acid-phosphatase and Muscular-Atrophy

Topics: Acid Phosphatase; Amino Acid Metabolism, Inborn Errors; Amniotic Fluid; Anemia, Hemolytic, Congenital Nonspherocytic; Anemia, Sickle Cell; Carbohydrate Metabolism, Inborn Errors; Cells, Cultured; Female; Glycolipids; Glycosaminoglycans; Heterozygote; Humans; Lipid Metabolism, Inborn Errors; Lipidoses; Metabolism, Inborn Errors; Muscular Atrophy; Pregnancy; Prenatal Diagnosis; Purine-Pyrimidine Metabolism, Inborn Errors; Transferases; Xanthomatosis

The present study was performed to investigate the influence of unloading on the regeneration of atrophied and injured skeletal muscle.. Male mice (C57BL/6J), aged 8 weeks, were used. Cardiotoxin (CTX) was injected into soleus muscles bilaterally. Gravitational unloading on soleus muscle was performed by hind limb suspension for 2 weeks before and additionally 6 weeks after CTX injection in one group. Soleus muscles in the remaining groups were loaded keeping the mice in the cages and were dissected 14, 28 and 42 days after the injection.. Recovery of the wet weight and protein content of soleus in the CTX-injected group was inhibited by unloading. Increase in satellite cell number, induced by CTX injection and loading, was also inhibited by unloading. Disappearance of infiltration of mononucleated cells into the necrotic area was also delayed. This phenomenon suggests that regeneration, which is indicated by the appearance of fibres with central nuclei, was inhibited by unloading.. Results suggested that loading plays an important role in the activation of the regenerating potential of injured skeletal muscle.

Topics: Acid Phosphatase; Animals; Body Weight; Cardiotoxins; Cell Count; Cell Movement; Cell Nucleus; Hindlimb Suspension; Male; Mice; Mice, Inbred C57BL; Muscle Fibers, Skeletal; Muscle Proteins; Muscle, Skeletal; Muscular Atrophy; Organ Size; PAX7 Transcription Factor; Phagocytes; Regeneration; Satellite Cells, Skeletal Muscle; Weight-Bearing

Age-associated muscle wasting (sarcopenia of old age) is a major problem in elderly people, however, the mechanisms of muscle proteolysis in aging remain obscure and enigmatic. Possible reasons for loss of skeletal muscle mass with aging may be attributed to multiple and complex proteolytic systems. The purpose of the present study was to explore the kinetics of activation of extracellular hydrolytic and proteolytic systems in muscles of hindlimbs immobilized by external fixation of 24-month-old female Wistar rats, in comparison with those of 6-month-old rats. Results show that elevated acid phosphatase activities (lysosomal hydrolytic enzyme activated mainly in macrophages) in immobilized limb muscles of young animals, differ from old animals. In young rats external fixation resulted in significantly elevated acid phosphatase activities (50-55%; p<0.05) after 4 weeks of immobilization, whereas in old animals similar increases were observed already during the first and second weeks of immobilization. The extracellular proteolytic enzymes, matrix metalloproteinases (MMP-2 and -9), were also differentially activated in old animals compared to young animals. In young animals, as shown in previous studies, both MMP-2 and -9 activities were elevated significantly in immobilized muscles. In this study of old animals, only MMP-2 activity was detected, with no significant elevation in the immobilized muscles of old animals. In addition, the levels of the transcription factor Nuclear Factor-kappaB (NF-kappaB) in nuclear extracts of old rat muscles, as detected by ELISA, showed a biphasic pattern after immobilization, suggesting that NF-kappaB could be activated by different processes in the atrophy process, at least in the old age. In conclusion, it seems that the kinetics of activation of extracellular hydrolytic and proteolytic systems differ in muscles of old animals compared to young animals.

Topics: Acid Phosphatase; Aging; Animals; Densitometry; Enzyme-Linked Immunosorbent Assay; Female; Hindlimb Suspension; Immunohistochemistry; Macrophages; Matrix Metalloproteinase 2; Matrix Metalloproteinase 9; Metalloproteases; Muscle, Skeletal; Muscles; Muscular Atrophy; NF-kappa B; Rats; Rats, Wistar; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Time Factors; Transcription Factor RelA

The purpose of this report was to study the effects of four weeks of hindlimb immobilization on acid phosphatase activity of old rats in comparison with the profile obtained after similar treatment in young rats.

Topics: Acid Phosphatase; Aging; Animals; Female; Immobilization; Muscles; Muscular Atrophy; Proteins; Rats; Rats, Wistar; Signal Transduction; Time Factors

The effects of beta adrenergic agonists, clenbuterol (2 mg/kg body weight/d) and isoproterenol (12 mg/kg body weight/d), in normal innervated and denervated rat gastrocnemius muscle were investigated. The daily administration of beta adrenergic agonists to normal innervated rats for a short period (7 d) resulted in the hypertrophy of gastrocnemius as confirmed from the measurement of total tissue protein contents. The development of denervation atrophy witnessed a stimulation in the expression of acid and alkaline phosphatases, pointing to an enhanced myofibrillar degeneration. An administration of beta adrenergic agonists inhibited the expression of raised levels of these enzymes in denervated muscle. A measurement of 3-methylhistidine in muscle revealed a loss of amino acid with the progress in the development of denervation atrophy. Serum and urine samples from denervated rats showed a progressive accumulation of 3-methylhistidine. Clenbuterol and isoproterenol treatment to these rats resulted in an inhibition of 3-methylhistidine accumulation. When 3-methylhistidine was used as a marker of myofibrillar degeneration, the results seemed to suggest that the degeneration of cyto-contractile apparatus accompanying denervation atrophy is attenuated in the presence of beta adrenergic agonists, implying that these sympathomimetic drugs are capable of reversing denervation atrophy in rat gastrocnemius.

Topics: Acid Phosphatase; Adrenergic beta-Agonists; Alkaline Phosphatase; Amino Acids; Animals; Biomarkers; Clenbuterol; Isoproterenol; Male; Methylhistidines; Muscle Denervation; Muscle Proteins; Muscle, Skeletal; Muscular Atrophy; Myofibrils; Rats; Rats, Wistar

Clinical and morphological features have been studied in 11 late onset Acid Maltase Deficient (AMD) patients. All patients have been diagnosed on biochemical evidence of acid maltase deficiency on muscle biopsy. Molecular studies showed a heterozygous mutation (IVS1-13 T > G transversion resulting in aberrant splicing) in the GSDII gene, which is the most common mutation in late onset AMD patients. Morphological features in muscle biopsy showed a vacuolar myopathy and Golgi apparatus proliferation within fibres. The peripheral areas of autophagic vacuoles were positive for caveolin-3 and dystrophin, documenting an extensive membrane turnover. The ultrastructural study of muscle biopsy showed randomly distributed or isolated vesicles sometimes derived from the Golgi apparatus. In subsarcolemmal region, lipofucsin bodies and abnormal mitochondria with crystalline inclusions were observed. Primary and secondary lysosomes were typically filled with glycogen. These data suggest a predominant role of Golgi in vesicle proliferation and extensive intra-fibral membrane remodelling. The pathological changes observed are selective for muscle fibres (mostly in type 1) and for muscle groups (mainly proximal). An attractive hypothesis for the variability of clinical phenotype in adult and infantile onset AMD patients is that in the former, an aberrant transcript of smaller size may have originated from alternative splicing (exon 2 skipping). A residual enzyme activity is detectable in muscle, but the intracellular processing of the enzyme precursor from Golgi to the mature form in lysosomes might be blocked.

Topics: Acid Phosphatase; Adult; Age of Onset; Aged; Alternative Splicing; Biomarkers; Female; Genetic Predisposition to Disease; Glucan 1,4-alpha-Glucosidase; Glycogen; Golgi Apparatus; Heterozygote; Humans; Immunohistochemistry; Lysosomes; Male; Microscopy, Electron; Middle Aged; Mitochondria, Muscle; Muscle Fibers, Skeletal; Muscle, Skeletal; Muscular Atrophy; Mutation; Sarcolemma; Time Factors; Vacuoles

We have examined muscle strength, mitochondrial enzyme activity, histochemistry and fibre size in the quadriceps muscle of 9 patients with severe chronic heart failure. A needle biopsy of the quadriceps muscle was taken with patients at rest. Maximum oxygen uptake was measured during treadmill exercise. Mean maximal oxygen consumption was 11.7 ml.kg-1.min-1. Isometric maximum voluntary contraction was reduced to 55% of the predicted value for weight. Eight biopsies were abnormal. Findings included increased acid phosphatase, increased interstitial cellularity, excess intracellular lipid accumulation, atrophy of both type I and II fibres and variation in size with hypertrophy and atrophy of fibers. Muscle fibre capillary density and the activity of mitochondrial enzymes were normal. Changes in skeletal muscle strength may play a role in the limitation of exercise capacity seen in patients with congestive heart failure.

Topics: Acid Phosphatase; Aged; Biopsy; Electron Transport Complex IV; Heart Failure; Humans; Lipid Metabolism; Male; Middle Aged; Mitochondria, Muscle; Muscle Contraction; Muscles; Muscular Atrophy; Oxidoreductases; Oxygen Consumption; Succinate Cytochrome c Oxidoreductase

On the basis of previous (n = 23) and current muscle biopsies (n = 25) as well as five animal-experimental investigations, the paper deals with the cause and the manifestation of perifascicular muscle-fiber atrophy. A deteriorated trophic situation of the subfascial or marginal muscle fibers in patients suffering from immunocomplex vasculopathies in connection with a reduced supply of blood to the muscles is seen as the cause of the areactive weight loss (atrophy). This is accompanied by a considerably reduced capillary supply of blood to the muscle fibers. Even in normal conditions, the portion of collateral vessels and capillaries is lower in the subfascial region than in the center of the fascicle. When the blood supply is disturbed, the marginal fibers are in a trophic situation worse than that of the central muscle fibers. They become atrophied. In responsive patients, the muscle fibers regenerate and recapillarize during the convalescence period. This can be shown histochemically by means of the alkaline phosphatase reaction. The extent of perifascicular musclefiber atrophy can be fixed in quantitative terms by the method of Baumli and Mumenthaler. Where a second biopsy is indicated, results can be obtained regarding the changes in the perifascicular atrophy as a consequence of the therapy provided.

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Animals; Basement Membrane; Biopsy; Capillaries; Child; Dermatomyositis; Female; Fluorescent Antibody Technique; Humans; Immune Complex Diseases; Immunoglobulins; Ischemia; Male; Middle Aged; Muscle, Smooth, Vascular; Muscles; Muscular Atrophy; Muscular Dystrophies; Myositis; Rats; Rats, Inbred Strains

The loss of muscle weight in the soleus (SOL) and extensor digitorum longus (EDL) muscles was compared after denervation and in the course of reflex muscle atrophy induced by unilateral fracture of metatarsal bones of the paw and local injection of 0.02 ml turpentine oil subcutaneously. This so-called reflex atrophy is significantly greater after 3 days than that after denervation. Seven days after the nociceptive stimulus, reflex and denervation atrophy are grossly similar in both muscles. This also applies in case that the nociceptive stimulus had been repeated on the third day. The EDL:SOL enzyme activities of energy supply metabolism reflect the differences between a glycolytic-aerobic (EDL) and predominantly aerobic type (SOL) of muscle. No consistent changes were found in either type of atrophy after 3 days. In 7 days' denervation, the activity of hydroxyacetyl-CoA-dehydrogenase (HOADH) and citrate synthase (CS) was decreased in the SOL, while glycerolphosphate:NAD dehydrogenase (GPDH) was enhanced. In the EDL, the activity of triosephosphate dehydrogenase (TPDH), GPDH, malate dehydrogenase (MDH), CS and HOADH was decreased. Acid phosphatase (AcP) was greatly increased in both muscles. Seven days after application of the nociceptive stimulus, all enzyme activities were altered in a grossly analogous manner as after denervation.

Topics: 3-Hydroxyacyl CoA Dehydrogenases; Acid Phosphatase; Animals; Citrate (si)-Synthase; Denervation; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycerolphosphate Dehydrogenase; Hexokinase; Malate Dehydrogenase; Male; Muscles; Muscular Atrophy; Rats

Modern morphological diagnostic methods for neuromuscular diseases are based on enzyme histological and electron microscopic techniques. By enzyme histochemical differentiation of fiber types, early morphological changes such as Type I atrophy in myotonic dystrophy, or particular disease forms like Type II atrophy or congenital fiber type disproportion and other congenital myopathies associated with a Type I atrophy may be detected. The ultrastructural characteristics and the fine structure of autofluorescent lipopigments rich in phosphatases in the skeletal muscle fiber permit appropriate diagnosis of the individual types of congenital myopathy or neuronal ceroid lipofuscinosis.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adolescent; Biopsy; Child; Child, Preschool; Female; Humans; Infant; Male; Middle Aged; Muscles; Muscular Atrophy; Muscular Dystrophies; Neuromuscular Diseases; Specimen Handling

The average diameter of the different enzymatic types of extra- and intrafusal muscle fibres is determined by means of a one millimeter scale ocular micrometer in the gastrocnemius muscle of twenty four female rats during three months, at regular intervals following tenotomy. There is a predominant atrophy of the type II extrafusal as well as intrafusal fibres in the period of immobilization. However, when the muscle becomes functional again, by healing and elongation of the tendon, the intrafusal type II fibres remain atrophic in contrast to the extrafusal ones, which regain their normal size.

Topics: Achilles Tendon; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Cholinesterases; Esterases; Female; Hindlimb; L-Lactate Dehydrogenase; Muscle Spindles; Muscles; Muscular Atrophy; Nucleotidases; Postoperative Complications; Rats; Succinate Dehydrogenase; Wound Healing

Non-specific esterase, acid phosphotase, beta-glucoronidase, and N-acetyl-beta-glucosamindase were revealed using the histochemical method of asocombinations in biopsy specimens of the muscular tissue taken from 99 patients suffering from neurogenic and myogenic disorders. Biopsy specimens were taken also from 7 healthy persons. Concentrations of the granular product of the reaction correlated with autofluorescence in the same section. Some bioptic materials were investigated using electron-microscopy. It was established that activity of lysosomal hydrolases in the normal muscular tissue was low, being increased with age. Autofluorescence in the majority of cases was well noticible. In the groups of atrophic fibres in neurogenic atrophy there were observed focal elevation of the lysosomal enzymatic activity. Product of the reaction, which pointed to the activity of nonspecific esterase and acid phosphotase, was localized predominantly along the periphery of muscular fibres. Autofluorescence of the product of the reaction was considerable. On the other hand, there were extensive areas of muscular fibres in which the concentration of the reaction product did not exceed the normal level. Activity of hydrolases in cells of the mesenchyma was of a low degree. Ist type of the lysosomal activity was observed in myogenic dystrophy with an acute course of the disease; it was characterized by structural changes in the muscular tissue, activation of the all hydrolases under study, absence of autofluorescence on the areas of localization of the reaction product, participation of the mesenchyma cells in the lysosomal activation. IInd type of the lysosomal activity was noted in the muscular tissue in neurogenic atrophy. There was no difference in principle between neuro- and myogenic lesions as far as the type of lysosomal activity is concerned. Collation of the results obtained in the investigations with the data reported in available literature enabled the authors to put forward the concept of the two types of the lysosomal activity in muscular lesions: 1) diffuse elevation of the lysosome activity associated with structural changes in the muscular tissue; 2) focal elevation of the physiological activity due to formation of lipopigment.

Topics: Acetylglucosaminidase; Acid Phosphatase; Adolescent; Adult; Biopsy; Child; Child, Preschool; Clinical Enzyme Tests; Esterases; Glucuronidase; Humans; Hydrolases; Infant; Lysosomes; Microscopy, Electron; Middle Aged; Muscular Atrophy; Muscular Dystrophies; Neurologic Manifestations

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; Alkaline Phosphatase; Amyotrophic Lateral Sclerosis; Biopsy; Child, Preschool; Dihydrolipoamide Dehydrogenase; Esterases; Glucosyltransferases; Glucuronidase; Glycerolphosphate Dehydrogenase; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Muscle Denervation; Muscles; Muscular Atrophy; Muscular Dystrophies; Myositis; Myotonic Dystrophy; NAD; Neuromuscular Diseases; Succinate Dehydrogenase

Topics: Acid Phosphatase; Biopsy; Child; Glucosidases; Glucosyltransferases; Glucuronidase; Glycogen; Glycogen Storage Disease; Hexosaminidases; Histocytochemistry; Humans; Intellectual Disability; Male; Microscopy; Microscopy, Electron; Muscles; Muscular Atrophy; Muscular Diseases

Topics: Acid Phosphatase; Adult; Age Factors; Autopsy; Brain Chemistry; Chronic Disease; Electroencephalography; Epilepsy, Tonic-Clonic; Fatty Acids; Gaucher Disease; Glomerulonephritis; Hepatomegaly; Histocompatibility; Humans; Hypertension, Renal; Immunosuppressive Agents; Kyphosis; Liver; Male; Muscular Atrophy; Nephrectomy; Pneumonia; Radionuclide Imaging; Sphingolipids; Spleen; Transplantation, Homologous

Topics: Acetates; Acid Phosphatase; Animals; Freezing; Galactosidases; Glucosidases; Glycoside Hydrolases; Hexosaminidases; Histocytochemistry; Hydrolases; Hypotonic Solutions; Lysosomes; Male; Mitochondria, Muscle; Muscles; Muscular Atrophy; Muscular Dystrophies; Rats; Sulfatases; Surface-Active Agents; Time Factors

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Adult; Alkaline Phosphatase; Esterases; Glucosyltransferases; Histocytochemistry; Humans; Magnesium; Male; Middle Aged; Monoamine Oxidase; Muscular Atrophy; Myofibrils; Neurons; Nucleotidases; Oxidoreductases; Phosphotransferases; Spinal Cord

Topics: Acid Phosphatase; Animals; Cathepsins; Centrifugation, Density Gradient; Glucuronidase; Lysosomes; Male; Mitochondria, Muscle; Muscle Denervation; Muscles; Muscular Atrophy; Rats; Ribonucleases; Sulfatases; Surface-Active Agents

Topics: Acid Phosphatase; Adult; Alcohol Oxidoreductases; Child; Electrophoresis; Esterases; Glucuronidase; Glycerolphosphate Dehydrogenase; Humans; Hydroxybutyrate Dehydrogenase; L-Lactate Dehydrogenase; Malate Dehydrogenase; Male; Muscular Atrophy; Muscular Diseases; Muscular Dystrophies; Oxidoreductases

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Amyotrophic Lateral Sclerosis; Animals; Cholinesterases; Electron Transport Complex IV; Glucosyltransferases; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Muscular Atrophy; Muscular Diseases; Muscular Dystrophies; Myasthenia Gravis; Neuromuscular Junction; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Birds; Esterases; Fats; Glucosephosphate Dehydrogenase; Glucosyltransferases; Glycolysis; Lipase; Male; Muscle Denervation; Muscles; Muscular Atrophy; Oxygen; Pectoralis Muscles; Phosphogluconate Dehydrogenase; Succinate Dehydrogenase