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Arrestin dependent activation of ERK1/2 in response to follicle stimulating hormone
Author(s) -
Chevalier Samantha,
Cohen Brian
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1031.16
Subject(s) - kinase , activator (genetics) , mapk/erk pathway , microbiology and biotechnology , protein kinase a , follicle stimulating hormone receptor , p38 mitogen activated protein kinases , chemistry , mitogen activated protein kinase , enzyme activator , biology , follicle stimulating hormone , receptor , medicine , endocrinology , signal transduction , hormone , biochemistry , luteinizing hormone
The human follicle stimulating hormone (hFSH) is a member of the glycoprotein hormone receptor family involved in regulating gametogenesis. When hFSH binds to its receptor it triggers the production of cAMP via adenylate cyclase and causes the activation of MAP kinases like p38 and ERK1/2. The goal of these experiments was to determine if MAP kinase activation was dependent on cAMP activation of protein kinase A. To characterize the role of PKA we used the inhibitor H89 and then investigated p38 and ERK1/2 activation in response to FSH. No effect was seen from H89 on p38 and ERK1/2 activation. In other labs, beta‐arrestin has been implicated as a potential activator of ERK1/2. To determine the role of beta‐arrestin in FSH induced MAP kinase activation we used short hairpin RNA (shRNA) to knockdown beta‐arrestin 1 and 2. When beta‐arrestin was knocked down ERK 1/2 activation was decreased and activation of p38 was unchanged. This suggests that there are two different activation pathways for p38 and p44/42. Understanding the mechanism of activation of the MAP kinases could lead to future advances in contraception or therapies for improvement of fertility.