenosine triphosphatase staining in biopsied muscle. Well-defined typing of these cases was possible by performing immunofluorescent staining using slow and fast skeletal troponin I (TnI) antibodies. By this means, small angular fibers were shown to be fast skeletal muscle, and myosin was absent from these muscle fibers. Actin and tropomyosin were maintained. Muscle protein ratios were determined by stoichiometry following sodium dodecyl sulfate-polyacrylamide gel electrophoresis of AQM myofibril specimens from four subjects. The myosin heavy chain/actin ratio was significantly decreased compared with a normal control group and other neuromuscular diseases. These pathologic findings returned to normal during recovery from AQM. Thus, myosin selectively decreases, whereas actin and regulatory proteins located above it are maintained during AQM.
 ...
PMID:Analysis of muscle proteins in acute quadriplegic myopathy. 1091 67

Numerous muscular dystrophies, such as dystrophinopathies, sarcoglycanopathies, and emerino- and laminopathies, are marked by the absence or reduction of mutant transsarcolemmal or nuclear proteins. In addition to these recently identified minus-proteinopathies, there are a growing number of plus-proteinopathies among neuromuscular disorders marked by a surplus or excess of endogenous proteins within muscle fibers of different, i.e., nontranssarcolemmal and nonnuclear types. These proteins are often filamentous; for example, desmin and actin accrue in respective desmin-related myopathies, among which are entities marked by mutant desmin, true desminopathies, and actinopathy, the latter often seen as a subgroup in nemaline myopathies. Desmin-related myopathies consist largely of those marked by desmin-containing inclusions and those characterized by desmin-containing granulofilamentous material. When mutations in the desmin gene can be identified, the mutant desmin is thought to form the major myopathological lesion. Together with desmin, other proteins often accumulate. The spectrum of these proteins is quite diverse and encompasses such proteins as dystrophin, nestin, vimentin, alphaB-crystallin, ubiquitin, amyloid precursor protein, and beta-amyloid epitopes, as well as gelsolin and alpha(1)-antichymotrypsin. Among these associated proteins, one, alphaB-crystallin, has been found mutant in one large family, justifying the term alphaB-crystallinopathy as a separate condition among the desmin-related myopathies. Other proteins accruing with desmin have not yet been identified as mutant in desmin-related myopathies. Mutations in the desmin gene entail missense mutations and small deletions. The formation of mutant actin may lead to aggregates of actin filaments which may or may not be associated with formation of sarcoplasmic and/or intranuclear nemaline bodies. A considerable number of missense mutations in the sarcomeric actin gene ACTA1 have been discovered in patients with nemaline myopathy and also in a few patients without myopathological evidence of nemaline bodies in biopsied skeletal muscle fibres. Apart from alphaB-crystallin, no other proteins coaggregating with actin in actin filament aggregates of actinopathy or the actin mutation type of nemaline myopathy have so far been identified. Two further candidates for protein surplus myopathies are hyaline body myopathy, which is marked by accumulation of granular nonfilamentous material within muscle fibers that is rich in myosin and adenosine triphosphatase activities, and hereditary inclusion body myopathies, which are marked by accumulation of tubulofilaments similar to the helical filaments of Alzheimer neurofibrillary tangles. These tubulofilaments consist of diverse proteins as well, though no mutant protein has yet been discovered. So far, no genes responsible for familial hyaline body and hereditary inclusion body myopathies have been identified. The discovery of mutant proteins, desmin, alphaB-crystallin, and actin, as components of surplus or excess proteins accumulating in muscle fibers in certain neuromuscular conditions is responsible for the recent emergence of this new concept of gene-related protein surplus myopathies.
 ...
PMID:Gene-related protein surplus myopathies. 1100 21

A 22-year-old man developed unconsciousness, severe quadriplegia and muscle atrophy, and had markedly elevated serum creatine kinase levels after using the high-dose steroid and nondepolarizing neuromuscular blocking agents during the course of sepsis and DIC. On neurological examination, he was lethargic. The patient had generalized muscle weakness and wasting, and diminished deep tendon reflexes. He weakly responsed to painful stimuli on the legs. The motor nerve conduction study demonstrated decreased CMAP (compound muscle action potential) amplitudes. Motor and sensory nerve conduction velocities and their distal latencies were normal. Muscle biopsy revealed marked muscle fiber atrophy predominantly in type 2 fibers and numerous basophilic and a few necrotic fibers. Some atrophic fibers had decreased to absent myosin adenosine triphosphatase activity in their center. Accordingly, he was diagnosed as having acute quadriplegic myopathy (AQM), which has been reported mainly in Western countries. The mechanism of muscle fiber degradation in this myopathy is still unknown. On immunohistochemical analysis to our patient, enzyme activities of various proteases such as calpain, cathepsin B, and proteasomes were increased in the sarcoplasm, especially in the atrophic fibers. We suggest that lysosomal cathepsin, nonlysosomal calpain, and ATP-ubiquitin-proteasome proteolytic pathways participate in muscle fiber degradation in AQM.
 ...
PMID:[A case of acute quadriplegic myopathy]. 1108 98

Proximal (vastus lateralis) and distal (gastrocnemius) muscles of 100-day-old normal and myopathic BIO TO-2 hamsters were analysed to study the effects of myopathy on the different muscle fibre types: SO (slow oxidative), FOG (fast oxidative glycolytic) and FG (fast glycolytic). Cytophotometric measurements of enzyme activities (myofibrillic adenosine triphosphatase, succinate dehydrogenase and glycerol-3-phosphate dehydrogenase), Western blot analysis of nitric oxide synthase (NOS) I, II, III isoforms and NOS II immunohistochemistry were performed. The following alterations were found in myopathic muscle fibres: all fibre types of both proximal and distal myopathic muscles showed decreased myofibrillic adenosine triphosphatase activity indicating depressed contractility. This was associated with depressed oxidative activity of the muscle fibres. A shift to more glycolytic metabolism was observed, mainly in FG fibres of proximal muscle. We found an increased NOS II expression in both myopathic muscle types investigated. It means that increased NO production inhibits force generation in myopathic muscle. NOS II immunoreactivity was found mainly in the cytoplasm of FG fibres. NOS I and NOS III expression was not significantly effected by this form of myopathy. Our findings demonstrate that muscle fibres of proximal and distal skeletal muscles of 100-day-old cardiomyopathic BIO TO-2 hamsters are altered with respect to contractility, metabolism and NOS II expression. FG fibres of the proximal muscle were effected most strongly.
 ...
PMID:Myopathy-dependent changes in activity of ATPase, SDH and GPDH and NOS expression in the different fibre types of hamster muscles. 1199 46

Myoclonus epilepsy with ragged red fibers (MERRF) is one of the major mitochondrial encephalomyopathies. Its main clinical features are myoclonus epilepsy, ataxia, and myopathy with ragged red fibers. Whereas there is a close correlation between MERRF syndrome and the A8344G mutation of mitochondrial DNA, the reverse is not true. In fact, this mutation is also responsible for various other syndromes, such as Leigh syndrome, spinocerebellar degeneration, atypical Charcot-Marie-Tooth disease, and multiple truncal lipomas. We describe a child with the A8344G mutation of mitochondrial DNA and an unusual clinical, neuroradiologic, and biochemical phenotype, characterized by early-onset, nonprogressive cerebellar ataxia, and subclinical myoclonias in association with bilateral putaminal necrosis on magnetic resonance imaging and a reduction in complex V activity. Our case confirms the existence of a relationship between alteration in adenosine triphosphatase activity and basal ganglia involvement. We recommend that the possibility of a mitochondrial pathology should always be taken into consideration in the presence of bilateral symmetric lesions of the basal ganglia, even when the typical clinical picture is lacking. (J Child Neurol 2006;21:79-82).
 ...
PMID:Bilateral putaminal necrosis associated with the mitochondrial DNA A8344G myoclonus epilepsy with ragged red fibers (MERRF) mutation: an infantile case. 1655 60

The morphological changes in deep pectoral myopathy of broilers have been studied by light- and electron-microscopy and histochemistry from 15 min to 15 months after its experimental induction. Oedema, mild alterations in some organelles and loss of glycogen were present throughout the supracoracoid muscle within 15 min but its anterior region quickly returned to normal. After 1 hour there were ultrastructural indications of the onset of permanent damage to the muscle and its associated vasculature and by 24 hours there was histological and ultrastructural evidence of ischaemic necrosis and glucan phosphorylase and myosin adenosine triphosphatase were reduced. By 3 days phagocytosis was established at the edge of the ischaemic, necrotic muscle and by 9 days there was capsule formation and active muscle regeneration in this location. Grossly the muscle now had the green periphery and pink interior characteristic of the naturally-occurring myopathy and it subsequently became of drier consistency. At the 3rd week atrophic muscle fibres were seen in the caudal region and by the 6th week this part had become an attenuated band of fibro-adipose tissue containing sparse groups of atrophic muscle fibres. There were morphological indications of reduced numbers of nerve fibres in this region. By the 6th month the atrophic region was unchanged and phagocytosis and overall regeneration had become quiescent. Thus, although regeneration was initially active, the extensive destruction in experimental myopathy was never completely replaced by new muscle.
 ...
PMID:The sequence of pathological events in deep pectoral myopathy of broilers. 1877 Jan 23

Mutations in valosin-containing protein (VCP) cause inclusion body myopathy (IBM), Paget's disease of the bone, and frontotemporal dementia (IBMPFD). Patient muscle has degenerating fibers, rimmed vacuoles (RVs), and sarcoplasmic inclusions containing ubiquitin and TDP-43 (TARDNA-binding protein 43). In this study, we find that IBMPFD muscle also accumulates autophagosome-associated proteins, Map1-LC3 (LC3), and p62/sequestosome, which localize to RVs. To test whether VCP participates in autophagy, we silenced VCP or expressed adenosine triphosphatase-inactive VCP. Under basal conditions, loss of VCP activity results in autophagosome accumulation. After autophagic induction, these autophagosomes fail to mature into autolysosomes and degrade LC3. Similarly, IBMPFD mutant VCP expression in cells and animals leads to the accumulation of nondegradative autophagosomes that coalesce at RVs and fail to degrade aggregated proteins. Interestingly, TDP-43 accumulates in the cytosol upon autophagic inhibition, similar to that seen after IBMPFD mutant expression. These data implicate VCP in autophagy and suggest that impaired autophagy explains the pathology seen in IBMPFD muscle, including TDP-43 accumulation.
 ...
PMID:Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease. 2000 65


<< Previous 1 2 3 Next >>