Involvement of prostaglandin endoperoxide H synthase-2 in osteoclast-like cell formation induced by interleukin-1β

2009 ◽  
Vol 11 (3) ◽  
pp. 392-400 ◽  
Author(s):  
Takahiro Sato ◽  
Ikuo Morita ◽  
Kouji Sakaguchi ◽  
Ken-Ichi Nakahama ◽  
William L. Smith ◽  
...  
Keyword(s):  
Cell Formation ◽  
Interleukin 1Β ◽  
Prostaglandin Endoperoxide ◽  
Endoperoxide H Synthase

scholarly journals Fatty Acid Substrate Specificities of Human Prostaglandin-endoperoxide H Synthase-1 and −2

1995 ◽  
Vol 270 (33) ◽  
pp. 19330-19336 ◽  
Author(s):  
Odette Laneuville ◽  
Debra K. Breuer ◽  
Naxing Xu ◽  
Z. H. Huang ◽  
Douglas A. Gage ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Substrate ◽  
Substrate Specificities ◽  
Prostaglandin Endoperoxide ◽  
Endoperoxide H Synthase ◽  
Acid Substrate

scholarly journals Tumour necrosis factor-alpha stimulates increased expression of prostaglandin endoperoxide H synthase Type 2 mRNA in amnion-derived WISH cells

1998 ◽  
Vol 20 (2) ◽  
pp. 221-231 ◽  
Author(s):  
WR Hansen ◽  
T Sato ◽  
MD Mitchell
Keyword(s):  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Alpha ◽  
Early Gene ◽  
Tnf Alpha ◽  
Necrosis Factor Alpha ◽  
Prostaglandin Endoperoxide ◽  
Factor Alpha ◽  
Endoperoxide H Synthase ◽  
Necrosis Factor

We have evaluated the mechanism by which tumour necrosis factor-alpha (TNF-alpha) induces increased prostaglandin (PG) biosynthesis in amnion-derived WISH cells. WISH cells were treated with 50 ng/ml TNF-alpha or vehicle for 0-24 h. PGE2 production was stimulated by TNF-alpha within 2 h and continued to accumulate for at least 24 h. Increased prostaglandin endoperoxide H synthase (PGHS)-2 mRNA expression was evident within 30 min and was highest by 1 h, returning to unstimulated levels by 2 h. The PGHS-2 mRNA was re-induced at 8 h and was also elevated at 16 h. Immunoreactive PGHS-2 protein was nearly undetectable in control cells. However, within 30 min of TNF-alpha treatment, PGHS-2 protein was elevated and was induced for at least 16 h suggesting rapid production of both the PGHS-2 mRNA and protein. Transcription run-on assays indicated that the initial increase in the PGHS-2 mRNA was due to a 20-fold increase in the rate of transcription. The PGHS-2 mRNA decayed with an apparent half-life of 1 h in TNF-alpha-stimulated WISH cells. Induction of PGHS-2 expression proceeded in the presence of 10 microg/ml cycloheximide which agrees with the classification of PGHS-2 as an immediate early gene. These results indicate that a bi-phasic induction of the PGHS-2 mRNA is due, in part, to an initial transcriptional activation which results in rapid and continued synthesis of the PGHS-2 protein. This may be a unique characteristic of amnion cells which may be partially responsible for increased PG concentrations in the amniotic fluid during infection-associated preterm labour.

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