Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Diacylglycerol kinase activity in brain cytosol and microsomes

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5334122
The ATP-dependent diacylglycerol (DG) kinase phosphorylated DG to form phosphatidic acids (PA). This enzymic conversion is particularly important in the receptor-mediated polyphosphoinositide metabolism. Controlling the DG level in synaptic membranes can also modulate the protein kinase activity within the cell. Using /sup 32/P-ATP, MgCl/sub 2/, NaF and heat treated membranes as substrate, DG-kinase activity was found in both cytosolic and microsomal fractions. Similarities in properties between the two kinase activities were noted. For example, activities in both fractions were stimulated by deoxycholate, and were inhibited by dibucaine and propranol. These results suggest that the microsomal and cytosolic DG-kinase(s) may belong to the same enzyme and that some intracellular factors may be responsible for regulation of the enzyme for interaction with membrane substrate. One of the factors tested was free fatty acid (FFA) which appeared to promote translocation of the cytosolic enzyme to the microsomes. Another factor for regulation is the availability of DG, which is formed via the poly-PI phosphodiesterase in synaptosomes and PA-phosphohydrolase in the microsomes (for de novo biosynthesis of phospholipids). Possible physiological significance of these regulatory mechanisms will be addressed.
Research Organization:
Univ. of Missouri, Columbia
OSTI ID:
5334122
Report Number(s):
CONF-8606151-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:6
Country of Publication:
United States
Language:
English