Abstract
Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the generation of prostanoids, and is thus one of the key players in the inflammatory process. Contrary to the constitutively expressed isoform COX-1, the expression of COX-2 is rapidly and transiently upregulated following pathological stimuli but little is known about pathways that mediate its degradation. Here we show that co-expression of COX-2 together with the β1 adrenergic receptor (β1AR) specifically lowers the expression of COX-2 in a dose-dependent manner. We further find that stimulation of the receptor for prolonged periods of time does not reverse the β1AR-induced decrease in COX-2, suggesting that this effect does not occur via classical β1-mediated signaling pathways. Rather we find that the half-life of COX-2 is significantly decreased in the presence of β1AR and that inhibition of the proteasome reverses the effect of the receptor on COX-2. Together these findings ascribe a new role for β1AR in the downregulation of COX-2.
Original language | English |
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Pages (from-to) | 319-321 |
Number of pages | 3 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 451 |
Issue number | 2 |
DOIs | |
State | Published - 22 Aug 2014 |
Bibliographical note
Funding Information:We thank Dr. Sagie Schif-Zuck for her assistance and expertise in the flow cytometry analyses. This work was supported by the BSF (United States-Israel Binational Scientific Foundation), project number 2009246.
Keywords
- Cyclooxygenase-2
- Degradation
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology