Bacopa monnieri and l-Deprenyl Differentially Enhance the Activities of Antioxidant Enzymes and the Expression of Tyrosine Hydroxylase and Nerve Growth Factor via ERK 1/2 and NF-κB Pathways in the Spleen of Female Wistar Rats

2012 ◽  
Vol 38 (1) ◽  
pp. 141-152 ◽  
Author(s):  
Hannah P. Priyanka ◽  
Preetam Bala ◽  
Sindhu Ankisettipalle ◽  
Srinivasan ThyagaRajan
Keyword(s):  
Antioxidant Enzymes ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Tyrosine Hydroxylase ◽  
Wistar Rats ◽  
Bacopa Monnieri ◽  
Nerve Growth ◽  
Female Wistar Rats

NERVE GROWTH FACTOR AND THE ACTIVITY OF TYROSINE HYDROXYLASE IN ORGAN CULTURES OF RAT SUPERIOR CERVICAL GANGLIA

1977 ◽  
Vol 28 (4) ◽  
pp. 835-842 ◽  
Author(s):  
M. W. Yu ◽  
B. Nikodijevic ◽  
J. Lakshmanan ◽  
V. Rowe ◽  
P. MacDonnell ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Tyrosine Hydroxylase ◽  
Organ Cultures ◽  
Superior Cervical Ganglia ◽  
Nerve Growth ◽  
Cervical Ganglia

scholarly journals Nerve growth factor action is mediated by cyclic AMP- and Ca+2/phospholipid-dependent protein kinases.

1986 ◽  
Vol 103 (3) ◽  
pp. 887-893 ◽  
Author(s):  
J Cremins ◽  
J A Wagner ◽  
S Halegoua
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Tyrosine Hydroxylase ◽  
Protein Kinase ◽  
Enzyme Activation ◽  
Dependent Protein Kinase ◽  
Nerve Growth ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Dose Dependent

Nerve growth factor (NGF) mediates the phosphorylation of tyrosine hydroxylase in PC12 cells on two distinct peptide fragments, separable by two-dimensional tryptic phosphopeptide mapping (phosphopeptides T1 and T3). Phorbol diester derivatives capable of activating Ca+2/phospholipid-dependent protein kinase (C-kinase) cause a specific phosphorylation of peptide T3 in a dose-dependent, saturable manner. Derivatives of the endogenous C-kinase activator diacylglycerol, also cause the phosphorylation of tyrosine hydroxylase on peptide T3. The C-kinase inhibitors chlorpromazine and trifluoperazine inhibit the phorbol diester stimulated phosphorylation of site T3 in a dose-dependent manner. These agents inhibit the phosphorylation of T3 in response to NGF, but have no effect on NGF's ability to cause T1 phosphorylation. In a PC12 mutant deficient in cAMP-dependent protein kinase activity, NGF mediates the phosphorylation of tyrosine hydroxylase on peptide T3 but not on T1. We conclude that NGF mediates the activation of both the cAMP-dependent protein kinase and the C-kinase to phosphorylate substrate proteins. These kinases can act independently to phosphorylate tyrosine hydroxylase, each at a different site, and each of which results in the enzyme activation. A molecular framework is thus provided for events underlying NGF action.

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