Effects of Newly Synthesized DCP-LA-Phospholipids on Protein Kinase C and Protein Phosphatases

Cellular Physiology and Biochemistry

关键词: Protein phosphatase 2A;    Protein tyrosine phosphatase 1B;    DCP-LA-phospholipid;    Protein kinase C;    Protein phosphatase 1;   

DOI  :  10.1159/000350076

学科分类：分子生物学，细胞生物学和基因

来源: S Karger AG

【 摘 要 】

Background/Aims The linoleic acid derivative DCP-LA selectively activates PKCε and inhibits protein phosphatase 1 (PP1). In the present study, we have newly synthesized phosphatidyl-ethanolamine, -serine, -choline, and -inositol containing DCP-LA at the α and β position (diDCP-LA-PE, -PS, PC, and -PI, respectively), and examined the effects of these compounds on activities of PKC isozymes and protein phosphatases. Methods Activities of PKC isozymes PKCα, -βΙ, -βΙΙ, -γ, -δ, -ε-, ι, and -ζ and protein phosphatases PP1, PP2A, and protein tyrosine phosphatase 1B (PTP1B) were assayed under the cell-free conditions. Results All the compounds activated PKC, with the different potential, but only PKCγ inhibition was obtained with diDCP-LA-PC. Of compounds diDCP-LA-PE alone significantly activated PKCι and -ζ. diDCP-LA-PE and diDCP-LA-PI suppressed PP1 activity, but otherwise diDCP-LA-PI enhanced PP2A activity. diDCP-LA-PE, diDCP-LA-PS, and diDCP-LA-PI strongly reduced PTP1B activity, while diDCP-LA-PC enhanced the activity. Conclusion All the newly synthesized DCP-LA-phospholipids serve as a PKC activator and of them diDCP-LA-PE alone has the potential to activate the atypical PKC isozymes PKCι and -ζ. diDCP-LA-PE and diDCP-LA-PI serve as an inhibitor for PP1 and PTP1B, diDCP-LA-PS as a PTP1B inhibitor, diDCP-LA-PI as a PP2A enhancer, and diDCP-LA-PC as a PTP1B enhancer.

【 授权许可】

CC BY-NC-ND