| Abstract
| - There is evidence that serious pathologies are associated with aluminum (Al). In the present work, the influenceof Al on enzymatic lipolysis was studied with the aim to get more insight into the possible link between the Al-inducedmembrane modification and the cytotoxicity of the trivalent cation (AlIII). Lipid monolayers were used as modelmembranes. The monomolecular film technique allowed monitoring the Al-dependent modifications of the lipidmonolayer properties and enzyme kinetics. Two enzymes, namely, Candida rugosa lipase and a calcium (CaII)-dependent phospholipase A2 from porcine pancreas, were used to catalyze the lipolysis of triglyceride andphosphoglyceride monolayers, respectively. The results obtained show that Al modifies both the monolayer structureand enzymatic reaction rates. While the enzymes used in this study can be considered as probes detecting lipidmembrane properties, it cannot be excluded that in physiological conditions modulation of the enzyme action by theAl-bound membranes is among the reasons for Al toxicity.
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