Protein kinase A activity is required for depolarization-induced proline-rich tyrosine kinase 2 and mitogen-activated protein kinase activation in PC12 cells

2000 ◽  
Vol 290 (1) ◽  
pp. 25-28 ◽  
Author(s):  
Jae Hong Park ◽  
Joong Kyu Park ◽  
Kee Won Bae ◽  
Hwan Tae Park
Keyword(s):  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Protein Kinase A ◽  
Pc12 Cells ◽  
Mitogen Activated Protein Kinase ◽  
Kinase Activation ◽  
Tyrosine Kinase 2 ◽  
Protein Kinase Activation ◽  
Mitogen Activated Protein ◽  
Kinase A

B-Raf-dependent regulation of the MEK-1/mitogen-activated protein kinase pathway in PC12 cells and regulation by cyclic AMP

1994 ◽  
Vol 14 (10) ◽  
pp. 6522-6530
Author(s):  
R R Vaillancourt ◽  
A M Gardner ◽  
G L Johnson
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Map Kinase ◽  
Protein Kinase A ◽  
Pc12 Cells ◽  
Kinase Activation ◽  
Mitogen Activated Protein ◽  
Epidermal Growth ◽  
Camp Levels ◽  
Kinase A

Growth factor receptor tyrosine kinase regulation of the sequential phosphorylation reactions leading to mitogen-activated protein (MAP) kinase activation in PC12 cells has been investigated. In response to epidermal growth factor, nerve growth factor, and platelet-derived growth factor, B-Raf and Raf-1 are activated, phosphorylate recombinant kinase-inactive MEK-1, and activate wild-type MEK-1. MEK-1 is the dual-specificity protein kinase that selectively phosphorylates MAP kinase on tyrosine and threonine, resulting in MAP kinase activation. B-Raf and Raf-1 are growth factor-regulated Raf family members which regulate MEK-1 and MAP kinase activity in PC12 cells. Protein kinase A activation in response to elevated cyclic AMP (cAMP) levels inhibited B-Raf and Raf-1 stimulation in response to growth factors. Ras.GTP loading in response to epidermal growth factor, nerve growth factor, or platelet-derived growth factor was unaffected by protein kinase A activation. Even though elevated cAMP levels inhibited Raf activation, the growth factor activation of MEK-1 and MAP kinase was unaffected in PC12 cells. The results demonstrate that tyrosine kinase receptor activation of MEK-1 and MAP kinase in PC12 cells is regulated by B-Raf and Raf-1, whose activation is inhibited by protein kinase A, and MEK activators, whose activation is independent of cAMP regulation.

scholarly journals B-Raf-dependent regulation of the MEK-1/mitogen-activated protein kinase pathway in PC12 cells and regulation by cyclic AMP.

1994 ◽  
Vol 14 (10) ◽  
pp. 6522-6530 ◽  
Author(s):  
R R Vaillancourt ◽  
A M Gardner ◽  
G L Johnson
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Map Kinase ◽  
Protein Kinase A ◽  
Pc12 Cells ◽  
Kinase Activation ◽  
Mitogen Activated Protein ◽  
Epidermal Growth ◽  
Camp Levels ◽  
Kinase A

Growth factor receptor tyrosine kinase regulation of the sequential phosphorylation reactions leading to mitogen-activated protein (MAP) kinase activation in PC12 cells has been investigated. In response to epidermal growth factor, nerve growth factor, and platelet-derived growth factor, B-Raf and Raf-1 are activated, phosphorylate recombinant kinase-inactive MEK-1, and activate wild-type MEK-1. MEK-1 is the dual-specificity protein kinase that selectively phosphorylates MAP kinase on tyrosine and threonine, resulting in MAP kinase activation. B-Raf and Raf-1 are growth factor-regulated Raf family members which regulate MEK-1 and MAP kinase activity in PC12 cells. Protein kinase A activation in response to elevated cyclic AMP (cAMP) levels inhibited B-Raf and Raf-1 stimulation in response to growth factors. Ras.GTP loading in response to epidermal growth factor, nerve growth factor, or platelet-derived growth factor was unaffected by protein kinase A activation. Even though elevated cAMP levels inhibited Raf activation, the growth factor activation of MEK-1 and MAP kinase was unaffected in PC12 cells. The results demonstrate that tyrosine kinase receptor activation of MEK-1 and MAP kinase in PC12 cells is regulated by B-Raf and Raf-1, whose activation is inhibited by protein kinase A, and MEK activators, whose activation is independent of cAMP regulation.

scholarly journals AMPN1-Oxide, a Unique Compound of Royal Jelly, Induces Neurite Outgrowth from PC12 Vells via Signaling by Protein Kinase A Independent of that by Mitogen-Activated Protein Kinase

2010 ◽  
Vol 7 (1) ◽  
pp. 63-68 ◽  
Author(s):  
Noriko Hattori ◽  
Hiroshi Nomoto ◽  
Hidefumi Fukumitsu ◽  
Satoshi Mishima ◽  
Shoei Furukawa
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Neurite Outgrowth ◽  
Neuronal Differentiation ◽  
Pc12 Cells ◽  
Royal Jelly ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Unique Compound ◽  
Kinase A

Earlier we identified adenosine monophosphate (AMP)N1-oxide as a unique compound of royal jelly (RJ) that induces neurite outgrowth (neuritegenesis) from cultured rat pheochromocytoma PC12 cells via the adenosine A2Areceptor. Now, we found that AMPN1-oxide stimulated the phosphorylation of not only mitogen-activated protein kinase (MAPK) but also that of cAMP/calcium-response element-binding protein (CREB) in a dose-dependent manner. Inhibition of MAPK activation by a MEK inhibitor, PD98059, did not influence the AMPN1-oxide-induced neuritegenesis, whereas that of protein kinase A (PKA) by a selective inhibitor, KT5720, significantly reduced neurite outgrowth. AMPN1-oxide also had the activity of suppressing the growth of PC12 cells, which correlated well with the neurite outgrowth-promoting activity. KT5720 restored the growth of AMPN1-oxide-treated PC12 cells. It is well known that nerve growth factor suppresses proliferation of PC12 cells before causing stimulation of neuronal differentiation. Thus, AMPN1-oxide elicited neuronal differentiation of PC12 cells, as evidenced by generation of neurites, and inhibited cell growth through adenosine A2Areceptor-mediated PKA signaling, which may be responsible for characteristic actions of RJ.

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