Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species.

ABSTRACT: A variety of diacylglycerol (DG) molecular species are produced in stimulated cells. Conventional (?, ?II and ?) and novel (?, ?, ? and ?) protein kinase C (PKC) isoforms are known to be activated by DG. However, a comprehensive analysis has not been performed. In this study, we analyzed activation of the PKC isozymes in the presence of 2-2000 mmol% 16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- or 18:0/22:6-DG species. PKC? activity was strongly increased by DG and exhibited less of a preference for 18:0/22:6-DG at 2 mmol%. PKC?II activity was moderately increased by DG and did not have significant preference for DG species. PKC? activity was moderately increased by DG and exhibited a moderate preference for 18:0/22:6-DG at 2 mmol%. PKC? activity was moderately increased by DG and exhibited a preference for 18:0/22:6-DG at 20 and 200 mmol%. PKC? activity moderately increased by DG and showed a moderate preference for 18:0/22:6-DG at 2000 mmol%. PKC? was not markedly activated by DG. PKC? activity was the most strongly increased by DG and exhibited a preference for 18:0/22:6-DG at 2 and 20 mmol% DG. These results indicate that conventional and novel PKCs have different sensitivities and dependences on DG and a distinct preference for shorter and saturated fatty acid-containing and longer and polyunsaturated fatty acid-containing DG species, respectively. This differential regulation would be important for their physiological functions.

SUBMITTER: Kamiya Y 

PROVIDER: S-EPMC5613651 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature