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Exp Cell Res. 1996 Jun 15;225(2):366-73.

Protein kinase C-delta associates with vimentin intermediate filaments in differentiated HL60 cells.

Author information

1
Department of Immunology, Birmingham University Medical School, United Kingdom.

Abstract

The subcellular localization of protein kinase C (PKC)-delta was determined in HL60 cells differentiated toward monocytes/macrophages by treatment with TPA. PKC-delta was detected in the nucleus and cytoplasm of differentiated HL60 cells and, more specifically, associated with structures resembling intermediate filaments. Indirect immunostaining revealed that PKC-delta colocalized with vimentin in the cytosol and perinuclear region of these cells. Immunoprecipitation studies showed that PKC-delta was in an active (autophosphorylated) state in differentiated HL60 cells and that vimentin immunoprecipitated from these cells was also phosphorylated. Treatment of HL60 cells with the PKC-specific inhibitor chelerythrine decreased the phosphorylation of vimentin. These data suggest that vimentin is a substrate for PKC-delta and that this PKC isoenzyme may play a specific role in the regulation of shape change and cell adhesion during HL60 differentiation.

PMID:
8660925
DOI:
10.1006/excr.1996.0187
[Indexed for MEDLINE]

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