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17 August 1994 Protein kinase C modulates the motional properties of its lipid cofactor DPH-diacylglycerol
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Abstract
The motional properties of DPH labelled diacylglycerol (DG) in vesicles have been investigated in the absence and presence of its biological target: protein kinase C (PKC). In the absence of PKC the extent of ordering and rotational dynamics of DPH-DG turned out to be considerably different from those of DPH labelled phosphatidylcholine (DPH-PC). When DPH-DG was dispersed in membranes containing 10 mole % of phosphatidylserine (PS), addition of PKC led to an immobilization as judged from a slower fluorescence anisotropy decay. This effect was not seen when PS was replaced by PC or in the absence of calcium indicating that negatively charged lipids and calcium are required for interaction between PKC and DPH-DG. Furthermore, the specificity of the interaction of PKC with DPH-DG was compared with that of the control choline lipid DPH-PC.
© (1994) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Eward Pap, Jan-Willem Borst, Martjin Ketelaars, Arie van Hoek, and Antonie J. W. G. Visser "Protein kinase C modulates the motional properties of its lipid cofactor DPH-diacylglycerol", Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); https://doi.org/10.1117/12.182783
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