Thiaminepyrophosphatase activity in the plasma membrane of microglia.
An intense thiaminepyrophosphatase (TPPase) activity was demonstrated in glial cells and blood vessels in the central nervous system (CNS), when incubation was carried out with thiaminepyrophosphte (TPP, cocarboxylase), using the method of Novikoff and Goldfischer (1961). Glial cells with TPPSase activity were identified as microglia because they were morphologically similar to microglial cells in the sections stained with silver impregnation. TPPase activity was localized in the microglial perikaryon and in the processes, as viewed under a light microscope. Electron microscopically, enzyme activity was localized in the plasma membrane of microglia. We consider this activity to be a true TPPase activity hydrolyzing TPP, and we then went on to examine the substrate specificity, optimum pH, effect of chemical inhibitors and activators, and the effect of glutaraldehyde fixation. Our data are reported herein.
D000818:Animals; D001921:Brain / Q000098:blood supply; D002415:Cats; D002462:Cell Membrane / Q000201:enzymology; D004727:Endothelium / Q000201:enzymology; D005260:Female; D005976:Glutaral / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008297:Male; D009457:Neuroglia / Q000201:enzymology* / Q000648:ultrastructure; D009940:Organoids / Q000201:enzymology; D011755:Pyrophosphatases / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D013379:Substrate Specificity; D013834:Thiamine Pyrophosphatase / Q000378:metabolism*
D011755:Pyrophosphatases; D013834:Thiamine Pyrophosphatase; D005976:Glutaral