Interaction between protein kinase C and sphingomyelin/cholesterol.
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.
Jiang
Y
Y
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
Pan
Z
Z
Chen
J W
JW
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
D008567:Membranes, Artificial; D013109:Sphingomyelins; D002784:Cholesterol; D011493:Protein Kinase C