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Updated: Sep 20, 2026

Mechanism of Regulation of Adipocyte Numbers in Adult Organisms Through Differentiation and Apoptosis Homeostasis
Published on: June 3, 2016
Protein kinase C-epsilon promotes adipogenic commitment and is essential for terminal differentiation of 3T3-F442A
P R Webb1, C Doyle, N G Anderson
1Division of Cancer Studies, University of Manchester, School of Medicine, Oxford Road, Manchester M13 9PT, United Kingdom.
Abstract:
The role of protein kinase C (PKC) isoforms in the commitment of multipotent fibroblasts to the adipocyte lineage and in their terminal differentiation into mature adipocytes was investigated. Ectopic overexpression of PKC-epsilon, but not other PKC isoforms, committed multipotent NIH-3T3 cells to adipogenic differentiation in the presence of hormonal inducers. In committed 3T3-F442A preadipocytes, PKC-epsilon protein expression increased during the course of terminal differentiation and cell-permeable PKC-epsilon inhibitory peptides, which prevent interaction with RACK (receptor for activated C-kinase) proteins, severely inhibited differentiation. PKC-epsilon accumulated in the nuclei of 3T3-F442A cells shortly after induction of differentiation and exhibited a distinctive punctate speckling immunocytochemical staining pattern. The spatiotemporal aspects of PKC-epsilon localization and expression coincided with that of C/EBP-beta, a transcription factor critically involved in promoting the early phase of adipogenesis. Collectively, these results demonstrate a role for PKC-epsilon in both adipogenic commitment and preadipocyte terminal differentiation.
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