Regulation of Neuropeptide Y Transcription and mRNA Levels by Nerve Growth Factor, Glucocorticoids, Cyclic AMP, and Phorbol Ester in PC12 Cells

1990 ◽  
Vol 611 (1 Central and P) ◽  
pp. 376-377 ◽  
Author(s):  
STEVEN L. SABOL ◽  
HIROSHI HIGUCHI
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Cyclic Amp ◽  
Neuropeptide Y ◽  
Pc12 Cells ◽  
Phorbol Ester ◽  
Mrna Levels ◽  
Nerve Growth

Short- and long-term mechanisms of tau regulation in PC12 cells

1995 ◽  
Vol 108 (8) ◽  
pp. 2857-2864 ◽  
Author(s):  
E. Sadot ◽  
J. Barg ◽  
D. Rasouly ◽  
P. Lazarovici ◽  
I. Ginzburg
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Pc12 Cells ◽  
Tau Protein ◽  
Immunoblot Analysis ◽  
Term Treatment ◽  
Mrna Levels ◽  
Short Term Treatment ◽  
Nerve Growth ◽  
Protein Levels

Induction by nerve growth factor of neurite outgrowth in PC12 cells is transcription-dependent and is associated with the accumulation of tau protein. It was recently shown that short-term treatment with staurosporine, a protein kinase alkaloid inhibitor, induced an elevation of tau protein levels and outgrowth of stable neurites. In this study, we analyzed the mechanism(s) by which nerve growth factor and staurosporine exert their effects on tau levels. We demonstrate that nerve growth factor affects tau mRNA stability, thus contributing to the observed increase in tau mRNA levels. On the other hand, tau mRNA levels were not affected by the treatment with staurosporine. We also demonstrate that the phosphorylation of tau protein was reduced after treatment of PC12 cells with nerve growth factor or staurosporine, as shown by immunoblot analysis using specific antibodies and alkaline phosphatase treatment. Thus, regulation of tau levels by nerve growth factor appears to be mediated by transcriptional, post-transcriptional and posttranslational steps, whereas the effect of staurosporine on tau levels may be attributed to its effect on the state of phosphorylation of the protein.

Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc, and actin gene transcription

1986 ◽  
Vol 6 (4) ◽  
pp. 1050-1057
Author(s):  
M E Greenberg ◽  
A L Hermanowski ◽  
E B Ziff
Keyword(s):  
Protein Synthesis ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Pc12 Cells ◽  
Gene Transcription ◽  
Actin Gene ◽  
Mrna Levels ◽  
Protein Synthesis Inhibitors ◽  
3T3 Cells ◽  
Nerve Growth

Stimulation of quiescent 3T3 cells with purified growth factors or of the pheochromocytoma cell line PC12 with nerve growth factor results in the rapid transient induction of c-fos, c-myc, and actin gene transcription (M.E. Greenberg and E.B. Ziff, Nature [London] 312:711-716; M.E. Greenberg, L.A. Greene, and E.B. Ziff, J. Biol. Chem. 26:14101-14110). We used protein synthesis inhibitors to investigate whether synthesis of new proteins plays a role in the rapid induction and subsequent repression of the transcription of these genes. Pretreatment of quiescent 3T3 cells with the inhibitor anisomycin before growth factor stimulation caused a superinduction of c-fos and c-myc mRNA levels upon growth factor addition. Nuclear runoff transcription analyses of 3T3 cells indicated that anisomycin potentiated c-fos, c-myc, and also actin expression at the transcriptional level, possibly by inhibiting transcriptional repression. Somewhat different results were obtained when PC12 cells were incubated with either anisomycin or cycloheximide. In PC12 cells protein synthesis inhibitors superinduced nerve growth factor activation of c-fos mRNA production but completely abolished the activation of c-myc. The results suggest that in PC12 cells c-fos transcription is activated by a protein-synthesis-independent mechanism, whereas c-myc stimulation requires new protein synthesis. The difference in the effect of anisomycin on growth factor activation of c-myc expression in 3T3 versus PC12 cells may be due to differential stringency of protein synthesis inhibition in the two cells or could reflect cell type differences in c-myc regulation.

Mechanisms of apoptosis in PC12 cells irreversibly differentiated with nerve growth factor and cyclic AMP

1999 ◽  
Vol 821 (1) ◽  
pp. 60-68 ◽  
Author(s):  
Nathalie Lambeng ◽  
Patrick P Michel ◽  
Bernard Brugg ◽  
Yves Agid ◽  
Merle Ruberg
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Cyclic Amp ◽  
Pc12 Cells ◽  
Nerve Growth

scholarly journals Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc, and actin gene transcription.

1986 ◽  
Vol 6 (4) ◽  
pp. 1050-1057 ◽  
Author(s):  
M E Greenberg ◽  
A L Hermanowski ◽  
E B Ziff
Keyword(s):  
Protein Synthesis ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Pc12 Cells ◽  
Gene Transcription ◽  
Actin Gene ◽  
Mrna Levels ◽  
Protein Synthesis Inhibitors ◽  
3T3 Cells ◽  
Nerve Growth

Stimulation of quiescent 3T3 cells with purified growth factors or of the pheochromocytoma cell line PC12 with nerve growth factor results in the rapid transient induction of c-fos, c-myc, and actin gene transcription (M.E. Greenberg and E.B. Ziff, Nature [London] 312:711-716; M.E. Greenberg, L.A. Greene, and E.B. Ziff, J. Biol. Chem. 26:14101-14110). We used protein synthesis inhibitors to investigate whether synthesis of new proteins plays a role in the rapid induction and subsequent repression of the transcription of these genes. Pretreatment of quiescent 3T3 cells with the inhibitor anisomycin before growth factor stimulation caused a superinduction of c-fos and c-myc mRNA levels upon growth factor addition. Nuclear runoff transcription analyses of 3T3 cells indicated that anisomycin potentiated c-fos, c-myc, and also actin expression at the transcriptional level, possibly by inhibiting transcriptional repression. Somewhat different results were obtained when PC12 cells were incubated with either anisomycin or cycloheximide. In PC12 cells protein synthesis inhibitors superinduced nerve growth factor activation of c-fos mRNA production but completely abolished the activation of c-myc. The results suggest that in PC12 cells c-fos transcription is activated by a protein-synthesis-independent mechanism, whereas c-myc stimulation requires new protein synthesis. The difference in the effect of anisomycin on growth factor activation of c-myc expression in 3T3 versus PC12 cells may be due to differential stringency of protein synthesis inhibition in the two cells or could reflect cell type differences in c-myc regulation.

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