Changes in PRL Gene Expression During Upstream Movement of the Japanese Eel, Anguilla japonica

2019 ◽  
Vol 36 (6) ◽  
pp. 521
Author(s):  
Takashi Yada ◽  
Nobuto Fukuda ◽  
Michihisa Abe ◽  
Katsumi Tsukamoto
2012 ◽  
Vol 29 (3) ◽  
pp. 204-211 ◽  
Author(s):  
Yukinori Kazeto ◽  
Mayuko Kohara ◽  
Ryota Tosaka ◽  
Koichiro Gen ◽  
Masahito Yokoyama ◽  
...  

2012 ◽  
Vol 16 (4) ◽  
pp. 289-294 ◽  
Author(s):  
Min Seop Choi ◽  
Se Ryun Kwon ◽  
Seong Hee Choi ◽  
Hyuk Chu Kwon

2002 ◽  
Vol 68 (sup1) ◽  
pp. 959-960 ◽  
Author(s):  
YUICHI OZAKI ◽  
HARUHISA FUKADA ◽  
YUKINORI KAZETO ◽  
SHINJI ADACHI ◽  
AKIHIKO HARA ◽  
...  

2010 ◽  
Vol 1 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Yi-Fan Chen ◽  
Shan-Ru Jeng ◽  
Ming-Chyuan Chen ◽  
Jin-Chywan Gwo ◽  
Yung-Sen Huang

2003 ◽  
Vol 17 (10) ◽  
pp. 1921-1930 ◽  
Author(s):  
Twila A. Jackson ◽  
David M. Koterwas ◽  
Melissa A. Morgan ◽  
Andrew P. Bradford

Abstract Fibroblast growth factors (FGFs) play a critical role in pituitary development and in pituitary tumor formation and progression. We have previously characterized FGF signal transduction and regulation of the tissue-specific rat prolactin (rPRL) promoter in GH4 pituitary cells. FGF induction of rPRL transcription is independent of Ras, but mediated by a protein kinase C-δ (PKCδ)-dependent activation of MAPK (ERK). Here we demonstrate a functional role for the Rho family monomeric G protein, Rac1, in FGF regulation of PRL gene expression via an atypical signaling pathway. Expression of dominant negative Rac, but not RhoA or Cdc42, selectively inhibited FGF-induced rPRL promoter activity. Moreover, expression of dominant negative Rac also attenuated FGF-2 and FGF-4 stimulation of MAPK (ERK). However, in contrast to other Rac-dependent signaling pathways, FGF activation of rPRL promoter activity was independent of the c-Jun N-terminal kinase (JNK) and phosphoinositide 3-kinase/Akt cascades. FGFs failed to activate JNK1 or JNK2, and expression of dominant negative JNK or Akt constructs did not block FGF-induced PRL transcription. Consistent with the role of PKCδ in FGF regulation of PRL gene expression, activation of the rPRL promoter was blocked by an inhibitor of phospholipase Cγ (PLCγ) activity. FGF treatment also induced rapid tyrosine phosphorylation of PLCγ in a Rac-dependent manner. These results suggest that FGF-2 and FGF-4 activate PRL gene expression via a novel Rac1, PLCγ, PKCδ, and ERK cascade, independent of phosphoinositol-3-kinase and JNK.


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