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Interaction of annexin A6 with cholesterol rich membranes is pH-dependent and mediated by the sterol OH by Magdalena M. Domon; Gladys Matar; Agnieszka Strzelecka-Kiliszek; Joanna Bandorowicz-Pikula; Slawomir Pikula; Françoise Besson is a Chemistry article available to read on EtoBox.

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Annexin A6 (AnxA6), a calcium-and membrane-binding protein, is well-known to play a role in calcium homeostasis, membrane traffic and membrane organization. It had been suggested that, despite calciumdependent interaction with anionic phospholipids, AnxA6 displays calcium-independent cholesterol binding properties. In this study, the following questions were addressed: does AnxA6 bind preferentially to cholesterol-containing biomimetic membranes? If so, what is the molecular mechanism of the binding? To answer these questions, human recombinant AnxA6-1 isoform was prepared and used with Langmuir monolayers containing various lipids. The interactions between AnxA6 and the lipid monolayers were examined by kinetic measurements of the interfacial adsorption and Brewster angle microscopy. We focused on the pH effect on the AnxA6 binding to monolayers containing cholesterol. At acidic pH, AnxA6-1 exhibits the highest affinity to monolayers containing the highest amount of cholesterol. Replacing cholesterol by cholesteryl acetate provided evidence that the hydroxyl group of cholesterol plays a role in AnxA6-lipid interactions. In addition, the affinity of recombinant AnxA6-1 tryptophan m

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Author

Magdalena M. Domon; Gladys Matar; Agnieszka Strzelecka-Kiliszek; Joanna Bandorowicz-Pikula; Slawomir Pikula; Françoise Besson

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0021-9797)

Published

2010

Language

EN

Field

Chemistry (Physical Sciences)