acid-phosphatase and Muscular-Diseases

Topics: Acid Phosphatase; Alkaline Phosphatase; Aspartate Aminotransferases; Biliary Tract Diseases; Cardiovascular Diseases; Clinical Enzyme Tests; Creatine Kinase; Esterases; Glucosephosphate Dehydrogenase; Humans; Isoenzymes; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Muscular Diseases; Neoplasms; Skin Diseases

Topics: Acid Phosphatase; Alkaline Phosphatase; Aspartate Aminotransferases; Biliary Tract Diseases; Cardiovascular Diseases; Clinical Enzyme Tests; Creatine Kinase; Esterases; Glucosephosphate Dehydrogenase; Humans; Isoenzymes; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Muscular Diseases; Neoplasms; Skin Diseases

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Clinical Enzyme Tests; Fructose-Bisphosphate Aldolase; Glucosyltransferases; Histocytochemistry; Humans; Isoenzymes; L-Lactate Dehydrogenase; Microscopy, Electron; Mitochondria, Muscle; Muscle Spindles; Muscles; Muscular Diseases; Nucleotidases; Succinate Dehydrogenase

Many studies have demonstrated an increase in reactive oxygen species (ROS) and oxidative damage markers after muscle damage. Phonophoresis aims to achieve therapeutically relevant concentrations of the transdermally introduced drug in the tissues subjected to the procedure by the use ultrasound waves. The aim of the study was to evaluate the effects on the therapeutic pulsed ultrasound (TPU) together with gel-dimethylsulfoxide (DMSO) in the parameters of muscular damage and oxidative stress. Male Wistar rats were divided randomly into six groups (n=6): sham (uninjured muscle); muscle injury without treatment; muscle injury and treatment with gel-saline (0.9%); muscle injury and treatment with gel-DMSO (15mg/kg); muscle injury and TPU plus gel-saline; and muscle injury and TPU plus gel-DMSO. Gastrocnemius injury was induced by a single impact blunt trauma. TPU (6min duration, frequency of 1.0MHz, intensity of 0.8W/cm(2)) was used 2, 12, 24, 48, 72, 96 and 120h after muscle trauma. The CK and acid phosphatase activity in serum was used as an indicator of skeletal muscle injury. Superoxide anion, TBARS, protein carbonyls, superoxide dismutase (SOD) and catalase (CAT) activity was used as indicators of stress oxidative. Results showed that TPU and gel-DMSO improved muscle healing. Moreover, superoxide anion production, TBARS level and protein carbonyls levels, superoxide dismutase (SOD) and catalase (CAT) activity were all decreased in the group TPU plus gel-DMSO. Our results show that DMSO is effective in the reduction of the muscular lesion and in the oxidative stress after mechanical trauma only when used with TPU. (E-mail: silveira_paulo2004@yahoo.com.br).

Topics: Acid Phosphatase; Analysis of Variance; Animals; Catalase; Creatine Kinase; Dimethyl Sulfoxide; Male; Muscle, Skeletal; Muscular Diseases; Oxidative Stress; Phonophoresis; Protein Carbonylation; Rats; Rats, Wistar; Superoxide Dismutase; Superoxides; Thiobarbituric Acid Reactive Substances; Treatment Outcome; Ultrasonic Therapy

Long-term administration of chloroquine to rats induces a vacuolar myopathy, which is specifically termed chloroquine myopathy (CM). In CM, tau mRNA levels were transiently upregulated in the early phase, while tau itself slowly accumulated in the late phase. The temporal profiles of tau mRNA levels and its accumulation were very similar to those of beta-amyloid protein precursor (APP) and its carboxyl-terminal fragments, both of which have been known to be degraded in lysosomes. Immunocytochemistry showed that tau progressively accumulated in the rimmed vacuoles exhibiting increased acid phosphatase activities, and immunoelectron microscopy demonstrated that tau was located within autophagic vacuoles. These results suggest that the accumulation of tau in CM is due to defective tau degradation in the lysosomal compartment in the muscle.

Topics: Acid Phosphatase; Amyloid beta-Protein Precursor; Animals; Autophagy; Chloroquine; Gene Expression Regulation; Immunohistochemistry; Lysosomes; Male; Microscopy, Immunoelectron; Muscle, Skeletal; Muscular Diseases; Polymerase Chain Reaction; Rats; Rats, Wistar; RNA, Messenger; tau Proteins; Transcription, Genetic; Vacuoles

Congenital muscular dystrophy syndromes are characterized by congenital weakness, contractures, and dystrophic features on muscle biopsy. However, these syndromes are often difficult to diagnose precisely because their clinical and pathologic characteristics are not specific and resemble changes in other myopathies. We examined muscle biopsies from 20 children with a congenital muscular dystrophy syndrome. Disease controls with dystrophies or other myopathies (n=19) and normal individuals (n=15) were studied for comparison. In each biopsy we determined (1) numbers of muscle fibers with alkaline phosphatase (AlkP) staining, (2) numbers of acid phosphatase-(AcP) positive cells, (3) dystrophin levels by immunocytochemistry, and (4) the distribution of merosin and laminin-A staining. A ratio of AcP:AlkP staining was calculated for each biopsy. In nine patients with congenital muscular dystrophy (younger than 4 years of age) with normal dystrophin, the AcP:AlkP ratio was low (0.09 +/- 0.03). In contrast, in Duchenne muscular dystrophy, the AcP:AlkP ratio was 15 times higher (1.6 +/- 0.04, p=0.001). The three children with congetial muscular dystrophy syndromes and reduced dystrophin and one child with facioscapulohumeral dystrophy had AcP:AlkP ratios in the range of Duchenne muscular dystrophy patients (2.4 +/- 1.4). Low Ac:AlkP ratios were related to relative absence of AcP-positive cells. Merosin staining was absent in 5 of the 17 congenital muscular dystrophy biopsies tested. None of the 5 children with merosin-negative but all 12 with merosin-positive stains walked (p=0.0002). We conclude that a pattern of few AcP-positive cells in the setting of numerous AlkP staining muscle fibers has specificity for congenital muscular dystrophy syndromes and provides histopathologic support for the diagnosis. Reduced merosin in muscle predicts more severe weakness and long-term disability.

Topics: Acid Phosphatase; Adolescent; Alkaline Phosphatase; Child; Child, Preschool; Dystrophin; Female; Humans; Infant; Laminin; Male; Muscles; Muscular Diseases; Muscular Dystrophies; Reference Values; Staining and Labeling; Syndrome

Topics: Acid Phosphatase; Antibodies, Monoclonal; Humans; Macrophages; Muscle, Skeletal; Muscular Diseases; Staining and Labeling

Lovastatin (LS) is a potent HMG-CoA inhibitor used in the treatment of hypercholesterolemia. In humans it can cause a severe, necrotizing myopathy with myoglobinuria and renal failure. To investigate the pathogenesis of LS-induced myopathy we studied the effects of LS on rat skeletal muscle. Lewis rats were gavage-fed 1 mg/g body weight/day of LS. Control rats received carboxymethylcellulose-based suspension by gavage. Gastrocnemius and soleus, fast and slow twitch muscles respectively, were studied by light and electron microscopy. By day 10 LS-treated rats became severely weak. Gastrocnemius was severely affected with degeneration of membranous organelles and microvacuole formation, but soleus was spared. Eventually, 20-50% of the gastrocnemius but none of the soleus fibers became necrotic. Non-necrotic fibers showed no increases of acid phosphatase, indicating that autophagy was not excited. We conclude that LS causes muscle injury by inducing degeneration of membranous organelles, and fast twitch muscle fibers are selectively vulnerable to LS myopathy.

Topics: Acid Phosphatase; Animals; Basement Membrane; Female; Intracellular Membranes; Lovastatin; Microscopy, Electron; Mitochondria, Muscle; Muscles; Muscular Diseases; Organelles; Rats; Rats, Inbred Lew

Histopathological changes induced by the intramuscular injection of glycerol were studied in the muscle fibers of rabbits. Fifteen minutes after the injection of 1 ml of 50% (v/v) glycerol, hypercontraction of fibers, disruption of the plasma membrane, and invasion of lanthanum into the sarcoplasm were observed. Between 12 and 24 h after the injection, more extensive pathological changes were seen which included: variation in fiber size; degeneration and necrosis of muscle fibers; hypercontraction of fibers by light microscopy; disruption of the plasma membrane by electron microscopy; vacuolar changes; hypercontraction of myofibrils, and selective loss of Z-bands. Between 7 and 14 days after glycerol injection, extensive regenerative changes were seen. The degenerative changes were similar to those seen in muscle in Duchenne muscular dystrophy, suggesting that a similar mechanism may be involved in the two conditions, so that experimental glycerol myopathy could be a good model for pathophysiological studies on Duchenne muscular dystrophy.

Topics: Acid Phosphatase; Animals; Calcium; Female; Glycerol; Microscopy, Electron; Muscles; Muscular Diseases; Necrosis; Rabbits; Regeneration

Four of seven patients with nemaline myopathy had severe, rapidly progressing symptoms. These four showed an increase in acid phosphatase activity in muscle fibers demonstrated by histochemistry and cathepsin B&L activity by biochemical measurement. On electron microscopy, nemaline bodies, occasionally disorganized myofibrils and autophagic vacuoles containing sarcoplasmic debris and glycogen particles were seen. Focal myofibrillar degeneration, through an unknown pathogenetic mechanism, induces an increase in lysosomal enzymes in the skeletal muscles which may be closely correlated with a rapid aggravation of muscle weakness in nemaline myopathy.

Topics: Acid Phosphatase; Cathepsin B; Cathepsin H; Cathepsin L; Cathepsins; Child; Child, Preschool; Cysteine Endopeptidases; Endopeptidases; Female; Histocytochemistry; Humans; Immunoenzyme Techniques; Infant; Male; Microscopy, Electron; Microscopy, Fluorescence; Muscles; Muscular Diseases

Localized high AMP deaminase activity was found in the rimmed vacuoles of skeletal muscles in acid maltase deficiency, distal myopathy with rimmed vacuole formation, and experimental chloroquine myopathy on histochemical staining. Acid phosphatase activity was also increased in and around these vacuoles, but the vacuoles were negative for other histochemical stainings such as with NADH-tetrazolium reductase, ATPase and phosphorylase. These findings suggest that AMP deaminase is bound to membranous components in addition to myosin in skeletal muscle.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; AMP Deaminase; Animals; Chloroquine; Female; Glucan 1,4-alpha-Glucosidase; Glucosidases; Humans; Infant; Male; Muscles; Muscular Diseases; NADH Tetrazolium Reductase; Nucleotide Deaminases; Phosphorylases; Rats; Rats, Inbred Strains; Vacuoles

The reliability of enzyme histochemical semipermeable membrane techniques for the demonstration of acid hydrolases was investigated with a combined histochemical and biochemical study. In part 1 the histochemical findings were presented. In this communication the biochemical findings are reported and compared with the histochemical findings. In m. soleus, m. plantaris, m. gastrocnemius and diaphragm of vitamin E deficient rabbits the activity of the lysosomal acid hydrolases, cathepsin D, acid maltase, acid phosphatase and beta-glucuronidase is significantly increased. This increase in activity of the investigated acid hydrolases was equal for muscles with an aerobic or an anaerobic metabolism. By means of statistical calculations the activity of the enzymes demonstrated with histochemical techniques was compared with the enzyme activity determined with biochemical techniques. From the results of this investigation it can be concluded that the histochemical semipermeable membrane techniques for the demonstration of activity of acid hydrolases are very reliable. Considering the fact that these techniques are also tissue-saving, they are therefore extremely suitable for the study of catabolic wasting processes in skeletal muscle tissues of patients with inherited or acquired muscular diseases.

Topics: Acid Phosphatase; alpha-Glucosidases; Animals; Cathepsins; Glucuronidase; Histocytochemistry; Humans; Hydrolases; Muscles; Muscular Diseases; Rabbits; Vitamin E Deficiency

Topics: Acid Phosphatase; Animals; Arylsulfatases; Back; Catalase; Cathepsins; Chickens; Chloroquine; Glucuronidase; Hindlimb; Lysosomes; Male; Muscle Denervation; Muscles; Muscular Diseases; Rats; Ribonucleases; Starvation; Time Factors

We established muscle-tissue cultures from biopsy of a patient with adult-onset acid maltase deficiency. Morphologically and biochemically, the newly grown fibers of the cultured muscle showed the same abnormalities as those of the biopsied muscle. Light microscopy showed multiple vacuoles filled with acid-phosphatase-positive material; on ultrastructural examination there was abnormal accumulation of glycogen in membrane-bound sacs (secondary lysosomes), some of which also contained dark membranous of homogeneous material. Acid maltase (pH 4.0), a lysosomal enzyme, was undetectable in either cultured or biopsied muscle by maltose hydrolysis, whereas acid phosphatase, also a lysosomal enzyme, was increased in both sources of muscle cells. Cultured muscle fibers demonstrate the same morphologic and biochemical abnormalities characteristic of biopsied muscle, supporting the concept of a biochemically distinct primary myopathy in man.

Topics: Acid Phosphatase; Adult; Age Factors; Creatine Kinase; Culture Techniques; Glucosidases; Glycogen; Glycogen Storage Disease; Humans; Lysosomes; Male; Muscles; Muscular Diseases

Selected lysosomal hydrolases have been investigated in the trigeminal ganglion of mice afflicted with an hereditary sensory neuropathy (dystonia musculorum). This was done using direct enzyme histochemistry. Correlative electron microscopy was also used to further elucidate perikaryal changes. The earlies observed lesion in the trigeminal ganglion of afflicted mice was numerous axon swellings containing intense lysosomal hydrolase activity. Subsequent to this observation, numerous neurones showed central chromatolysis, eccentric nucleus and increased lysosomal hydrolase activity. As various neurones throughout the ganglion underwent the classical chromatolytic reaction, the Golgi apparatus moved to a juxtanuclear location, and there was a focal juxtanuclear accumulation of lysosomes. During the later stages of the disease, a striking decrease in neuronal hydrolase activity characteristic of neuronal atrophy was observed. These results are consistent with earlier suggestions that loss of sensation in the disease could be due to an interruption of axonal transport in primary sensory of neurones.

Topics: Acid Phosphatase; Animals; Arylsulfatases; Axonal Transport; Axons; Esterases; Golgi Apparatus; Histocytochemistry; Hydrolases; Lysosomes; Mice; Mice, Inbred C57BL; Muscular Diseases; Neuromuscular Diseases; Neurons; Schwann Cells; Trigeminal Ganglion; Trigeminal Nerve

Clinical, electrophysiological and histological evidence is presented of a myopathy not previously described. The patient, aged 15 years, was generally weak and wasted. His condition probably began in utero, but abnormalities of the serum CPK and EMG did not become evident until adolescence. Wide variation in fibre diameter, vacuolation, calcification, increased endomysial connective tissue and intra-fibre splitting were prominent in muscle biopsy sections. Electron microscopy showed numerous rod bodies, fibre disorganisation with loss of Z-bands and occasional honeycomb structures. Frequent zebra bodies were present. Because of the large number of zebra bodies seen, the name "zebra body myopathy" is provisionally proposed.

Topics: Acid Phosphatase; Adolescent; Creatine Kinase; Electromyography; Histocytochemistry; Humans; Inclusion Bodies; Male; Microscopy, Electron; Muscles; Muscular Diseases; Myofibrils

A 28-year-old female, who showed a floppy baby syndrome during early infancy, had a non-progressive proximal muscle weakness with easy fatiguability since childhood. Two muscle specimens biopsied at the age of 28 years revealed myriads of 1-3-mum wide abnormal spaces containing neutral fat in type I and type II fibers. Both biopsies demonstrated a type I fiber preponderance. Electron microscopy demonstrated lipid excess and normal mitochondria by simple inspection. The mitochondrial area and sarcotubular membrane profile concentration in morphometry of longitudinal sections were also normal. Cross-sections, however, revealed a slight decrease of the individual mitochondrial size and of the sarcotubular membrane profile concentration . Serum and muscle carnitine levels and the muscle carnitine palmityltransferase level were all within normal range. Besides carnitine deficiency other biochemical defects can occur in lipid storage myopathy, which represents a syndrome rather than a unique disease entity.

Topics: Acetyltransferases; Acid Phosphatase; Adenosine Triphosphatases; Adult; Carnitine; Electromyography; Female; Humans; Lipid Metabolism; Lipidoses; Male; Mitochondria, Muscle; Muscles; Muscular Diseases; Myofibrils; NADH, NADPH Oxidoreductases; Syndrome

A case of the carcinoid syndrome associated with a proximal myopathy is reported. Histology showed advanced atrophy of type II muscle fibres but no inflammation. Perinuclear acid phosphatase was increased. Electron microscopy revealed persistence of the Z-line until the muscle fibre had been severely disrupted. Similar lesions have been observed in the hereditary muscular dystrophy in mice, and also in these animals and in rats when injected with 5-hydroxytryptamine (5-HT). Treatment with cyproheptadine caused a documented response in the patient's debilitating diarrhoea and also produced symptomatic improvement in her muscular power. We suggest that the myopathy is due to circulating 5-HT or is a non-metastatic complication of the carcinoid tumour.

Topics: Acid Phosphatase; Cyproheptadine; Diarrhea; Feces; Female; Fenclonine; Humans; Hydroxyindoleacetic Acid; Malignant Carcinoid Syndrome; Microscopy, Electron; Middle Aged; Muscles; Muscular Diseases; Myofibrils

Topics: Acid Phosphatase; Adenosine Triphosphatases; Chronic Disease; Creatine Kinase; Female; Glycogen; Histocytochemistry; Humans; Inclusion Bodies; Lipid Metabolism; Lipoproteins; Microscopy, Electron; Middle Aged; Muscles; Muscular Diseases; Myofibrils; NAD; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adolescent; Child; Consanguinity; Glucosyltransferases; Histocytochemistry; Humans; Male; Microscopy, Electron; Microscopy, Phase-Contrast; Microtubules; Muscles; Muscular Diseases; Oxidoreductases; Sarcoplasmic Reticulum; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Amylases; Biliary Tract Diseases; Bone Diseases; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Humans; Isoenzymes; Liver Diseases; Male; Muscular Diseases; Myocardial Infarction; Nervous System Diseases; Organ Specificity; Oxidoreductases; Pancreatic Diseases; Prostatic Diseases; Pulmonary Embolism; Transaminases

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: Acetates; Acid Phosphatase; Adolescent; Adult; Child; Child, Preschool; Dermatomyositis; Glycoside Hydrolases; Hexosaminidases; Humans; Middle Aged; Muscles; Muscular Diseases; Muscular Dystrophies; Myositis; Myotonic Dystrophy; Surface-Active Agents

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Biopsy; Chloroquine; Female; Histocytochemistry; Microscopy, Electron; Microscopy, Phase-Contrast; Muscles; Muscular Diseases; Peroxidases; Rats

Topics: Acid Phosphatase; Age Factors; Alkaline Phosphatase; Animals; Deficiency Diseases; Glucuronidase; Kidney; Liver; Lysosomes; Muscular Diseases; Myocardium; Selenium; Sheep; Spleen; Sulfatases

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; Amylases; Basophils; Cardiomyopathies; Glucosyltransferases; Glycerolphosphate Dehydrogenase; Glycoproteins; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Ligases; Male; Microscopy, Electron; Microtomy; Muscles; Muscular Diseases; Myofibrils; Staining and Labeling; Succinate Dehydrogenase

Topics: Acid Phosphatase; Biopsy; Clinical Enzyme Tests; Electromyography; Glucosyltransferases; Graves Disease; Histocytochemistry; Humans; Long-Acting Thyroid Stimulator; Male; Middle Aged; Muscles; Muscular Diseases; Myofibrils; Ophthalmoplegia; Succinate Dehydrogenase; Thyroid Function Tests; Triiodothyronine

Topics: Acid Phosphatase; Alkaline Phosphatase; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Female; Humans; Isoenzymes; Liver Diseases; Male; Metabolism, Inborn Errors; Muscular Diseases; Myocardial Infarction; Transaminases

Topics: Acid Phosphatase; Animals; Axons; Cytoplasm; Electromyography; Genes, Recessive; Mice; Microscopy, Electron; Muscular Diseases; Neuromuscular Junction

Topics: Acid Phosphatase; Animals; Creatine Kinase; Histocytochemistry; Isoenzymes; L-Lactate Dehydrogenase; Muscles; Muscular Diseases; Necrosis; Rabbits; Regeneration; Tibia

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Azo Compounds; Food Additives; Glucosyltransferases; Heart; Heart Diseases; Histocytochemistry; Lysosomes; Microscopy, Electron; Muscles; Muscular Diseases; Myocardium; Myofibrils; Pigments, Biological; Rats

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; Cholinesterases; Glucosephosphate Dehydrogenase; Glycerolphosphate Dehydrogenase; Glycogen; Humans; L-Lactate Dehydrogenase; Malate Dehydrogenase; Methods; Muscles; Muscular Diseases; Myofibrils; Oxidoreductases; Oxygen; Succinate Dehydrogenase; Water-Electrolyte Balance

Topics: Acid Phosphatase; Animals; Cathepsins; Galactosidases; Glucuronidase; Lysosomes; Muscular Diseases; Sheep; Sheep Diseases; Sulfatases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Coxsackievirus Infections; Dihydrolipoamide Dehydrogenase; Electron Transport Complex II; Glucosephosphate Dehydrogenase; Histocytochemistry; Hydrocortisone; Mice; Muscles; Muscular Diseases; Necrosis; Pharmacology; Rabbits; Rats; Regeneration; Research; RNA; Succinate Dehydrogenase; Triamcinolone

The study of children with symmetrical nonprogressive muscle weakness and hypotonia has previously led to the discovery of two new disorders of striated muscle. A third myopathy in a child with hypotonia and proximal weakness is reported. Cytochemical and electron-microscopic studies reveal large, bizarre, interfibrillary and subsarcolemmal mitochondria in muscle obtained by biopsy. Smooth muscle of the vascular wall did not show such abnormalities nor did leucocytes or intramuscular nerves with cytochemical techniques. The basal metabolic rate of the patient was within normal limits.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Biopsy; Child; Electron Transport Complex IV; Electrons; Histocytochemistry; Humans; Lysosomes; Microscopy; Microscopy, Electron; Mitochondria; Mitochondrial Diseases; Muscles; Muscular Diseases; NAD; Oxidoreductases; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Amylases; Aspartate Aminotransferases; Clinical Enzyme Tests; Creatine Kinase; D-Alanine Transaminase; Diagnosis, Differential; Humans; Liver Diseases; Muscular Diseases; Myocardial Infarction; Pancreatitis

Topics: Acid Phosphatase; Adrenal Cortex Hormones; Animals; Dihydrolipoamide Dehydrogenase; Epinephrine; Histocytochemistry; Mitochondria; Muscles; Muscular Diseases; Pathology; Phosphotransferases; Rabbits; Research; Succinate Dehydrogenase; Toxicology; Triamcinolone