scholarly journals Molecular cloning of human prostaglandin endoperoxide synthase type II and demonstration of expression in response to cytokines.

1993 ◽  
Vol 268 (12) ◽  
pp. 9049-9054 ◽  
Author(s):  
D.A. Jones ◽  
D.P. Carlton ◽  
T.M. McIntyre ◽  
G.A. Zimmerman ◽  
S.M. Prescott
2009 ◽  
Vol 285 (7) ◽  
pp. 5026-5039 ◽  
Author(s):  
Monica R. Walker ◽  
Sarah L. Brown ◽  
Terrence E. Riehl ◽  
William F. Stenson ◽  
Thaddeus S. Stappenbeck

Medicine ◽  
2015 ◽  
Vol 94 (35) ◽  
pp. e1116 ◽  
Author(s):  
Hong-guang Li ◽  
Fang-feng Liu ◽  
Hua-qiang Zhu ◽  
Xu Zhou ◽  
Jun Lu ◽  
...  

1993 ◽  
Vol 2 (2) ◽  
pp. 143-147 ◽  
Author(s):  
Chin-Yuh Yang ◽  
Ching-Liang Meng ◽  
Patrick Y- K. Wong

The human parathyroid hormone N-terminal fragment [hPTH-(1–34)] increases the conversion of exogenous unsaturated fatty acids to prostaglandins (PGs) in calvarial homogenates. Enzyme activities were completely blocked by indomethacin (5 × 10−7M), a PG synthase inhibitor, and actinomycin D (5 μM), an inhibitor of transcription, by binding to DNA. In addition, a potent inhibitor of protein synthesis, cycloheximide (10 μM), totally inhibited the stimulating effect of hPTH-(1–34) on prostaglandin endoperoxide synthase (PG synthase, EC 1.14.99.1). The stimulatory effect of hPTH-(1–34) on PG synthase was also reduced by the addition of stannous chloride. However, epidermal growth factor (EGF), platelet-derived activating factor (PDGF), and ionophore A23187 did not show the same stimulating effect as hPTH-(1–34) on PG synthase in calvaria. The results further demonstrated that PG synthase is a membrane-bound enzyme in chick calvaria. In this communication, evidence is presented that hPTH-(1–34) stimulates thede novosynthesis of PG synthase as demonstrated by the increased activity in calvarial homogenates and microsomes.


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