Interaction between protein kinase C and sphingomyelin/cholesterol |
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Authors: | Jiang Y Pan Z Chen J W |
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Affiliation: | National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China. |
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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. |
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Keywords: | PKC caveolae sphingomyelin fluorescence |
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