✦ LIBER ✦

INTERACTION BETWEEN PROTEIN KINASE C AND SPHINGOMYELIN/CHOLESTEROL

✍ Scribed by Yan Jiang; Zui Pan; Jian Wen Chen

Publisher: Elsevier Science
Year: 1999
Tongue: English
Weight: 137 KB
Volume: 23
Category: Article
ISSN: 1065-6995
DOI: 10.1006/cbir.1999.0374

No coin nor oath required. For personal study only.

✦ Synopsis

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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