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J Biol Chem, Vol. 274, Issue 51, 36181-36186, December 17, 1999
, but Not 
, Selectively Removes
Polyunsaturated Diacylglycerol, Inducing Altered Protein Kinase C
Distribution in Vivo*
From the Institute for Cancer Studies, The University of
Birmingham, Birmingham B15 2TA, United Kingdom
Porcine aortic endothelial cells have previously
been shown to contain particularly high basal levels of polyunsaturated
diacylglycerol (DAG) together with a very high degree of
membrane-associated protein kinase C (PKC), which is largely
insensitive to further activation (Pettitt, T. R., Martin, A.,
Horton, T., Liossis, C., Lord, J. M., and Wakelam, M. J. O. (1997) J. Biol. Chem. 272, 17354-17359). To
investigate the possibility that the high polyunsaturated DAG levels
were constitutively activating PKC, we transfected porcine aortic
endothelial cells with two different forms of human diacylglycerol
kinase, 
and 
. In vitro, the former is specific for
polyunsaturated structures, whereas the latter shows no apparent selectivity. Overexpression of DAGK specifically reduced the level
of polyunsaturated DAG in the transfected cells while having little
effect on the more saturated structures. It also caused the
redistribution of PKC
and from the membrane to the cytosol. Overexpression of DAGK caused a general reduction in DAG levels but
had little effect on PKC distribution. These results for the first time
show that DAGK specifically phosphorylates polyunsaturated DAG
in vivo and that in so doing it regulates PKC localization and activity. This provides support for the proposal that it is the
polyunsaturated DAGs that function as messengers and convincing evidence for DAGK being a physiological terminator of DAG second messenger signaling.
To whom correspondence should be addressed. Tel.: 44-121-414-3293;
Fax: 44-121-414-5376; E-mail: M.J.O.Wakelam@bham.ac.uk.
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