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 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

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 The role of mitogen-activated protein kinase–extracellular receptor kinase pathway in female fertility outcomes: a focus on pituitary gonadotropins regulation

2018 ◽  
Vol 9 (7) ◽  
pp. 209-215 ◽  
Author(s):  
Samira Kahnamouyi ◽  
Mohammad Nouri ◽  
Laya Farzadi ◽  
Masoud Darabi ◽  
Vahid Hosseini ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Ovarian Function ◽  
Vascular System ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Pituitary Cells ◽  
Gonadotropin Secretion ◽  
Α Subunit ◽  
Mitogen Activated Protein ◽  
Main Components

Mammalian reproduction systems are largely regulated by the secretion of two gonadotropins, that is, luteinizing hormone (LH) and follicle-stimulating hormone (FSH). The main action of LH and FSH on the ovary is to stimulate secretion of estradiol and progesterone, which play an important role in the ovarian function and reproductive cycle control. FSH and LH secretions are strictly controlled by the gonadotropin-releasing hormone (GnRH), which is secreted from the hypothalamus into the pituitary vascular system. Maintaining normal secretion of LH and FSH is dependent on pulsatile secretion of GnRH. Extracellular signal-regulated kinase (ERK) proteins, as the main components of mitogen-activated protein kinase (MAPK) signaling pathways, are involved in the primary regulation of GnRH-stimulated transcription of the gonadotropins’ α subunit in the pituitary cells. However, GnRH-stimulated expression of the β subunit has not yet been reported. Furthermore, GnRH-mediated stimulation of ERK1 and ERK2 leads to several important events such as cell proliferation and differentiation. In this review, we briefly introduce the relationship between ERK signaling and gonadotropin secretion, and its importance in female infertility.

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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