Different effects of aluminum upon carbonic anhydrases and Na+/K+-ATPase activities in rat.
Aluminum (Al(III)) is a well established toxicant implicated as an etiological factor in several neuropathies. In this paper we report results regarding opposite effects produced by Al(III) on the activity of two enzymes utilized as models. While sodium-potassium ATP-ase (Na/K-ATPase) is strongly activated by Al(III) in a dose-effect dependent way, on the contrary, carbonic anhydrase (CA) is remarkably inhibited. The relevance of the metal speciation together with the enzymatic structural modification demonstrated by circular dichroism measurements could explain the observed modified enzymatic activities. In addition, a new experimental protocol for the preparation of Al(III) solutions at physiological pH useful in the standardization of Al(III) experimental toxicology is also proposed and discussed.
CNR-Center on Metalloproteins, University of Padova, Department of Biology, Italy.
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Zatta
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Zambenedetti
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Pizziuti
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Perazzolo
D000535:Aluminum / Q000494:pharmacology*; D000818:Animals; D001921:Brain / Q000187:drug effects / Q000201:enzymology; D002257:Carbonic Anhydrase Inhibitors / Q000494:pharmacology*; D002256:Carbonic Anhydrases / Q000097:blood / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology; D051381:Rats; D017208:Rats, Wistar; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000378:metabolism*
D002257:Carbonic Anhydrase Inhibitors; D000535:Aluminum; D002256:Carbonic Anhydrases; D000254:Sodium-Potassium-Exchanging ATPase