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

Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species.
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DOI:
10.1016/j.bbrep.2016.07.017
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发表时间:
2016-09
影响因子:
2.7
通讯作者:
Sakane F
Sakane F
中科院分区:
其他
文献类型:
--
作者:
Kamiya Y;Mizuno S;Komenoi S;Sakai H;Sakane F

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受刺激的细胞中会产生多种二酰基甘油 (DG) 分子种类。已知传统(α、βII 和 γ)和新型(δ、ε、η 和 θ)蛋白激酶 C (PKC) 亚型可被 DG 激活。但尚未进行全面分析。在本研究中,我们分析了 2–2000 mmol% 16:0/16:0-、16:0/18:1-、18:1/18:1-、18:0/20:4- 或 18:0/22:6-DG 物种存在下 PKC 同工酶的活化情况。 DG 显着提高了 PKCα 活性,并且对 2 mmol% 的 18:0/22:6-DG 表现出较低的偏好。 DG 适度增加了 PKCβII 活性,并且对 DG 物种没有显着的偏好。 DG 适度增加了 PKCγ 活性,并且对 2 mmol% 的 18:0/22:6-DG 表现出适度的偏好。 DG 适度增加了 PKCδ 活性,并且在 20 和 200 mmol% 时表现出对 18:0/22:6-DG 的偏好。 DG 适度增加了 PKCε 活性,并且对 2000 mmol% 的 18:0/22:6-DG 显示出适度的偏好。 DG 没有显着激活 PKCη。 PKCθ 活性通过 DG 增强最为强烈,并且在 2 mmol% 和 20 mmol% DG 时表现出对 18:0/22:6-DG 的偏好。这些结果表明,传统和新型 PKC 对 DG 具有不同的敏感性和依赖性,并且分别对较短且含有饱和脂肪酸和较长且含有多不饱和脂肪酸的 DG 物种具有明显的偏好。这种差异调节对于它们的生理功能很重要。我们全面分析了不同 DG 物种对 c/nPKC 同工酶的激活。 c/nPKC 对 DG 具有不同的敏感性和依赖性。 c/nPKC 对不同的含脂肪酸 DG 物种具有明显的偏好。这种差异调节对于 PKC 的生理功能非常重要。
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. We comprehensively analyzed activation of c/nPKC isozymes by different DG species. c/nPKCs have different sensitivities and dependences on DG. c/nPKCs have a distinct preference for different fatty acid-containing DG species. This differential regulation would be important for PKCs' physiological functions.