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N‐myc disrupts protein kinase C‐mediated signal transduction in neuroblastoma.
Author(s) -
Bernards R.
Publication year - 1991
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1991.tb08052.x
Subject(s) - neuroblastoma , biology , protein kinase c , microbiology and biotechnology , signal transduction , protein kinase a , gene isoform , transfection , kinase , phorbol , gene , cancer research , cell culture , genetics
In neuroblastoma, amplification of the N‐myc gene is closely correlated with increased metastatic ability. The mechanism by which N‐myc acts to increase neuroblastoma malignancy is poorly understood as yet. It is shown here that transfection of N‐myc in a neuroblastoma cell line causes suppression of one isoform of protein kinase C, named delta, and induction of an unusual type of protein kinase C, named zeta. N‐myc‐transfected neuroblastoma cells were found to be blocked in the activation of both c‐fos mRNA and the NF‐kappa B transcription factor by phorbol ester. Introduction of a protein kinase C expression vector in N‐myc transfected neuroblastoma cells restored inducibility of both c‐fos and NF‐kappa B by phorbol ester. These observations indicate that changes in protein kinase C gene expression significantly alter the response of N‐myc‐amplified neuroblastomas to a variety of external signals.