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Nucleic Acids Research, 1990, Vol. 18, No. 12 3605-3610
© 1990

MOLECULAR BIOLOGY

Unusual c-fos induction upon chromaffin PC12 differentiation by sodium butyrate: loss of fos autoregulatory function

Jose R. Naranjo1,2, Britt Mellström1,2, Johan Auwerx2, Faustino Mollinedo3 and Paolo Sassone-Corsi2,*

1Instituto Cajal de Neurociencia, Consejo Superior Investigaciones Cientificas Av. Doctor Arce 37, 28002 Madrid, Spain 2Laboratoire de Genetique Moleculaire des Eucaryotes, CNRS 11 rue Humann, 67085 Strasbourg Cedex, France 3Centro Investigaciones Biologicas, CSIC C/ Velazquez 144, 28006 Madrid, Spain

*To whom correspondence should be addressed

Received February 8, 1990. Revised May 11, 1990. Accepted May 11, 1990.

Induction of PC12 pheochromocytoma cells neuronal differentiation upon treatment with nerve growth factor (NGF) is accompanied by a coupled stimulation of c-fos and c-jun oncogene transcription. We found that induction of c-fos and c-jun proto-oncogene mRNAs levels following the endocrine differentiation of PC12 cells by sodium butyrate is uncoupled. While c-fos mRNA level increased within minutes, the content of c-jun mRNA was significantly elevated only 24 hours after treatment. Continuous presence of sodium butyrate for 72 hours resulted in stable high levels of c-fos and c-jun mRNAs. Gene transcription of the other members of the jun family, jun B and jun D, was not significantly modified at any induction time. The early accumulation of c-fos mRNA was accompanied by increased levels of c-Fos protein. While the NGF-induced c-Fos protein migrates with an apparent homogeneous molecular weight of 62 kDa, the sodium butyrate-stimulated Fos protein is of heterogeneous lower molecular weight. The different gel mobility of the Fos immunoreactive bands induced by sodium butyrate and the sustained Fos mRNA levels after induction suggested that the sodium butyrate-induced c-Fos protein could be non-functional in the autoregulation of the c-fos gene. Gel shift analysis showed unimpaired capacity of the butyrate-induced c-Fos protein to participate in the formation of transcriptional complexes with the Jun/AP-1 protein. However, transfection experiments indicate that the sodium butyrate-induced c-Fos protein is not able to negatively trans-regulate the c-fos promoter.


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