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1.
J Hirnforsch ; 39(2): 183-91, 1998.
Article in English | MEDLINE | ID: mdl-10022342

ABSTRACT

Brain phagocytes are members of a heterogeneous family of microglial cells. In this study we investigated the membrane activity of the enzyme, thiamine pyrophosphatase (TPP-ase), in brain phagocytes. Studies were performed on rats subjected to a transient ischemia because ischemic incident precipitates proliferation of microglial cells in the brain. Brain tissue was sampled from animals that survived 12 months after experimentally evoked cardiac arrest. The product characteristic for TPP-ase activity was present in the Golgi cisterns of neurons, basement membranes of endothelia and capillary pericytes. TPP-ase activity was present on plasma membranes of brain phagocytes. The phagocyte TPP-ase activity did not depend on the anatomical localization of the cell in the brain (cortex, hippocampus, hypothalamus). Thus, TPP-ase activity can be considered as a marker of brain phagocytes.


Subject(s)
Brain/enzymology , Brain/pathology , Heart Arrest/enzymology , Heart Arrest/pathology , Phagocytes/enzymology , Phagocytes/ultrastructure , Thiamine Pyrophosphatase/ultrastructure , Animals , Brain/ultrastructure , Brain Ischemia/enzymology , Brain Ischemia/pathology , Cell Membrane/enzymology , Cell Membrane/ultrastructure , Cerebral Cortex/enzymology , Cerebral Cortex/pathology , Cerebral Cortex/ultrastructure , Hippocampus/enzymology , Hippocampus/pathology , Hippocampus/ultrastructure , Hypothalamus/enzymology , Hypothalamus/pathology , Hypothalamus/ultrastructure , Male , Microglia/enzymology , Microglia/pathology , Microglia/ultrastructure , Microscopy, Electron , Rats , Rats, Wistar , Thiamine Pyrophosphatase/metabolism
2.
J Electron Microsc (Tokyo) ; 40(6): 399-402, 1991 Dec.
Article in English | MEDLINE | ID: mdl-1806652

ABSTRACT

The thiamine pyrophosphatase (TPPase) activity described by Novikoff and Goldfisher was examined in osteoclasts affected by calcitonin in order to elucidate whether the morphological and functional changes of the osteoclasts have an influence over the secretion function of their Golgi apparatus. The Golgi apparatus of osteoclasts of which the ruffled border had disappeared and bone resorption discontinued as the result of treatment with calcitonin showed a slight TPPase activity. The reaction products of the enzyme in these inactive osteoclasts were distinctly fewer than that of control osteoclasts, which were not affected by calcitonin. From these results, it is suggested that there may be a connection between the morphological and functional changes of osteoclasts and the secretion function of the Golgi apparatus.


Subject(s)
Calcitonin/pharmacology , Golgi Apparatus/enzymology , Osteoclasts/enzymology , Thiamine Pyrophosphatase/ultrastructure , Animals , Golgi Apparatus/metabolism , Golgi Apparatus/ultrastructure , Osteoclasts/metabolism , Osteoclasts/ultrastructure , Rats , Rats, Inbred Strains , Thiamine Pyrophosphatase/chemistry
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