Stimulation of Mitogen-Activated Protein Kinase Pathway in Rat Somatotrophs by Growth Hormone-Releasing Hormone

Endocrine ◽  
2000 ◽  
Vol 12 (3) ◽  
pp. 257-264 ◽  
Author(s):  
Philip Zeitler ◽  
Gamini Siriwardana
Keyword(s):  
Growth Hormone ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Growth Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Mitogen Activated Protein ◽  
Kinase Pathway ◽  
Stimulation Of

scholarly journals Growth Hormone-Releasing Hormone Stimulates Mitogen-Activated Protein Kinase*

Endocrinology ◽  
2000 ◽  
Vol 141 (6) ◽  
pp. 2113-2119 ◽  
Author(s):  
Celia M. Pombo ◽  
Juan Zalvide ◽  
Bruce D. Gaylinn ◽  
Carlos Diéguez
Keyword(s):  
Growth Hormone ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Growth Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Mitogen Activated Protein

Peptides Derived from Pro-Growth Hormone-Releasing Hormone Activate p38 Mitogen-Activated Protein Kinase in GH3 Pituitary Cells

Endocrine ◽  
2001 ◽  
Vol 15 (1) ◽  
pp. 119-128 ◽  
Author(s):  
Rosemary Steinmetz ◽  
Pingyu Zeng ◽  
Denise Walker King ◽  
Emily Walvoord ◽  
Ora Hirsch Pescovitz
Keyword(s):  
Growth Hormone ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Pituitary Cells ◽  
Growth Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Mitogen Activated Protein

scholarly journals Proinsulin C-peptide activates cAMP response element-binding proteins through the p38 mitogen-activated protein kinase pathway in mouse lung capillary endothelial cells

2002 ◽  
Vol 366 (3) ◽  
pp. 737-744 ◽  
Author(s):  
Takanori KITAMURA ◽  
Kazuhiro KIMURA ◽  
Bae Dong JUNG ◽  
Kennedy MAKONDO ◽  
Naoki SAKANE ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Mouse Lung ◽  
Camp Response Element ◽  
Site Specific ◽  
C Peptide ◽  
Mitogen Activated Protein ◽  
Capillary Endothelial Cells ◽  
Kinase Pathway ◽  
Stimulation Of

Proinsulin C-peptide has been reported to have some biological activities and to be possibly involved in the development of diabetic microangiopathy. In the present study, we examined the effects of C-peptide on the mitogen-activated protein kinase pathway in LEII mouse lung capillary endothelial cells. Stimulation of the cells with C-peptide increased both p38 mitogen-activated protein kinase (p38MAPK) and extracellular signal-regulated kinase (ERK1/2) activities and activity-related site-specific phosphorylation of the respective kinases in a concentration-dependent manner, but failed to activate c-Jun N-terminal kinase. Stimulation of the cells with C-peptide also induced site-specific phosphorylation of cAMP response element (CRE)-binding protein (CREB)/activating transcription factor 1 (ATF1), and thereby binding of these transcription factors to CRE. Among three CREB kinases tested, phosphorylation of mitogen-activated protein kinase-activated protein kinase 2 (MAPKAP-K2) was induced after stimulation with C-peptide. The phosphorylation of CREB, ATF1 and MAPKAP-K2 were inhibited by SB203580, a p38MAPK inhibitor, but not by PD98059, an ERK kinase inhibitor. These results indicate that C-peptide activates p38MAPK followed by MAPKAP-K2 to enhance DNA—CREB/ATF1 interactions.

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