Activation of acetylcholinesterase by aluminium(III): the relevance of the metal species.
The present paper reports how aluminium [Al(III)] at a concentration of 3.7 microM can activate the bovine erythrocytic enzyme acetylcholinesterase (AChE) by about 38% in vitro. This same activating effect was observed on AChE form human as well as from rat erythrocyte ghosts and murine neuroblastoma cells. The interaction between Al3+ and gamma-peripheral sites of the enzyme produces AChE structural modifications as evidenced by circular dichroism measurements. This may provide a molecular explanation of the raised enzymatic activity.
Zatta
P
P
Center CNR-Metalloproteins, University of Padova, Department of Biology, Italy.
Zambenedetti
P
P
Bruna
V
V
Filippi
B
B
D000110:Acetylcholinesterase / Q000378:metabolism*; D000535:Aluminum / Q000737:chemistry / Q000494:pharmacology*; D000818:Animals; D001932:Brain Neoplasms / Q000201:enzymology; D002417:Cattle; D002942:Circular Dichroism; D004789:Enzyme Activation / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000201:enzymology; D006801:Humans; D066298:In Vitro Techniques; D051379:Mice; D009447:Neuroblastoma / Q000201:enzymology; D051381:Rats; D014407:Tumor Cells, Cultured
D000535:Aluminum; D000110:Acetylcholinesterase