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INTERACTION BETWEEN PROTEIN KINASE C AND SPHINGOMYELIN/CHOLESTEROL
Author(s) -
Jiang Yan,
Pan Zui,
Chen Jian Wen
Publication year - 1999
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1999.0374
Subject(s) - sphingomyelin , tryptophan , biochemistry , quenching (fluorescence) , chemistry , fluorescence , lipid bilayer , cholesterol , protein kinase a , kinase , biophysics , membrane , biology , amino acid , physics , quantum mechanics
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.