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FSH can induce ERK activation in a cAMP independent manner
Author(s) -
Curtis Chelsea L,
Cohen Brian D
Publication year - 2012
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.26.1_supplement.601.4
Subject(s) - adenylyl cyclase , mapk/erk pathway , protein kinase a , camp dependent pathway , chemistry , signal transduction , stimulation , kinase , gs alpha subunit , microbiology and biotechnology , receptor , follicle stimulating hormone receptor , endocrinology , medicine , follicle stimulating hormone , hormone , biology , luteinizing hormone , biochemistry
When human follicle stimulating hormone (hFSH) binds to its receptor (hFSHR) it signals through the Gs alpha protein leading to an increase in cyclic AMP (via adenylyl cyclase) which activates protein kinase A (PKA). In addition to this canonical pathway, activation of both the p38 and p44/42 (ERK1) MAP kinases has also been demonstrated in response to FSH. Previous research in our lab has demonstrated that when cells are treated with the cholesterol depleting agent methyl beta‐cyclodextrin it blocks FSH stimulation of adenylyl cyclase but not the activation of ERK1. Surprisingly, when cells were treated with H89, an inhibitor of PKA, FSH induced ERK1 activation was decreased. When these two treatments were combined, FSH induced ERK1 activation was restored. These seemingly inconsistent findings suggest an alternate pathway of activation for ERK1 that is regulated by cyclic AMP but PKA independent. The identification of the regulators in this alternate pathway could lead to new therapies for regulating reproduction.