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. 1990 Jun;87(12):4417–4420. doi: 10.1073/pnas.87.12.4417

Introduction of the beta isozyme of protein kinase C accelerates induced differentiation of murine erythroleukemia cells.

E Melloni 1, S Pontremoli 1, B Sparatore 1, M Patrone 1, F Grossi 1, P A Marks 1, R A Rifkind 1
PMCID: PMC54125  PMID: 2352925

Abstract

Induction of differentiation in murine erythroleukemia cells (MELCs) involves a protein kinase C (PKC)-mediated step. Vincristine-resistant cells respond more rapidly to hybrid polar/apolar inducers than the parental cells. These vincristine-resistant MELCs contain elevated levels of the beta isozyme of PKC (PKC-beta). Exogenous homologous murine PKC-beta, incorporated into permeabilized MELCs, accelerates induced differentiation. Neither rat PKC-beta, nor mouse PKC-alpha, nor rat PKC-alpha, incorporated into permeabilized MELCs, is effective in altering the kinetics of induced differentiation. This provides direct evidence for a rate-limiting role for this PKC isozyme during N,N'-hexamethylenebisacetamide-mediated induced differentiation of a transformed cell.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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