scholarly journals Janus Kinase 2-dependent Activation of p38 Mitogen-activated Protein Kinase by Growth Hormone

2000 ◽  
Vol 275 (3) ◽  
pp. 2103-2114 ◽  
Author(s):  
Tao Zhu ◽  
Peter E. Lobie
Keyword(s):  
Growth Hormone ◽  
Protein Kinase ◽  
Janus Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Janus Kinase 2 ◽  
Mitogen Activated Protein

Mechanism of signaling by growth hormone receptor

1996 ◽  
Vol 76 (4) ◽  
pp. 1089-1107 ◽  
Author(s):  
L. S. Argetsinger ◽  
C. Carter-Su
Keyword(s):  
Growth Hormone ◽  
Protein Kinase ◽  
Growth Hormone Receptor ◽  
Second Messengers ◽  
Current Model ◽  
Mitogen Activated Protein Kinase ◽  
Gh Receptor ◽  
Insulin Receptor Substrates ◽  
Mitogen Activated Protein ◽  
Control Body

Growth hormone (GH) has long been known to stimulate linear growth and regulate metabolism. The cellular mechanism by which GH elicits these effects has only recently begun to be understood. This review provides an overview of a current model of GH signaling. Briefly, binding of GH to GH receptor induces receptor dimerization and activation of the tyrosine kinase JAK2. Tyrosyl phosphorylation of GH receptor and JAK2 recruits and activates signaling molecules such as Stat transcription factors, SHC, and insulin receptor substrates 1 and 2 that lead to the release of second messengers such as diacylglycerol, calcium, and nitric oxide and the activation of enzymes such as mitogen-activated protein kinase, protein kinase C, phospholipase A2, and phosphatidylinositol 3'-kinase. These pathways regulate cellular function including gene transcription, metabolite transport, and enzymatic activity that result in the ability of GH to control body growth and metabolism.

scholarly journals Growth hormone activates mitogen-activated protein kinase and S6 kinase and promotes intracellular tyrosine phosphorylation in 3T3-F442A preadipocytes

1992 ◽  
Vol 284 (3) ◽  
pp. 649-652 ◽  
Author(s):  
N G Anderson
Keyword(s):  
Growth Hormone ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Phorbol Esters ◽  
Mitogen Activated Protein Kinase ◽  
S6 Kinase ◽  
Kinase C ◽  
Transient Activation ◽  
Mitogen Activated Protein

Physiological concentrations of growth hormone induced a rapid and transient activation of mitogen-activated protein kinase (MAP kinase) and S6 kinase in 3T3-F442A preadipocytes. These effects were abrogated by staurosporine and in cells chronically pretreated with phorbol esters, suggesting that protein kinase C is involved in the mechanism of activation. In addition, three cytosolic proteins exhibited a growth-hormone-dependent increase in tyrosine phosphorylation.

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