Activation of bile salt dependent lipase by (lyso)phosphatidic acid and platelet activating factor
Hervé Fontbonne1, Antoine Puigserver, Bernard Bouza
1Aix Marseille Université, CNRS, Centrale Marseille, ISM2 UMR 7313, Case 342, Faculté des Sciences et Techniques de Saint Jérôme, 13397 Marseille, France.
Abstract:
The activity of breast milk BSDL was assayed with or without phospholipids as extra-intestinal effector candidates. Phosphatidic acid, lysophosphatidic acid and platelet activating factor but not phosphatidylcholine and lysophosphatidylcholine stimulated BSDL activity at least as efficiently as taurocholate. The apparent dissociation constants of PA and LPA at saturating concentrations of three different substrates were between 0.1 and 13.4 μM and that of PAF was below or equal to 200 pM. Kinetic data suggested the existence of at least one binding site for each of these effectors. PA, LPA and PAF are likely extra-intestinal modulators of BSDL activity.
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