Regulation of protein kinase C in NG108-15 cell differentiation.

Journal Article

The involvement of PKC in NG108-15 cell differentiation was investigated. Differentiation with dBcAMP was associated with a decrease in total cellular phorbol ester binding. The histone-directed PKC activity was decreased in the soluble fraction. Northern and Western blotting revealed the presence of only PKC alpha but not PKC beta and PKC gamma among the calcium-dependent isoforms. Differentiation induced a decrease of cytosolic PKC alpha immunoreactivity, with no changes of mRNA content or appearance of PKC beta and PKC gamma isoforms. The low levels of PKC alpha in the soluble fraction suggest that the mRNA for this species is less efficiently translated in differentiated NG108-15 cells. The data suggest that down-regulation of PKC alpha protein and kinase activity are associated with induction of neuronal morphology in NG108-15 cells.

Full Text

Duke Authors

Cited Authors

  • Battaini, F; Garbillo, G; Bergamaschi, S; Parenti, M; Wetsel, WC; Govoni, S; Trabucchi, M

Published Date

  • May 30, 1994

Published In

Volume / Issue

  • 201 / 1

Start / End Page

  • 135 - 142

PubMed ID

  • 8198566

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1994.1679

Language

  • eng

Conference Location

  • United States