Rapid activation of MAP kinase by estrogen in the bone cell line
H Endoh, H Sasaki, K Maruyama, K Takeyama… - Biochemical and …, 1997 - Elsevier
H Endoh, H Sasaki, K Maruyama, K Takeyama, I Waga, T Shimizu, S Kato, H Kawashima
Biochemical and biophysical research communications, 1997•ElsevierWe examined the effect of estrogen on mitogen-activated protein kinase (MAPK) in
osteoblastic cells. Rat ROS 17/2.8 cells were exposed to 17β-estradiol (E2) and MAPK
activity in the cells was measured by anin vitrophosphorylation assay. E2treatment caused a
rapid and transient MAPK activation within 5 min. Insulin-like growth factor-I, which acts via
their membrane receptors, caused a similar effect, but it required 10 min to reach the
maximum level. Western blot analyses with anti-MAPK and anti-phosphotyrosine antibodies …
osteoblastic cells. Rat ROS 17/2.8 cells were exposed to 17β-estradiol (E2) and MAPK
activity in the cells was measured by anin vitrophosphorylation assay. E2treatment caused a
rapid and transient MAPK activation within 5 min. Insulin-like growth factor-I, which acts via
their membrane receptors, caused a similar effect, but it required 10 min to reach the
maximum level. Western blot analyses with anti-MAPK and anti-phosphotyrosine antibodies …
We examined the effect of estrogen on mitogen-activated protein kinase (MAPK) in osteoblastic cells. Rat ROS 17/2.8 cells were exposed to 17β-estradiol (E2) and MAPK activity in the cells was measured by anin vitrophosphorylation assay. E2treatment caused a rapid and transient MAPK activation within 5 min. Insulin-like growth factor-I, which acts via their membrane receptors, caused a similar effect, but it required 10 min to reach the maximum level. Western blot analyses with anti-MAPK and anti-phosphotyrosine antibodies demonstrated that the E2activation of MAPK was accompanied by phosphorylation of the enzyme. The concentration range (10 nM-1 pM) of E2needed for this MAPK activation was less than that (1 μM-0.1 nM) needed for the transcriptional activation via the nuclear estrogen receptor (ER). These data provide the first evidence of MAPK activation by E2through phosphorylation, which may be mediated through a putative plasma membrane receptor in the cultured bone cells.
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