scholarly journals Melia toosendan Regulates PC12 Cell Differentiation via the Activation of Protein Kinase A and Extracellular Signal-Regulated Kinases

Neurosignals ◽  
2004 ◽  
Vol 13 (5) ◽  
pp. 248-257 ◽  
Author(s):  
Jowie C.H. Yu ◽  
Zhi-da Min ◽  
Nancy Y. Ip
Keyword(s):  
Cell Differentiation ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Pc12 Cell ◽  
Extracellular Signal ◽  
Kinase A

scholarly journals Constitutively Active Protein Kinase A Qualitatively Mimics the Effects of Follicle-Stimulating Hormone on Granulosa Cell Differentiation

2008 ◽  
Vol 22 (8) ◽  
pp. 1842-1852 ◽  
Author(s):  
Rosalba Escamilla-Hernandez ◽  
Lynda Little-Ihrig ◽  
Kyle E. Orwig ◽  
Junming Yue ◽  
Uma Chandran ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Granulosa Cell ◽  
Follicle Stimulating Hormone ◽  
Active Protein ◽  
Kinase A ◽  
Constitutively Active ◽  
Stimulating Hormone

scholarly journals The Lutropin/Choriogonadotropin Receptor-Induced Phosphorylation of the Extracellular Signal-Regulated Kinases in Leydig Cells Is Mediated by a Protein Kinase A-Dependent Activation of Ras

2003 ◽  
Vol 17 (11) ◽  
pp. 2189-2200 ◽  
Author(s):  
Takashi Hirakawa ◽  
Mario Ascoli
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Leydig Cells ◽  
Primary Cultures ◽  
Nucleotide Exchange ◽  
Camp Phosphodiesterase ◽  
Human Choriogonadotropin ◽  
Extracellular Signal ◽  
Guanosine Triphosphatase ◽  
Kinase A

Abstract The pathways involved in activation of the ERK1/2 cascade in Leydig cells were examined in MA-10 cells expressing the recombinant human LH receptor (hLHR) and in primary cultures of rat Leydig cell precursors. In MA-10 cells expressing the recombinant hLHR, human choriogonadotropin-induced activation of ERK1/2 is effectively inhibited by overexpression of a cAMP phosphodiesterase (a manipulation that blunts the human choriogonadotropin-induced cAMP response), by addition of H89 (a selective inhibitor of protein kinase A), or by overexpression of the heat-stable protein kinase A inhibitor, but not by overexpression of an inactive mutant of this inhibitor. Stimulation of hLHR did not activate Rap1, but activated Ras in an H89-sensitive fashion. Addition of H89 to MA-10 cells that had been cotransfected with a guanosine triphosphatase-deficient mutant of Ras almost completely inhibited the hLHR-mediated activation of ERK1/2. We also show that 8-bromo-cAMP activates Ras and ERK1/2 in MA-10 cells and in primary cultures of rat Leydig cells precursors in an H89-sensitive fashion, whereas a cAMP analog 8-(4-chloro-phenylthio)-2′-O-methyl-cAMP (8CPT-2Me-cAMP) that is selective for cAMP-dependent guanine nucleotide exchange factor has no effect. Collectively, our results show that the hLHR-induced phosphorylation of ERK1/2 in Leydig cells is mediated by a protein kinase A-dependent activation of Ras.

Sign in / Sign up

Export Citation Format

Share Document