acid-phosphatase and Muscular-Dystrophy--Animal

Dystrophic hamster has been regarded as the useful model animal for Severe childhood autosomal recessive muscular dystrophy (SCARMD). Although, many studies on Dystrophic hamster have utilized the muscular tissue of the trunk, however no study have been analyzed for the masticatory muscle. For this study, we used a Dystrophic hamster (UM-X7.1 Syrian hamster) to histochemically investigate the effect of muscular dystrophy on the masseter muscle. Large and small regenerated muscle fibers, and necrotic fibers were detected almost in all areas. Opaque fiber, hypertrophic fiber with fiber splitting structure and necrotic fiber filled up by mononuclear phagocytes were recognized. The region, in which the mononuclear phagocytic cells infiltrated, showed strong positivity to acid phosphatase, and lysosome enzyme. There were many muscle fibers with reduced levels of succinate dehydrogenase (SDH) activities in the muscle fiber. Some TUNEL-positive cells were confirmed in both necrotic and non-necrotic areas. It was suggested that a part of TUNEL-positive cells are the cells originated from the connective tissue or immunocytes. In this result, histopathologic changes of the masseter muscle of the UM-X7.1 Syrian hamster was similar to muscle of the body trunk in the past reports. As the result, it was suggested that jaw closing movements may be negatively affected caused by the decline of the masseter muscle twitch. And, the point of view by which apoptosis is the trigger for the muscle fiber collapse were not seen in the Dystrophic hamster masseter muscle. We suggest that apoptosis is a one step in the process of regeneration of muscle fibers.

Topics: Acid Phosphatase; Animals; Cricetinae; In Situ Nick-End Labeling; Male; Masseter Muscle; Mesocricetus; Muscular Dystrophy, Animal; Succinate Dehydrogenase

C2 mouse myogenic cells carrying the lacZ gene coding for beta-galactosidase (beta-gal) were injected into the tibialis anterior muscle of dystrophin-deficient mdx mice. Introduced cells were shown to have been incorporated into fibres of the injected muscle by virtue of the colocalization of beta-gal and dystrophin within them. Synthetic Nuclepore membrane inserted between the injected tibialis anterior and adjacent extensor digitorum longus muscle permitted the visualization of cells migrating between the two muscles through the pores of the membrane. Although the exact nature of the cells passing through the Nuclepore could not be determined by this method, they were thought to include implanted myogenic cells. Evidence for this was gained by the presence of beta-gal/dystrophin positive fibres within the extensor digitorum longus. Incorporation of cells into the adjacent extensor digitorum longus was greater in animals where this muscle had been autografted by the cutting and resuturing of the distal tendon. Autografted extensor digitorum longi differed from those which had not been subject to this procedure, by undergoing extensive fibre degeneration followed by regeneration, and further by the stripping of their surrounding epimysial covering. Implanted cells substantially participated in extensor digitorum longus fibre formation in these mice, up to 31% of their fibres 3 weeks after implantation coexpressing both the introduced lacZ gene product and the dystrophin gene product, the latter not normally expressed within the fibres of this myopathic recipient.

Topics: Acid Phosphatase; Animals; beta-Galactosidase; Cell Line; Cell Movement; Disease Models, Animal; Genetic Linkage; Glucose-6-Phosphate Isomerase; Lac Operon; Mice; Mice, Mutant Strains; Mice, Nude; Muscles; Muscular Dystrophy, Animal; Transfection; X Chromosome

Macrophages and mast cells in masseter muscle from normal and dystrophic mice were studied by light and electron microscopy. Acid phosphatase activity and FITC-dextran were used to identify and describe macrophages. Toluidine blue was used as a marker for mast cells. In dystrophic muscle, the number of macrophages was greatly increased and they contained large amounts of phagocytozed material. In normal muscle, mast cells were rarely identified whereas dystrophic muscle contained many mast cells which were often in close contact with macrophages.

Topics: Acid Phosphatase; Animals; Cytoplasmic Granules; Macrophages; Masseter Muscle; Mast Cells; Masticatory Muscles; Mice; Mice, Inbred C57BL; Microscopy, Electron; Muscular Dystrophy, Animal; Vacuoles

The activity of acid phosphatase in skeletal muscle fibres of the plantaris and soleus of normal and dystrophic male hamsters was quantified using a histochemical post-coupling semipermeable membrane technique. Although the absolute levels of activity were found to vary widely from one animal to another, the ratio of the mean activities in the two muscles in each animal was virtually constant. In normal muscles, the ratio was about 0.73 and in dystrophic muscles, about 0.77. The activity in plantaris muscle fibres was always significantly lower than that in the corresponding soleus fibres, and in normal fibres compared to dystrophic ones. Another difference was that in normal fibres the mean activity declined to a constant level in mature animals older than about 3 months. In contrast, the activity in dystrophic muscles appeared to fall exponentially throughout life. The functional significance of these findings is discussed.

Topics: Acid Phosphatase; Age Factors; Animals; Cricetinae; Histocytochemistry; Male; Muscles; Muscular Dystrophy, Animal

Three distinct acid phosphatases were recently reported in avian breast muscle [J. H. Baxter and C. H. Suelter (1984) Arch. Biochem. Biophys. 228, 397-406]. Of the increased acid phosphatase activity in dystrophic muscle compared to normal muscle, 84% can be accounted for as a low-molecular-weight, cytosolic form. This low-molecular-weight form has now been purified and resolved into two distinct forms, A and B, differing in isoelectric point, apparent molecular weight, substrate specificity, and activation by guanosine. One of the two enzymes exhibits substrate inhibition with 4-methylumbelliferyl phosphate, indicating a further difference. The evidence suggests that both enzymes are Class IV acid phosphatases. Their concentrations are highest in tissues with a high catabolic activity.

Topics: Acid Phosphatase; Animals; Chickens; Enzyme Activation; Guanosine; Isoelectric Focusing; Kinetics; Molecular Weight; Muscles; Muscular Dystrophy, Animal; Substrate Specificity; Tissue Distribution

There are at least three forms of acid phosphatase in avian pectoralis muscle differing in molecular weight, subcellular location, and response to various substrates and inhibitors. These enzymes are separated by differential sedimentation into postmicrosomal supernatant, lysosomal, and microsomal activities with apparent molecular weights in Triton X-100 of 68,000, 198,000, and 365,000, respectively. All of the enzymes show acid pH optima (pH approximately 5), but the postmicrosomal supernatant form is distinctly different from the other two forms in its resistance to most common phosphatase inhibitors and in its reduced activity against several organic phosphates. Quantitation of these three forms of acid phosphatase in normal and dystrophic avian pectoralis muscle shows that the postmicrosomal supernatant form is significantly elevated in dystrophic muscle; at 33 days ex ovo, 84% of the increased acid phosphatase activity in dystrophic muscle can be attributed to the postmicrosomal supernatant form. The microsomal form is only slightly elevated; the level of the lysosomal form is not altered.

Topics: Acid Phosphatase; Animals; Chickens; Chromatography, Gel; Cytosol; Hydrogen-Ion Concentration; Lysosomes; Microsomes; Muscles; Muscular Dystrophy, Animal; Substrate Specificity

Topics: Acetylglucosaminidase; Acid Phosphatase; alpha-Glucosidases; Animals; Catalase; L-Lactate Dehydrogenase; Mice; Muscle Proteins; Muscles; Muscular Dystrophy, Animal; Nucleotidases; Succinate Dehydrogenase

In hamsters, the specific activities of acid phosphatase and beta-glucuronidase are much greater in homogenates of dystrophic muscle than in homogenates of normal muscle because, it is argued in this paper, dystrophic muscles concentrate such enzymes within themselves, in contrast to normal muscles which do not, or only very little. Both enzymes are first apparent histochemically (using the appropriate naphthol AS-BI substrates) in the atrophic type I fibres of, for example, 3--4 weeks-old dystrophic hamsters, at which age type II fibres (in the Johnson & Pearse nomenclature) contain neither enzyme and a myopathy is undetectable by standard clinical criteria. We have been unable to find out where the enzymes originate from, or in or on which organelle in dystrophic muscle they are localised; the histochemical, organelle fractionation, isoelectric focussing and electron microscopic evidence on these points is conflicting. On balance it seems that the acid hydrolases are synthesised by the dystrophic muscle fibres themselves, rather than being derived from discharged macrophage granules as is more commonly believed. But whatever their origin, a histochemical test for acid hydrolases should be useful, it is concluded, for diagnosing the preclinical phase of myopathies in children.

Topics: Acid Phosphatase; Animals; Cricetinae; Glucuronidase; Muscles; Muscular Dystrophy, Animal; Subcellular Fractions

Topics: Acid Phosphatase; Animals; Cricetinae; Histocytochemistry; Lysosomes; Male; Mitochondria, Muscle; Muscles; Muscular Dystrophy, Animal; Sarcoplasmic Reticulum; Subcellular Fractions

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Animals; Cricetinae; Glycogen; Histocytochemistry; Muscles; Muscular Dystrophy, Animal; Myofibrils; NADH, NADPH Oxidoreductases; Phosphorylases; Regeneration; RNA; Transplantation, Autologous; Transplantation, Homologous