acid-phosphatase and Brain-Diseases

Topics: Acid Phosphatase; Aged; Aging; Aluminum; Animals; Brain Diseases; Cerebral Cortex; Cholinesterases; Dementia; Esterases; Glutamate Dehydrogenase; Hippocampus; Histocytochemistry; Humans; Lysosomes; Male; Microscopy, Electron; Nervous System; Neurons; Nissl Bodies; Oxidoreductases; Phosphates; Pigments, Biological; Rabbits; Spinal Cord

Focal cortical dysplasia (FCD) is a localized malformation of cortical development and is the commonest cause of severe childhood epilepsy in surgical practice. Children with FCD are severely disabled by their epilepsy, presenting with frequent seizures early in life. The commonest form of FCD in children is characterized by the presence of an abnormal population of cells, known as balloon cells. Similar pathological changes are seen in the cortical malformations that characterize patients with tuberous sclerosis complex (TSC). However, the cellular and molecular mechanisms that underlie the malformations of FCD and TSC are not well understood. We provide evidence for a defect in autophagy in FCD and TSC. We have found that balloon cells contain vacuoles that include components of the autophagy pathway. Specifically, we show that balloon cells contain prominent lysosomes by electron microscopy, immunohistochemistry for LAMP1 and LAMP2, LysoTracker labelling and enzyme histochemistry for acid phosphatase. Furthermore, we found that balloon cells contain components of the ATG pathway and that there is cytoplasmic accumulation of the regulator of autophagy, DOR. Most importantly we found that there is abnormal accumulation of the autophagy cargo protein, p62. We show that this defect in autophagy can be, in part, reversed in vitro by inhibition of the mammalian target of rapamycin (mTOR) suggesting that abnormal activation of mTOR may contribute directly to a defect in autophagy in FCD and TSC.

Topics: Acid Phosphatase; Adaptor Proteins, Signal Transducing; Autophagy; Brain; Brain Diseases; Cells, Cultured; Child; Cytoplasm; Epilepsy; Humans; Immunohistochemistry; Lysosomal Membrane Proteins; Lysosomal-Associated Membrane Protein 2; Lysosomes; Malformations of Cortical Development; Malformations of Cortical Development, Group I; Sequestosome-1 Protein; Tissue Banks; TOR Serine-Threonine Kinases; Tuberous Sclerosis

Many studies have shown that pigment epithelium-derived factor (PEDF) has neurotrophic effects on retinal cells and hippocampal, spinal cord, and cerebellar granule cell neurons, but much less work has examined the effects of PEDF on glia. In this study, we show that PEDF changes microglial morphology within 1 h of exposure, to a more deactivated form, while having no effect on the expression of such activation markers as OX-42 and ED-1. In contrast, urea activates acid phosphatase, and PEDF blocks that activation. PEDF also activates NFkappaB, accompanied by the induction of mRNAs and proteins for the chemokines macrophage inflammatory protein-1alpha (MIP-1alpha, MIP-2, and MIP-3alpha. All the chemokines stimulate acid phosphatase activity, and high doses of MIP-2 and MIP-3alpha), alter the morphology of the microglia at 1 h after treatment. These results suggest that the use of PEDF for clinical treatments, such as for retinal neovascularization, brain injury, or ischemia, should be undertaken with caution because of the possibility of induction of inflammation caused by microglial or other immune cell migration in response to the chemokines induced by PEDF.

Topics: Acid Phosphatase; Active Transport, Cell Nucleus; Animals; Brain Diseases; Cell Movement; Cell Shape; Cells, Cultured; Chemokine CCL3; Chemokine CCL4; Chemokines; Enzyme Activation; Eye Proteins; Gliosis; Inflammation Mediators; Macrophage Inflammatory Proteins; Microglia; Nerve Growth Factors; NF-kappa B; Rats; Rats, Sprague-Dawley; RNA, Messenger; Serpins; Up-Regulation; Urea

Encephalopathy was induced in 14-day-old chicks by a vitamin E-deficient diet containing 15% thermally oxidized safflower oil. Bound acid phosphatase activity in the cerebellum was markedly lower in affected chicks than in vitamin E-supplied control chicks. Free activity also tended to be lower in the deficient group. There were no differences in enzyme activities of cerebrum and liver between deficient and control chicks.

Topics: Acid Phosphatase; Animals; Brain Diseases; Cerebellar Diseases; Chickens; Lysosomes; Male; Poultry Diseases; Safflower Oil; Vitamin E Deficiency

Polyglucine infusions (10 ml/kg) during the first 10 days of postresuscitation period after 4-hour hypovolemic hypotension promotes normalization of general RNA content, quick mobile protein fractions, corresponding prealbumins, albumins, postalbumins, ceruloplasmin, transferrin, and alpha-globulins. Macromolecular protein fractions beta- and gamma-globulins--remained considerably changed: beta-globulins doubled, and gamma-globulins decreased 1.7-fold. Acid phosphatase specific activity increased in the postmitochondrial supernatant by 53%; an increase in the acid phosphatase activity was revealed in the neurons, glia, and vascular endothelium. The amount of Purkinje's cells in the cerebral cortex in the experimental group did not differ essentially from the control values. Thus, the results obtained emphasize the importance of prolonged polyglucine infusions together with other resuscitation measures in the treatment of hypovolemic states.

Topics: Acid Phosphatase; Animals; Brain Diseases; Cerebral Cortex; Dextrans; DNA; Dogs; Female; Histocytochemistry; Male; Nerve Tissue Proteins; Resuscitation; RNA

Topics: Acid Phosphatase; Animals; Blood Vessels; Brain Diseases; Cerebellum; Chickens; Chloroquine; Endothelium; Fatty Acids; Histocytochemistry; Inclusion Bodies; Linoleic Acids; Lipid Metabolism; Microscopy, Electron; Microscopy, Fluorescence; Neurons; Phospholipids; Purkinje Cells; Vitamin E Deficiency

Topics: Acid Phosphatase; Animals; Blood-Brain Barrier; Brain Diseases; Diabetes Complications; Enzyme Activation; Humans; Lysosomes; Mice; Rats

Topics: Acid Phosphatase; Adenosine Triphosphatases; Aerosols; Animals; Brain Diseases; Corpus Callosum; Cyanides; Demyelinating Diseases; Histocytochemistry; Necrosis; Neuroglia; Oxidoreductases; Phosphoric Monoester Hydrolases; Rats; Thiamine Pyrophosphate

Topics: Acid Phosphatase; Adenosine Triphosphatases; Aged; Autopsy; Brain; Brain Diseases; Cholinesterases; Dementia; Esterases; Histocytochemistry; Humans; Middle Aged

Topics: Acid Phosphatase; Aging; Amyloidosis; Animals; Axons; Brain; Brain Diseases; Cerebral Cortex; Dementia; Dog Diseases; Dogs; Histocytochemistry; Humans; Macrophages; Microscopy; Nerve Degeneration; Neuroglia

Topics: Acid Phosphatase; Animals; Brain Diseases; Histocytochemistry; Lymphedema; Lysosomes; Male; Microscopy, Electron; Neck; Pantothenic Acid; Pyridoxine; Rats

Topics: Acid Phosphatase; Animals; Arteries; Azides; Basal Ganglia; Brain Diseases; Capillaries; Dihydrolipoamide Dehydrogenase; Electron Transport Complex IV; Glutamate Dehydrogenase; Histocytochemistry; Malate Dehydrogenase; Necrosis; Neuroglia; Phosphogluconate Dehydrogenase; Rats; Sodium; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Brain; Brain Diseases; Deoxyribonucleases; Glucuronidase; In Vitro Techniques; Lysosomes; Mice; Microscopy, Electron; Mitochondria; Prions; Proteins; Succinate Dehydrogenase; Virus Diseases

Topics: Acid Phosphatase; Alkaline Phosphatase; Brain; Brain Diseases; Cerebrospinal Fluid; DNA; Edema; Histocytochemistry; Kidney Diseases; Mercury Poisoning; Phosphoric Monoester Hydrolases; Rabbits; Research; RNA; Toxicology

Topics: Acid Phosphatase; Animals; Brain; Brain Diseases; Histocytochemistry; Hypoxia; Hypoxia-Ischemia, Brain; Hypoxia, Brain; Lysosomes; Phosphoric Monoester Hydrolases; Rats