acid-phosphatase and Brain-Edema

Liberation and consequent activation of lysosomal enzymes seems to play significant role in the development of brain edema. In the present experiment with adult rabbits, anesthetized with urethane we investigated in the brain tissue homogenates the activity of four lysosomal enzymes, such as desoxyribonuclease, ribonuclease, katepsine D and acid phosphatase following the development of osmotic brain edema as well as in control animals. The activities of the lysosomal enzymes were investigated with a spectrophotometric technique. Experiments showed that the activity of lysosomal enzymes increased sharply during development of brain edema. Thus the obtained results demonstrate the behaviour of activity of the lysosomal enzymes in the brain tissue during development of brain edema and a way of normalization of these processes.

Topics: Acid Phosphatase; Animals; Brain Edema; Lysosomes; Rabbits; Ribonucleases

Topics: Acid Phosphatase; Animals; Animals, Newborn; Blood-Brain Barrier; Brain Edema; Carotid Arteries; Endothelium, Vascular; Histamine; Injections, Intra-Arterial; Swine

In order to clarify the role of lysosomal enzymes in the developmental mechanisms of cerebral lesions under chronic hypertensive conditions, we histochemically and biochemically investigated acid phosphatase, N-acetyl-beta-glucosaminidase, and cathepsin B in the cerebral cortex and subcortical white matter in stroke-prone spontaneously hypertensive rats (SHRSP). Histochemical investigation showed that SHRSP had an increased number of cells with positive reaction to these enzymes in the edematous cortex and degenerated subcortical white matter. The cells with positive reaction were made up of reactive astrocytes and microglias. The activities of all enzymes in the aged SHRSP were higher than those in normotensive rats, the differences being significant at 24 weeks of age. The present study suggests that chronic hypertension or chronic edema causes increased activities of lysosomal enzymes in the cerebral cortex and subcortical white matter, and that the activated lysosomal enzymes take part in the developmental mechanisms of cystic formation as well as the diffuse degeneration of the white matter.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Astrocytes; Brain; Brain Edema; Cathepsin B; Cerebral Cortex; Cerebrovascular Disorders; Enzyme Activation; Hypertension; Male; Nerve Degeneration; Neurons; Rats; Rats, Inbred SHR; Rats, Inbred WKY

The role of two phosphatases (acid and alkaline phosphatase) and a lysosomal aspartyl endopeptidase (cathepsin D) in producing rat brain oedema was studied in 3 different rat cerebral areas (i.e. frontal cortex, hippocampus and striatum) at 1, 2 and 3 d after vasogenic brain oedema induction. The percentage of water content in the frontal cortex increased immediately, 1 d after oedema induction and remained high for 2 and 3 d after oedema induction. In the hippocampus and the striatum the water content only increases 3 d after oedema induction. In the oedematous hemisphere (right), when compared to the contralateral hemisphere (left), the acid phosphatase activity decreases in the hippocampus, while the alkaline phosphatase increases in the frontal cortex and striatum; cathepsin D increases only in the striatum. The changes caused by the enzymatic activities were significant only 2 and 3 d after oedema induction. The results of this study show that: (i) the vasogenic oedema induced in experimental conditions was not sufficient to cause a massive liberation of lysosomal enzymes and (ii) brain areas adjacent (below) to the site of the experimental oedematous lesion (frontal cortex) were influenced by oedema induction.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Brain Edema; Cathepsins; Female; Rats; Rats, Inbred Strains

The disturbances of the carbohydrate metabolism and the activation of acid phosphatases with and without protection by O-(beta-hydroxyethyl)-rutoside (HR) were studied in irradiated rat brains by means of the light microscope. The histochemically demonstrable deposition of glycogen and acid mucopolysaccharides serves as a criterion for a reversible lesion of the irradiated cerebral tissue. The extent of local activation of repair processes following to irradiation can be determined by the quantity of acid phosphatases in the lysosomes. For the dose range of 1 to 5 Gy, HR seems to exert a protective effect on the cellular metabolism of the irradiated cerebral tissue shown by a slight decrease of glycogen and mucopolysaccharide deposits compared to the untreated animals. However, when exceeding a threshold dose of 10 Gy, the deposition of carbohydrates in the HR group is strongly increased. A slightly increased activity of acid phosphatases induced by HR can be supposed at best for the dose range of 5 to 7.5 Gy. If the dose is even more increased, the reverse effect found in the carbohydrate metabolism, too, and an increased activation of acid phosphatases in the control group will be observed. This unexpected reversion of the protective effect could be related to the assumed inhibitory effect of HR on the ATPases and thus on the anaerobic part of glycolysis or to a breakdown of the cell interaction system of endothelial cells, glia cells, and neurons.

Topics: Acid Phosphatase; Animals; Brain; Brain Edema; Carbohydrate Metabolism; Enzyme Activation; Histocytochemistry; Hydroxyethylrutoside; Radiation Dosage; Radiation-Protective Agents; Rats; Rutin

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Brain; Brain Edema; Chlorfenvinphos; Cholinesterases; Female; Insecticides; Male; Rats; Rats, Inbred Strains; Thiamine Pyrophosphatase

The present paper was designed to the study of cerebral edema induced by intracarotid infusion of dinitrophenol. The determinations included variations in three lysosomal enzymes (acid phosphatase, cathepsin C and beta-glucuronidase), Na+-K+-ATP-ase, changes in cerebral RNA and protein concentrations and the synthesis of these macromolecules in vitro. In experimental brain edema a drastic drop in the activity of lysosomal enzymes took place. The acid phosphatase decreased to less than 30% of controls. Cathepsin C and beta-glucuronidase were reduced about 30% and 50% of control levels respectively. Protein concentration in the cerebral tissue also decreased by more than 50%. The concentration of RNA, RNA synthesis, and the level of Na+-K+-ATP-ase remained unchanged. Protein synthesis was stimulated by 75% (against controls). All these phenomena were suppressed when the animals subjected to the action of dinitrophenol were concomitantly treated with the antiacidotic substance, tris (hydroxymethyl) aminomethane.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Brain; Brain Chemistry; Brain Edema; Cathepsins; Dinitrophenols; Glucuronidase; Lysosomes; Rats; RNA

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Brain; Brain Edema; Brain Injuries; Cold Temperature; Dexamethasone; Endopeptidases; Lysosomes; Rats

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Brain Edema; Cholinesterases; Esterases; Histocytochemistry; Injections, Intraperitoneal; Male; Neuroglia; Pyrophosphatases; Rats; Rats, Inbred Strains; Sulfatases; Thiamine Pyrophosphate; Time Factors; Tin

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Brain Edema; Cats; Cerebral Cortex; Histocytochemistry; Hypotonic Solutions; Neuroglia; Phosphoric Monoester Hydrolases; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Amidohydrolases; Animals; Brain Edema; Brain Injuries; Cathepsins; Cold Temperature; Glucuronidase; Histocytochemistry; Lysosomes; Mitochondria; Nerve Endings; Peptide Hydrolases; Phosphoric Monoester Hydrolases; Rats

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Brain; Brain Edema; Dinitrophenols; Dogs; Isocitrate Dehydrogenase; Oxidative Phosphorylation; Oxidoreductases; Succinate Dehydrogenase; Transaminases; Water

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Brain Edema; Calcium; Cell Membrane Permeability; Dogs; Esterases; Glycolysis; Histocytochemistry; In Vitro Techniques; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Magnesium; Neuroglia; Oxidative Phosphorylation; Pinocytosis; Psyllium; Staining and Labeling; Succinate Dehydrogenase

Topics: Acid Phosphatase; Brain Abscess; Brain Edema; Brain Neoplasms; Cerebellum; Cerebral Cortex; Cerebral Hemorrhage; Esterases; Histocytochemistry; Humans; Neuroglia; Staining and Labeling

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Axons; Brain Edema; Cerebrovascular Disorders; Dendrites; Female; Histocytochemistry; Hypoxia, Brain; In Vitro Techniques; Ischemia; Lysosomes; Male; Neuroglia; Neurons; Oxidoreductases; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Brain Edema; Brain Neoplasms; Histocytochemistry; Humans; In Vitro Techniques; Neuroglia; Pyrophosphatases; Thiamine