Takuwa Y, Matsui T, Abe Y, Nagafuji T, Yamashita K, Asano T
Department of Cardiovascular Biology, Faculty of Medicine, University of Tokyo, Japan.
J Cereb Blood Flow Metab. 1993 May;13(3):409-15. doi: 10.1038/jcbfm.1993.55.
Changes in protein kinase C (PKC) activity, membrane lipid metabolism, and the extent of 20-kDa myosin light chain (MLC) phosphorylation in spastic cerebral basilar arteries were examined by using the beagle "two-hemorrhage" model of subarachnoid hemorrhage. In spastic arteries at days 4 and 7, cytosolic PKC activity showed a decrease of 40-45% with no significant changes in membrane PKC activity as compared with nonspastic control arteries. Cytosolic PKC activity of the day 14 arteries returned toward the normal control level with the remission of vasospasm. Western blot analysis of the PKC isoforms revealed that the amounts of PKC alpha and PKC epsilon but not PKC zeta were decreased in spastic arteries. As compared with nonspastic arteries, spastic arteries showed higher rates of incorporation of [3H]choline into phosphatidylcholine (PC) and [14C]ethanolamine into phosphatidylethanolamine (PE), but not of [3H]myoinositol into phosphoinositides, suggesting the stimulated turn-over of PC and PE. The extent of 20-kDa MLC phosphorylation was not increased in the spastic arteries at days 4 or 7 as compared with that in the nonspastic control arteries. These results demonstrate that PKC activity and related membrane lipid metabolism are altered in spastic basilar arteries after subarachnoid hemorrhage.