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

Biochemistry and biophysics reports (2016-07-20)
Yuuna Kamiya, Satoru Mizuno, Suguru Komenoi, Hiromichi Sakai, Fumio Sakane
RÉSUMÉ

A variety of diacylglycerol (DG) molecular species are produced in stimulated cells. Conventional (α, βII and γ) and novel (δ, ε, η and θ) 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. PKCα activity was strongly increased by DG and exhibited less of a preference for 18:0/22:6-DG at 2 mmol%. PKCβII activity was moderately increased by DG and did not have significant preference for DG species. PKCγ activity was moderately increased by DG and exhibited a moderate preference for 18:0/22:6-DG at 2 mmol%. PKCδ activity was moderately increased by DG and exhibited a preference for 18:0/22:6-DG at 20 and 200 mmol%. PKCε activity moderately increased by DG and showed a moderate preference for 18:0/22:6-DG at 2000 mmol%. PKCη was not markedly activated by DG. PKCθ 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.

MATÉRIAUX
Référence de produit
Marque
Description du produit

Avanti
18:0-20:4 DG, 1-stearoyl-2-arachidonoyl-sn-glycerol, chloroform
Avanti
16:0-23:2 Diyne PE, 1-palmitoyl-2-(10,12-tricosadiynoyl)-sn-glycero-3-phosphoethanolamine, powder
Avanti
18:0-22:6 DG, 1-stearoyl-2-docosahexaenoyl-sn-glycerol, chloroform