title: Interaction between protein kinase C and sphingomyelin/cholesterol.
abstract: Physical characteristics of binding of protein kinase C with sphingomyelin/cholesterol lipid bilayers were analysed using three complementary approaches: acrylodan fluorescence, fluorescence energy transfer and quenching of tryptophan fluorescence. It was demonstrated that sphingomyelin/cholesterol lipid membranes were available for protein kinase C binding. The intensity of the binding was dependent on the sphingomyelin content. The results of quenching of intrinsic tryptophan fluorescence showed that the enzyme molecule penetrated the sphingomyelin/cholesterol lipid bilayer to the C-16 position of labeled fatty acid probes. Our results also showed sphingomyelin itself restrains protein kinase C activity. A possible explanation for our results is that caveolae function as signaling storage devices.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
authors.forename: Y
authors.initials: Y
authors.lastname: Jiang
authors.forename: Z
authors.initials: Z
authors.lastname: Pan
authors.forename: J W
authors.initials: JW
authors.lastname: Chen
mesh_terms: D002784:Cholesterol / Q000737:chemistry* / Q000378:metabolism; D008567:Membranes, Artificial; D011485:Protein Binding; D011493:Protein Kinase C / Q000737:chemistry* / Q000378:metabolism; D013109:Sphingomyelins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D008567:Membranes, Artificial; D013109:Sphingomyelins; D002784:Cholesterol; D011493:Protein Kinase C