acid-phosphatase and Cardiomyopathies

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adenylyl Cyclases; Animals; Biological Transport; Calcium; Cardiomyopathies; Collagen; Cricetinae; Energy Metabolism; Microscopy, Electron; Microsomes; Mitochondria, Muscle; Myocardium; Myofibrils

Bones of cardiomyopathic hamsters (UM-X7.1 Syrian hamsters), at 5, 10 and 20 weeks of age, were compared chemically and histomorphologically with those of normal Syrian hamsters. Femurs of UM-X7.1 hamsters were significantly shorter than those of normal hamsters, and the mean dry weight, mean volume, mean ash weight per unit bone volume and mean ash as a percentage of dry weight of femurs were all significantly less in UM-X7.1 hamsters. The bone disorder preceded the myocardial calcium precipitation and myocardial hypertrophy in the cardiomyopathic hamsters. In addition, the percentage of cortical area measured on the cross-section of tibia and the appositional rate of bone minerals, determined by a tetracycline labelling technique, were also lower in the UM-X7.1 hamsters. These findings suggest that the bone disorder was associated with decreased bone formation in the UM-X7.1 Syrian hamsters.

Topics: Acid Phosphatase; Age Factors; Alkaline Phosphatase; Animals; Body Weight; Bone and Bones; Bone Density; Calcium; Cardiomegaly; Cardiomyopathies; Cricetinae; Female; Femur; Mesocricetus; Myocardium; Radiography; Tibia

The new calcium antagonist anipamil (1,7-bis-(3-methoxyphenyl)-3-methylaza-7-cyano-nonadecane) exhibited a pronounced protective effect against isoprenaline-induced myocardial necrosis in rats. Anipamil was administered in single doses of 10 or 20 mg/kg daily for 4 days. 30 mg/kg isoprenaline was given by subcutaneous injection on the 3rd and 4th days of the study. The protective effect of anipamil was assessed by histological investigations, and its effect on the activity of the enzymes succinate dehydrogenase, NADH-NBT reductase, acid phosphatase and glucose-6-phosphate dehydrogenase in experimentally-induced myocardial damage was assessed quantitatively by microphotometry. The protective effect of anipamil against isoprenaline-induced myocardial necrosis was definitely dose-dependent: 10 mg/kg anipamil exhibited a partial protective effect, whilst 20 mg/kg anipamil protected the heart completely.

Topics: Acid Phosphatase; Animals; Calcium Channel Blockers; Cardiomyopathies; Glucosephosphate Dehydrogenase; Isoproterenol; Male; NADPH-Ferrihemoprotein Reductase; Necrosis; Propylamines; Rats; Rats, Inbred Strains; Succinate Dehydrogenase

Morphologic and enzymic changes in heart lysosomes were studied following a chronic treatment of animals with a cumulative dose of 15 mg/kg of adriamycin. Myocardial cell damage due to adriamycin included lysosomal changes, sarcotubular swelling, vacuolization and myofibrillar drop-out. These structural changes were more pronounced in the 6-week treated group as opposed to the 3-week treated group. The number of lysosomes per unit area increased from a control value of 3.6 +/- 1.7 to 17.8 +/- 4.0 in the 3-week treated group and 35.9 +/- 9.2 in the 6-week treated groups, respectively. The scatter in the size distribution of lysosomes was much wider in treated animals. Lysosomal hydrolases in the 3-week and 6-week adriamycin-treated group changed as follows: N acetyl beta-glucosaminidase activity fell in the homogenate (H) and nonsedimentable (NS) and rose in the serum (Ser) fractions; a drop in alpha-mannosidase was seen in the sedimentable (S) and Ser fractions; an increase in beta-galactosidase was noted in the H, S and Ser fractions; acid phosphatase was increased in H, S, NS and Ser fractions. Lanthanum staining, used as a cytochemical probe for normal membrane permeability, revealed intracytoplasmic localization of the tracer only in the 6-week group. Malondialdehyde content was increased significantly in the 3-week and 6-weed treated groups. These results show lysosomal changes in adriamycin-treated hearts which precede as well as accompany nonspecific permeability changes in the sarcolemma.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; beta-Galactosidase; Cardiomyopathies; Doxorubicin; Lysosomes; Male; Mannosidases; Myocardium; Rats; Rats, Inbred Strains

Topics: Acid Phosphatase; Adolescent; Adult; Blood Platelets; Cardiomyopathies; Female; Humans; Male; Middle Aged; Myocarditis; Oxidoreductases; Platelet Adhesiveness; Platelet Count; Platelet Function Tests

The initial phase and the development of myocardial focal necroses were studied in 50 rats adapted successively to intermittent high altitude. The altitude hypoxia was produced in a low pressure chamber (7000 m, five days a week, four hours daily). First-minute myocardial changes detected by histochemical methods were found after 4 exposures at a level of 3000 m and distinct ones after 8 exposures at a level of 4500 m. Histologically, acute focal necroses were found after 11 exposures at a level of 6000 m. Hypoxia and stress are suggested to account for these myocardial focal changes. During further adaptation no further acute focal necroses were observed.

Topics: Acid Phosphatase; Altitude; Animals; Cardiomyopathies; Hypoxia; Male; Necrosis; Rats; Succinate Dehydrogenase

Activities of phosphatidate phosphohydrolase and palmitoyl-CoA hydrolase were determined in cardiac subcellular fractions prepared from rabbits which has received tri-iodothyronine and from hamsters with hereditary cardiomyopathy (strain BIO 14.6). 1. Both mitochondrial and microsomal fractions of hyperthyroid rabbit hearts produced 4-5 times as much diacylglycerol 3-phosphate from glycerol 3-phosphate and palmitate as did those of euthyroid hearts. 2. Phosphatidate phosphohydrolase, measured with phosphatidate emulsion, was activated by 1mm-Mg(2+) in all but the mitochondrial fraction of euthyroid rabbit hearts. The activation was more pronounced in subcellular fractions isolated from hyperthyroid hearts, so that the measured activities were significantly increased above those of the controls. The highest activity was found in the microsomal and lysosomal fractions. 3. In the absence of Mg(2+) during incubation, the difference in phosphohydrolase activities between eu- and hyper-thyroid states was not significant. 4. The phosphohydrolase of subcellular fractions of control hamsters did not respond to addition of 0.5-8.0mm-Mg(2+). The enzyme from cardiomyopathic hearts was slightly inhibited by this bivalent cation and therefore significant increases in activity were observed only in the absence of Mg(2+) from the assay system. 5. The rate of reaction by soluble phosphatidate phosphohydrolase was similar regardless of the nature of the substrate. Both when microsomal-bound phosphatidate was used as the substrate and when phosphatidate suspension was used, the activity of soluble enzyme was lower than that of the microsomal and lysosomal enzymes measured with phosphatidate suspension; this was especially so when the assay was carried out in the absence of Mg(2+). Neither tri-iodothyronine nor cardiomyopathy influenced the soluble phosphohydrolase activity in the two species. 6. Neither tri-iodothyronine nor cardiomyopathy significantly changed palmitoyl-CoA hydrolase activities in subcellular fractions. 7. Microsomal diacylglycerol acyltransferase and myocardial triacylglycerol content were also unchanged in the hyperthyroid state.

Topics: Acid Phosphatase; Acyltransferases; Adenosine Triphosphatases; Animals; Cardiomyopathies; Cricetinae; Electron Transport Complex IV; Glycerol; Heart; Hyperthyroidism; Lipid Metabolism; Lysosomes; Magnesium; Male; Microsomes; Mitochondria; Myocardium; NADPH-Ferrihemoprotein Reductase; Phosphoric Monoester Hydrolases; Proteins; Rabbits; Subcellular Fractions; Thiolester Hydrolases; Triiodothyronine

Topics: Acid Phosphatase; Cardiomegaly; Cardiomyopathies; Esterases; Glycogen; Humans; Lysosomes; Microscopy, Electron; Mitochondria, Muscle; Myocardial Contraction; Myocardium; NADH, NADPH Oxidoreductases

Topics: Acid Phosphatase; Beer; Cardiomyopathies; Cardiomyopathy, Hypertrophic; Cobalt; Glycogen; Histocytochemistry; Humans; Microscopy, Electron; Mitochondria, Muscle; Myocardium; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenine Nucleotides; Adenosine Triphosphatases; Animals; Biological Transport, Active; Cardiomyopathies; Cricetinae; Disease Models, Animal; Endoplasmic Reticulum; Female; Heart Valves; Lipid Metabolism; Male; Microscopy, Electron; Mitochondria, Muscle; Myocardium; Myofibrils; NAD; Oxidoreductases; Sarcolemma

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