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ORIGINAL ARTICLE
Year : 2020  |  Volume : 63  |  Issue : 4  |  Page : 179-186

Novel regulation of PKC-induced inflammation by Akt and protein phosphatase 2A in ovarian granulosa cells


1 Department of Physiology, School of Medicine, National Yang-Ming University, Taipei, Taiwan
2 Department of Obstetrics and Gynecology, Cheng Hsin General Hospital, Taipei, Taiwan

Correspondence Address:
Prof. Yuh-Lin Wu
Room 405, Shouren Building, National Yang-Ming University, No 155, Sec. 2, Linong Street, Taipei City 112
Taiwan
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Source of Support: This research was supported by grants from the Ministry of Science and Technology (MOST 105-2320-B-010-026-MY3; MOST 108-2320-B-010-025), the Cheng Hsin General Hospital (CY10603; CY10802), and the Taiwan Ministry of Education Aim for the Top University Plan., Conflict of Interest: None


DOI: 10.4103/CJP.CJP_44_20

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PKC-mediated inflammation is important in ovarian physiology. The roles of Akt and protein phosphatase 2A (PP2A) in PKC-mediated inflammation in ovarian granulosa cells (GCs) remain mostly unclear. PKC activator phorbol 12-myristate 13-acetate induced the Akt phosphorylation in rat primary GCs but reduced the Akt phosphorylation in KGN human GCs. In rat GCs, an inhibitory effect of PI3K inhibitor wortmannin and a stimulatory effect of Akt activator SC79 on PKC-induced cyclooxygenase-2 (COX-2)/PGE2production were noted; wortmannin and SC79 acted oppositely in human GCs. In rat GCs, PP2A inhibitor okadaic acid further enhanced the PKC-mediated promoter activation and elevation of mRNA and protein levels of the COX-2 gene, whereas PP2A activator sodium selenate attenuated the PKC-mediated COX-2 expression and promoter activation. PKC activation did not affect PP2A phosphorylation, but okadaic acid indeed augmented the PKC-induced NF-κB nuclear translocation. Thus, PP2A appears to act as a negative modulator in PKC-mediated cellular inflammation in rat GCs, at least in part due to its attenuating effect on the PKC-induced NF-κB activation.


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