Share Email Print

Proceedings Paper

Protein kinase C modulates the motional properties of its lipid cofactor DPH-diacylglycerol
Author(s): Eward Pap; Jan-Willem Borst; Martjin Ketelaars; Arie van Hoek; Antonie J. W. G. Visser
Format Member Price Non-Member Price
PDF $17.00 $21.00

Paper 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.

Paper Details

Date Published: 17 August 1994
PDF: 5 pages
Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); doi: 10.1117/12.182783
Show Author Affiliations
Eward Pap, Agricultural Univ. Wageningen (Netherlands)
Jan-Willem Borst, Agricultural Univ. Wageningen (Netherlands)
Martjin Ketelaars, Agricultural Univ. Wageningen (Netherlands)
Arie van Hoek, Agricultural Univ. Wageningen (Netherlands)
Antonie J. W. G. Visser, Agricultural Univ. Wageningen (Netherlands)

Published in SPIE Proceedings Vol. 2137:
Time-Resolved Laser Spectroscopy in Biochemistry IV
Joseph R. Lakowicz, Editor(s)

© SPIE. Terms of Use
Back to Top
Sign in to read the full article
Create a free SPIE account to get access to
premium articles and original research
Forgot your username?