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Journal articles on the topic 'Cyclooxygenase'

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Published: 4 June 2021

Last updated: 9 March 2023

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1

Zhang, Xinping, Scott G. Morham, Robert Langenbach, and Donald A. Young. "Malignant Transformation and Antineoplastic Actions of Nonsteroidal Antiinflammatory Drugs (Nsaids) on Cyclooxygenase-Null Embryo Fibroblasts." Journal of Experimental Medicine 190, no. 4 (August 16, 1999): 451–60. http://dx.doi.org/10.1084/jem.190.4.451.

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In this study, we use primary embryonic fibroblasts derived from cyclooxygenase-deficient transgenic embryos to further investigate the role of the two cyclooxygenases, cyclooxygenase 1 (COX-1) and cyclooxygenase 2 (COX-2), in the process of neoplastic transformation. Cells with either, neither, or both of the cyclooxygenases were transformed by Ha-ras and/or SV40. Our results show that when a cyclooxygenase enzyme is present, the transformed cells have marked increases in COX-2 and/or COX-1 expression. Nevertheless, each type of cell, deficient in either or both cyclooxygenases, can be readily transformed at almost equal efficiency. Different nonsteroidal antiinflammatory drugs (NSAIDs) were used to examine their possible antineoplastic effects on the transformed cells, which have various levels of expression of COX-1 or COX-2. Our results show that NSAIDs suppress the colony formation in soft agar in a dosage-dependent manner in the absence of the cyclooxygenase(s). Thymidine incorporation and apoptosis analyses further demonstrate that the NSAIDs are effective in the cyclooxygenase-null cells. Our findings with cyclooxygenase knockout cells confirm recent reports that some of the antiproliferative and antineoplastic effects of NSAIDs are independent of the inhibition of either COX-1 or COX-2. They also show that transformation is independent of the status of cyclooxygenase expression, suggesting that the involvement of the cyclooxygenases in tumorigenesis may occur at later steps.

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2

Dolan, Sharron, James G. Kelly, Marie Huan, and Andrea M. Nolan. "Transient Up-regulation of Spinal Cyclooxygenase-2 and Neuronal Nitric Oxide Synthase following Surgical Inflammation." Anesthesiology 98, no. 1 (January 1, 2003): 170–80. http://dx.doi.org/10.1097/00000542-200301000-00027.

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Background Surgery induces pain and hyperalgesia postoperatively. The products of cyclooxygenases and nitric oxide synthase (NOS) have been implicated in the development of inflammatory pain and hyperalgesia experimentally, and the use of drugs clinically that modify cyclooxygenase activity has been advocated in the management of perioperative pain. However, regulation of these enzymes following surgery has not been studied. Methods Adult female sheep (n = 12) undergoing a midline laparotomy for collection of ova were used in this study. Lumbar and cervical spinal cord tissue was collected from animals euthanized 1 day and 6 or 7 days after surgery and processed for cyclooxygenase (cyclooxygenase-1 and cyclooxygenase-2), neuronal NOS mRNA expression using reverse-transcription polymerase chain reaction and hybridization. Tissues were also processed for NADPH-diaphorase staining and cyclooxygenase-1 and cyclooxygenase-2 protein expression by immunohistochemistry and Western blotting. Results No alteration in cyclooxygenase-1 or cyclooxygenase-2 mRNA or protein concentrations were detected in spinal cord by reverse-transcription polymerase chain reaction and Western blotting, respectively, at 1 day or 6 or 7 days after surgery. However, using techniques that localize mRNA and protein expression ( hybridization and immunohistochemistry, respectively), increases in cyclooxygenase-2 were identified in lamina V dorsal horn neurons in lumbar spinal cord 1 day after surgery. A significant increase in neuronal NOS mRNA was observed in lumbar spinal cord 1 day after surgery, localized to laminae I-II and lamina V neurons, which returned to baseline concentrations by 6 to 7 days. NADPH-diaphorase staining was significantly increased in laminae I-II in lumbar spinal cord 1 day after surgery but not after 6 to 7 days. Conclusions Spinal cyclooxygenase and neuronal NOS pathways are differentially altered following surgical inflammation. The early and transient nature of these changes suggests that these enzymes are implicated in postoperative pain and hypersensitivity.

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3

YAMAMOTO, KEI. "Cyclooxygenase - 1 and cyclooxygenase - 2." Japanese Journal of Clinical Immunology 19, no. 6 (1996): 564–67. http://dx.doi.org/10.2177/jsci.19.564.

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4

Stockton, Rebecca A., and Bruce S. Jacobson. "Modulation of Cell-Substrate Adhesion by Arachidonic Acid: Lipoxygenase Regulates Cell Spreading and ERK1/2-inducible Cyclooxygenase Regulates Cell Migration in NIH-3T3 Fibroblasts." Molecular Biology of the Cell 12, no. 7 (July 2001): 1937–56. http://dx.doi.org/10.1091/mbc.12.7.1937.

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Adhesion of cells to an extracellular matrix is characterized by several discrete morphological and functional stages beginning with cell-substrate attachment, followed by cell spreading, migration, and immobilization. We find that although arachidonic acid release is rate-limiting in the overall process of adhesion, its oxidation by lipoxygenase and cyclooxygenases regulates, respectively, the cell spreading and cell migration stages. During the adhesion of NIH-3T3 cells to fibronectin, two functionally and kinetically distinct phases of arachidonic acid release take place. An initial transient arachidonate release occurs during cell attachment to fibronectin, and is sufficient to signal the cell spreading stage after its oxidation by 5-lipoxygenase to leukotrienes. A later sustained arachidonate release occurs during and after spreading, and signals the subsequent migration stage through its oxidation to prostaglandins by newly synthesized cyclooxygenase-2. In signaling migration, constitutively expressed cyclooxygenase-1 appears to contribute ∼25% of prostaglandins synthesized compared with the inducible cyclooxygenase-2. Both the second sustained arachidonate release, and cyclooxygenase-2 protein induction and synthesis, appear to be regulated by the mitogen-activated protein kinase extracellular signal-regulated kinase (ERK)1/2. The initial cell attachment-induced transient arachidonic acid release that signals spreading through lipoxygenase oxidation is not sensitive to ERK1/2 inhibition by PD98059, whereas PD98059 produces both a reduction in the larger second arachidonate release and a blockade of induced cyclooxygenase-2 protein expression with concomitant reduction of prostaglandin synthesis. The second arachidonate release, and cyclooxygenase-2 expression and activity, both appear to be required for cell migration but not for the preceding stages of attachment and spreading. These data suggest a bifurcation in the arachidonic acid adhesion-signaling pathway, wherein lipoxygenase oxidation generates leukotriene metabolites regulating the spreading stage of cell adhesion, whereas ERK 1/2-induced cyclooxygenase synthesis results in oxidation of a later release, generating prostaglandin metabolites regulating the later migration stage.

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5

Tegeder, Irmgard, Josef Pfeilschifter, and Gerd Geisslinger. "Cyclooxygenase‐independent actions of cyclooxygenase inhibitors." FASEB Journal 15, no. 12 (October 2001): 2057–72. http://dx.doi.org/10.1096/fj.01-0390rev.

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6

Kutil, Zsofia, Veronika Temml, David Maghradze, Marie Pribylova, Marcela Dvorakova, Daniela Schuster, Tomas Vanek, and Premysl Landa. "Impact of Wines and Wine Constituents on Cyclooxygenase-1, Cyclooxygenase-2, and 5-Lipoxygenase Catalytic Activity." Mediators of Inflammation 2014 (2014): 1–8. http://dx.doi.org/10.1155/2014/178931.

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Cyclooxygenases and lipoxygenases are proinflammatory enzymes; the former affects platelet aggregation, vasoconstriction, vasodilatation and later the development of atherosclerosis. Red wines from Georgia and central and western Europe inhibited cyclooxygenase-1 (COX-1) activity in the range of 63–94%, cyclooxygenase-2 (COX-2) activity in the range of 20–44% (tested at a concentration of 5 mL/L), and 5-lipoxygenase (5-LOX) activity in the range of 72–84% (at a concentration of 18.87 mL/L). White wines inhibited 5-LOX in the range of 41–68% at a concentration of 18.87 mL/L and did not inhibit COX-1 and COX-2. Piceatannol (IC50= 0.76 μM) was identified as a strong inhibitor of 5-LOX followed by luteolin (IC50= 2.25 μM), quercetin (IC50= 3.29 μM), and myricetin (IC50= 4.02 μM).trans-Resveratrol was identified as an inhibitor of COX-1 (IC50= 2.27 μM) and COX-2 (IC50= 3.40 μM). Red wine as a complex mixture is a powerful inhibitor of COX-1, COX-2, and 5-LOX, the enzymes involved in eicosanoid biosynthetic pathway.

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7

Sladek, Krzysztof, and James R. Sheller. "Cyclooxygenase Mediators." Immunology and Allergy Clinics of North America 10, no. 2 (May 1990): 409–18. http://dx.doi.org/10.1016/s0889-8561(22)00279-x.

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8

Mao, Yumeng, Isabel Poschke, and Rolf Kiessling. "Cyclooxygenase-2." OncoImmunology 2, no. 8 (August 2013): e25157. http://dx.doi.org/10.4161/onci.25157.

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9

Marnett, Lawrence J. "Cyclooxygenase mechanisms." Current Opinion in Chemical Biology 4, no. 5 (October 2000): 545–52. http://dx.doi.org/10.1016/s1367-5931(00)00130-7.

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10

Breyer, Matthew D. "Beyond cyclooxygenase." Kidney International 62, no. 5 (November 2002): 1898–99. http://dx.doi.org/10.1046/j.1523-1755.2002.00645.x.

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11

Furst, Daniel E. "Perspectives on the Cyclooxygenase-2/ Cyclooxygenase-1 Hypothesis." JCR: Journal of Clinical Rheumatology 4, Supplement (October 1998): 40–48. http://dx.doi.org/10.1097/00124743-199810001-00007.

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12

Gilroy, Derek W., Annette Tomlinson, and Derek A. Willoughby. "Differential effects of inhibitors of cyclooxygenase (cyclooxygenase 1 and cyclooxygenase 2) in acute inflammation." European Journal of Pharmacology 355, no. 2-3 (August 1998): 211–17. http://dx.doi.org/10.1016/s0014-2999(98)00508-1.

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13

Hofer, Michal, and Milan Pospíšil. "Stimulated recovery of perturbed haematopoiesis by inhibition of prostaglandin production — promising therapeutic strategy." Open Life Sciences 1, no. 4 (December 1, 2006): 584–93. http://dx.doi.org/10.2478/s11535-006-0033-3.

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AbstractInhibitors of prostaglandin production, designated as classical non-steroidal anti-inflammatory drugs (NSAIDs) and acting on the base of non-selective inhibition of cyclooxygenases, have been found in numerous studies to potentiate recovery of perturbed haematopoiesis by removing the negative feedback control mediated by prostaglandins. However, classical NSAIDs show pronounced undesirable gastrointestinal side effects, which limits the possibility of their utilization for various pathophysiological states including myelosuppression. Specific cyclooxygenase-2 (COX-2) inhibitors, targeted at selective inhibition of this inducible cyclooxygenase isoform and having much better gastrointestinal side effect profile, have been found in recent studies to retain the haematopoiesis-stimulating effects of classical NSAIDs. These results suggest that the indication spectrum of selective COX-2 inhibitors may be extended to the indication of myelosuppression of various etiology. Combining the anti-tumour and haematopoiesis-stimulating activities in a single COX-2 inhibitor may have a positive clinical impact.

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14

Biava, Mariangela, Giulio Cesare Porretta, Giovanna Poce, Sibilla Supino, Stefano Forli, Michele Rovini, Andrea Cappelli, et al. "Cyclooxygenase-2 Inhibitors. 1,5-Diarylpyrrol-3-acetic Esters with Enhanced Inhibitory Activity toward Cyclooxygenase-2 and Improved Cyclooxygenase-2/Cyclooxygenase-1 Selectivity." Journal of Medicinal Chemistry 50, no. 22 (November 2007): 5403–11. http://dx.doi.org/10.1021/jm0707525.

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15

Cho, Kang Han, Kyoung Hwan Kim, Sang Heum Paik, Young Ho Hong, Hoon Shik Yang, Hoon Kim, and Chun Gil Kim. "Expression of Cyclooxygenase-2 in Laryngeal Squamous Cell Carcinoma." Journal of Clinical Otolaryngology Head and Neck Surgery 12, no. 2 (November 2001): 244–48. http://dx.doi.org/10.35420/jcohns.2001.12.2.244.

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16

Endo, T., F. Ogushi, and S. Sone. "LPS-dependent cyclooxygenase-2 induction in human monocytes is down-regulated by IL-13, but not by IFN-gamma." Journal of Immunology 156, no. 6 (March 15, 1996): 2240–46. http://dx.doi.org/10.4049/jimmunol.156.6.2240.

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Abstract We investigated the effects of Th2 cell-associated cytokines, IL-4, IL-10, and IL-13, on prostaglandin (PG) production by human peripheral blood monocytes (HPBM) in terms of four parameters: PGE2 synthesis; cyclooxygenase activity; protein; and mRNA of two cyclooxygenase isozymes (cyclooxygenase-1 and cyclooxygenase-2). LPS-stimulated PGE2 synthesis and cyclooxygenase activity were suppressed by IL-4, IL-10, or IL-13. Furthermore, the LPS-dependent increase of cyclooxygenase activity in HPBM was attributable to cyclooxygenase-2 because it was inhibited by NS-398 (a cyclooxygenase-2-specific inhibitor). Western and Northern blot analyses revealed that the LPS-induced increases in cyclooxygenase-2 protein and mRNA were attenuated by the addition of IL-4, IL-10, or IL-13. In contrast, cyclooxygenase-1 protein and mRNA were hardly detected in monocytes that were incubated with or without LPS in the presence or absence of IL-4, IL-10, and IL-13. These results suggest that the reduction of LPS-induced PGE2 synthesis and cyclooxygenase activity by IL-4, IL-10, and IL-13 in HPBM are mainly due to the down-regulation of cyclooxygenase-2 selectively induced by LPS. Conversely, IFN-gamma, a Th1 cell-associated cytokine, did not affect PGE2 production and cyclooxygenase activity. These data suggest a mechanism for modulation of inflammation by the anti-inflammatory Th2 cell-associated cytokines but not a Th1 cell-associated cytokine.

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17

Chandrakirana Krisnamurti, Gabriella, and Fatchiyah Fatchiyah. "The Biological Function Prediction of The 10-gingerol Compound of Ginger in Inhibiting Cyclooxygenase-2 Activity." Journal of Pure and Applied Chemistry Research 9, no. 3 (December 31, 2020): 222–32. http://dx.doi.org/10.21776/ub.jpacr.2020.009.03.547.

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Anti-inflammatory agents inhibit prostaglandin synthesis by blocking cyclooxygenases (COXs). The compounds extracted from ginger, 10-gingerol and 10-shogaol can inhibit inflammation but the mechanism of inhibition remains unclear. Here we used molecular docking to predict the molecular interactions between COXs and the three inhibitors, acetaminophen (CID1983), 10-gingerol (CID168115) and 10-shogaol (CID6442612). By using that acetaminophen as a gold standard, the results demonstrated that acetaminophen, 10-gingerol, and 10-shogaol could bind catalytic domain and membrane binding domain of cyclooxygenase-1 (COX-1) and cyclooxygenase-2 (COX-2). The 10-shogaol did not show significantly different binding energy to bind to COX-1 and COX-2. The 10-gingerol posed a stronger and more specific binding to the membrane-binding domain of COX-2 than acetaminophen and 10-shogaol. The specific binding of the 10-gingerol to COX-2 could prevent the binding of the natural substrate, arachidonic acid. The results provide useful information to improving activities of anti-inflammatory.

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18

Claria, Joan. "Cyclooxygenase-2 Biology." Current Pharmaceutical Design 9, no. 27 (October 1, 2003): 2177–90. http://dx.doi.org/10.2174/1381612033454054.

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19

Reitz, David B., and Peter C. Isakson. "Cyclooxygenase-2 Inhibitors." Current Pharmaceutical Design 1, no. 2 (September 1995): 211–20. http://dx.doi.org/10.2174/1381612801666220917221427.

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Prostaglandins are synthesized by the enzyme cyclooxygenase (COX), which is the target for nonsteroidal anti-inflammatory drugs (NSAIDs). Recently a second form of COX was discovered (COX-2) that is induced by inflammatory stimuli. The identification of an inducible form of COX led to the hypothesis that COX-2 is responsible for inflammatory prostaglandins, whereas the constitutive COX-I produces physiologically important prostaglandins, e.g., in stomach and kidney. Selective COX- 2 inhibitors have been shown to be anti-inflammatory but do not cause ulcers in the stomach or intestines. It is anticipated that drugs which selectively inhibit COX-2 will be superior anti-inflammatory agents with clear benefits over existing NSAIDs. In this review, the expression of human COX-I and COX-2 are discussed. A survey of the different chemical classes of COX-2 inhibitors with structure-activity relationships (SAR) and relevant pharmacological profiles are also presented.

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20

Hankey, Graeme J., and John W. Eikelboom. "Cyclooxygenase-2 Inhibitors." Stroke 34, no. 11 (November 2003): 2736–40. http://dx.doi.org/10.1161/01.str.0000097301.50041.6e.

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21

Cipollone, Francesco, and Carlo Patrono. "Cyclooxygenase-2 Polymorphism." Arteriosclerosis, Thrombosis, and Vascular Biology 22, no. 10 (October 2002): 1516–18. http://dx.doi.org/10.1161/01.atv.0000035402.68085.a0.

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22

Soumaoro, Labile Togba, Hiroyuki Uetake, Tetsuro Higuchi, Yoko Takagi, Masayuki Enomoto, and Kenichi Sugihara. "Cyclooxygenase-2 Expression." Clinical Cancer Research 10, no. 24 (December 15, 2004): 8465–71. http://dx.doi.org/10.1158/1078-0432.ccr-04-0653.

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23

Langenbach, Robert, Charles Loftin, Christopher Lee, and Howard Tiano. "Cyclooxygenase knockout mice." Biochemical Pharmacology 58, no. 8 (October 1999): 1237–46. http://dx.doi.org/10.1016/s0006-2952(99)00158-6.

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24

DuBois, Raymond N. "Cyclooxygenase and cancer." Prostaglandins & Other Lipid Mediators 59, no. 1-6 (December 1999): 59. http://dx.doi.org/10.1016/s0090-6980(99)90294-0.

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25

Masferrer, Jaime L., Peter C. Isakson, and Karen Seibert. "CYCLOOXYGENASE-2 INHIBITORS." Gastroenterology Clinics of North America 25, no. 2 (June 1996): 363–72. http://dx.doi.org/10.1016/s0889-8553(05)70252-1.

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26

McGoldrick, Kathryn E. "Cyclooxygenase-2 Inhibitors." Survey of Anesthesiology 48, no. 4 (August 2004): 207–8. http://dx.doi.org/10.1097/01.sa.0000132028.95631.1d.

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27

Hawkey, Christopher J., and Paul J. Fortun. "Cyclooxygenase-2 inhibitors." Current Opinion in Internal Medicine 5, no. 1 (February 2006): 106–10. http://dx.doi.org/10.1097/01.mog.0000182860.11669.04.

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28

Leon, Carmen G., Jeannine Marchetti, and Carlos P. Vio. "Renal Cyclooxygenase-2." Hypertension 38, no. 3 (September 2001): 630–34. http://dx.doi.org/10.1161/hy09t1.094509.

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29

Glaser, K. B. "Cyclooxygenase selectivity and NSAIDs: Cyclooxygenase-2 selectivity of etodolac (LODINE)." Inflammopharmacology 3, no. 4 (December 1995): 335–45. http://dx.doi.org/10.1007/bf02668029.

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30

Beer, A., P. Zagorchev, M. Filipova, and J. Lukanov. "Wirkungen von wässerigem Torfextrakt auf die Aktivität der Cyclooxygenase und deren Isoformen Cyclooxygenase-1 und Cyclooxygenase-2." Physikalische Medizin, Rehabilitationsmedizin, Kurortmedizin 25, no. 01 (February 10, 2015): 51–54. http://dx.doi.org/10.1055/s-0034-1396796.

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31

Fornai, Matteo, Rocchina Colucci, Filippo Graziani, Silvia Cei, Luca Antonioli, Matteo Tonelli, Cristina Vassalle, Corrado Blandizzi, Mario Gabriele, and Mario Del Tacca. "Cyclooxygenase-2 Induction after Oral Surgery Does Not Entirely Account for Analgesia after Selective Blockade of Cyclooxygenase 2 in the Preoperative Period." Anesthesiology 104, no. 1 (January 1, 2006): 152–57. http://dx.doi.org/10.1097/00000542-200601000-00021.

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Background The administration of selective cyclooxygenase-2 inhibitors before surgery is regarded as an innovative option to manage postoperative pain. This study was designed to (1) examine the efficacy of preoperative cyclooxygenase-2 blockade on postoperative oral pain and (2) compare pain intensity with prostaglandin E2 (PGE2) production and cyclooxygenase isoform (cyclooxygenase-1, cyclooxygenase-2) messenger RNA (mRNA) expression at the surgical site during the postoperative period. Methods Sixty patients with impacted lower third molars were randomly allocated to three single-dose treatment groups--placebo, 50 mg rofecoxib, or 550 mg naproxen--1 h before extraction. Pain intensity was evaluated with categorical and visual analog scales every 30 min from 90 to 240 min after surgery. At these times, PGE2 production in the alveolar socket was also evaluated. Cyclooxygenase-1 and cyclooxygenase-2 mRNA expression was examined by reverse-transcription polymerase chain reaction in gingival specimens collected during tooth removal and 240 min after surgery. Results Pain intensity and PGE2 production in the placebo group increased throughout the observation period. Naproxen prevented pain and decreased PGE2 release at all time points. Rofecoxib reduced PGE2 production versus placebo from 150 min onward, while inducing analgesia through the whole observation period. mRNA assay in gingival specimens collected at tooth extraction revealed cyclooxygenase-1 expression, whereas cyclooxygenase 2 was undetectable. At the end of observation, cyclooxygenase-1 mRNA expression was unchanged, whereas cyclooxygenase-2 mRNA was significantly induced. Conclusions This study indicates that preoperative administration of a selective cyclooxygenase-2 inhibitor ensures effective control of postoperative pain. It is suggested that the selective blockade of inducible cyclooxygenase 2 at the surgical site does not entirely account for the analgesic action occurring in the postoperative period.

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32

Sorenmo, K. U., M. H. Goldschmidt, F. S. Shofer, C. Goldkamp, and J. Ferracone. "Evaluation of cyclooxygenase-1 and cyclooxygenase-2 expression and the effect of cyclooxygenase inhibitors in canine prostatic carcinoma." Veterinary and Comparative Oncology 2, no. 1 (March 2004): 13–23. http://dx.doi.org/10.1111/j.1476-5810.2004.00035.x.

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33

Zhang, Xiao, Keqin Yan, Lin Deng, Jing Liang, Haiyan Liang, Dingqing Feng, and Bin Ling. "Cyclooxygenase 2 Promotes Proliferation and Invasion in Ovarian Cancer Cells via the PGE2/NF-κB Pathway." Cell Transplantation 28, no. 1_suppl (December 2019): 1S—13S. http://dx.doi.org/10.1177/0963689719890597.

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Ovarian cancer is the leading cause of death among gynecological malignancies. Cyclooxygenase 2 is widely expressed in various cancer cells and participates in the occurrence and development of tumors by regulating a variety of downstream signaling pathways. However, the function and molecular mechanisms of cyclooxygenase 2 remain unclear in ovarian cancer. Here, we demonstrated that cyclooxygenase 2 was highly expressed in ovarian cancer and the expression level was highly correlated with ovarian tumor grades. Further, ovarian cancer cells with high expression of cyclooxygenase 2 exhibit enhanced proliferation and invasion abilities. Specifically, cyclooxygenase 2 promoted the release of prostaglandin E2 upregulated the phosphorylation levels of phospho-nuclear factor-kappa B p65. Celecoxib, AH6809, and BAY11-7082 all can inhibit the promoting effect of cyclooxygenase 2 on SKOV3 and OVCAR3 cell proliferation and invasion. Besides, celecoxib inhibited SKOV3 cell growth in the xenograft tumor model. These data suggest that high expression of cyclooxygenase 2 promotes the proliferation and invasion of ovarian cancer cells through the prostaglandin E2/nuclear factor-kappa B signaling pathway. Cyclooxygenase 2 may be a potential therapeutic target for the treatment of ovarian cancer.

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34

Longo, W. E., L. J. Damore, J. E. Mazuski, G. S. Smith, N. Panesar, and D. L. Kaminski. "The role of cyclooxygenase-1 and cyclooxygenase-2 in lipopolysaccharide and interleukin-1 stimulated enterocyte prostanoid formation." Mediators of Inflammation 7, no. 2 (1998): 85–91. http://dx.doi.org/10.1080/09629359891225.

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Lipopolysaccharide is an inflammatory agent and interleukin-1 is a cytokine. Their pro-inflammatory effects may be mediated by prostanoids produced by inducible cyclooxygenase-2. The aim of this study was to determine the prostanoids produced by lipopolysaccharide and interleukin-1 stimulated enterocytes through the cyclooxygenase-1 and 2 pathways. Cultured enterocytes were stimulated with lipopolysaccharide or interleukin-1 β with and without cyclooxygenase inhibitors. Low concentrations of indomethacin and valerylsalicylic acid (VSA) were evaluated as cyclooxygenase-1 inhibitors and their effects compared with the effects of a specific cyclooxygenase-2 inhibitor, SC-58125. Prostaglandin E2, 6-keto prostaglandin F1α, prostaglandin D2and leukotriene B4levels were determined by radio immunoassay. Immunoblot analysis using isoformspecific antibodies showed that the inducible cyclooxygenase enzyme (COX-2) was expressed by 4 h in LPS and IL-1β treated cells while the constitutive COX-1 remained unaltered in its expression. Interleukin-1β and lipopolysaccharide stimulated the formation of all prostanoids compared with untreated cells, but failed to stimulate leukotriene B4. Indomethacin at 20 μ M concentration, and VSA inhibited lipopolysaccharide and interleukin 1β stimulated prostaglandin E2, but not 6-keto prostaglandin F1αformation. SC-58125 inhibited lipopolysaccharide and interleukin-1β stimulated 6-keto prostaglandin F1αbut not prostaglandin E2release. The specific cyclooxygenase-2 inhibitor also inhibited lipopolysaccharide produced prostaglandin D2but not interleukin-1β stimulated prostaglandin D2While SC-58125 inhibited basal 6-keto prostaglandin-F1αformation it significantly increased basal prostaglandin E2and prostaglandin D2formation. As SC-58125 inhibited lipopolysaccharide and interleukin-1β induced 6-keto prostaglandin F1αproduction but not prostaglandin E2production, it suggests that these agents stimulate prostacyclin production through a cyclooxygenase-2 mediated mechanism and prostaglandin E2production occurs through a cyclooxygenase-1 mediated mechanism. Prostaglandin D2production appeared to be variably produced by cyclooxygenase-1 or cyclooxygenase-2, depending on the stimulus.

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35

Hwang, Daniel, Jane Byrne, David Scollard, and Edward Levine. "Expression of Cyclooxygenase-1 and Cyclooxygenase-2 in Human Breast Cancer." JNCI: Journal of the National Cancer Institute 90, no. 6 (March 18, 1998): 455–60. http://dx.doi.org/10.1093/jnci/90.6.455.

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36

Littner, M. R., G. M. Kazmi, and F. D. Lott. "Distribution of cyclooxygenase products with cyclooxygenase inhibition in isolated dog lung." Journal of Applied Physiology 61, no. 3 (September 1, 1986): 988–93. http://dx.doi.org/10.1152/jappl.1986.61.3.988.

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Arachidonic acid metabolism can lead to synthesis of cyclooxygenase products in the lung as indicated by measurement of such products in the perfusate of isolated lungs perfused with a salt solution. However, a reduction in levels of cyclooxygenase products in the perfusate may not accurately reflect the inhibition of levels of such products as measured in lung parenchyma. We infused sodium arachidonate into the pulmonary circulation of isolated dog lungs perfused with a salt solution and measured parenchymal, as well as perfusate, levels of 6-keto-prostaglandin F1 alpha (6-keto-PGF1 alpha), prostaglandin F2 alpha (PGF2 alpha), prostaglandin E2 (PGE2), and thromboxane B2 (TxB2). These studies were repeated with indomethacin (a cyclooxygenase enzyme inhibitor) in the perfusate. We found that indomethacin leads to a marked reduction in perfusate levels of PGF2 alpha, PGE2, 6-keto-PGF1 alpha, and TxB2, as well as a marked reduction in parenchymal levels of 6-keto-PGF1 alpha and TxB2 when parenchymal levels of PGF2 alpha and PGE2 are not reduced. We conclude that, with some cyclooxygenase products, a reduction in levels of these products in the perfusate of isolated lungs may not indicate inhibition of levels of these products in the lung parenchyma and that a reduction in one parenchymal product may not predict the reduction of other parenchymal products. It can be speculated that some of the physiological actions of indomethacin in isolated lungs may result from incomplete or selective inhibition of synthesis of pulmonary cyclooxygenase products.

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Kirschenbaum, Alexander, Adam P. Klausner, Richard Lee, Pamela Unger, Shen Yao, Xin-Hua Liu, and Alice C. Levine. "Expression of Cyclooxygenase-1 and Cyclooxygenase-2 in the human prostate." Urology 56, no. 4 (October 2000): 671–76. http://dx.doi.org/10.1016/s0090-4295(00)00674-9.

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Kirschenbaum, A., A. P. Klausner, R. Lee, P. Unger, S. Yao, X. H. Liu, and A. C. Levine. "Expression of Cyclooxygenase-1 and Cyclooxygenase-2 in the Human Prostate." Journal of Urology 175, no. 3 (March 2006): 1033. http://dx.doi.org/10.1016/s0022-5347(05)00608-7.

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39

Rodler, D., and F. Sinowatz. "Expression of cyclooxygenase 1 and cyclooxygenase 2 in the canine testis." Reproductive Biology 13 (February 2013): 33. http://dx.doi.org/10.1016/j.repbio.2013.01.089.

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Snipes, James A., Bela Kis, Gregory S. Shelness, James A. Hewett, and David W. Busija. "Cloning and Characterization of Cyclooxygenase-1b (Putative Cyclooxygenase-3) in Rat." Journal of Pharmacology and Experimental Therapeutics 313, no. 2 (January 13, 2005): 668–76. http://dx.doi.org/10.1124/jpet.104.079533.

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Martinez, Rosa Ventura, Ma Irene Díaz Reval, Myrna Déciga Campos, José Antonio Terrón, Adriana M. Domínguez Ramírez, and Francisco J. López-Muñoz. "Involvement of peripheral cyclooxygenase-1 and cyclooxygenase-2 in inflammatory pain." Journal of Pharmacy and Pharmacology 54, no. 3 (March 2002): 405–12. http://dx.doi.org/10.1211/0022357021778475.

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42

Handler, Norbert, Walter Jaeger, Bea Kuen-Krismer, and Thomas Erker. "Cyclooxygenase-1 and Cyclooxygenase-2 Inhibition of Novel 1,2-Disubtituted Imidazoles." Archiv der Pharmazie 338, no. 12 (December 2005): 602–4. http://dx.doi.org/10.1002/ardp.200500178.

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NEUFELD, ARTHUR H., M. ROSARIO HERNANDEZ, MIRIAM GONZALEZ, and ARI GELLER. "Cyclooxygenase-1 and Cyclooxygenase-2 in the Human Optic Nerve Head." Experimental Eye Research 65, no. 6 (December 1997): 739–45. http://dx.doi.org/10.1006/exer.1997.0394.

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Kumar, Vinay, Lilly Ganju, and Iti Garg. "Role of Cyclooxygenase Pathway and Risk Associated with Non-Steroidal Anti-inflammatory Drugs Therapy in Cardiovascular Diseases." Defence Life Science Journal 3, no. 3 (June 25, 2018): 270. http://dx.doi.org/10.14429/dlsj.3.12914.

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<p>Non-steroidal anti-inflammatory drugs (NSAIDs) inhibit the cyclooxygenase enzyme activity through different<br />mechanisms and prevent inflammation. But they all have different risks associated with them. Some are associated with<br />gastrointestinal bleeding and some are strongly allied with the cardiovascular risks. Cyclooxygenase enzyme regulates<br />prostaglandin synthesis by converting arachidonic acid present at the sn-2 position of membrane phospholipids to<br />prostaglandin H2. Prostaglandin H2 is the precursor of all prostaglandins. There are two isoforms of cyclooxygenase<br />enzyme, cyclooxygenase-1 and cyclooxygenase-2 which differ in their active site due to an isoleucine to valine<br />substitution at amino acid 523 in cyclooxygenase-2. Cyclooxygenase-1 is constitutively expressed in platelets<br />where it helps in the formation of thromboxane whereas cyclooxygenase-2 is inductive form and is expressed in<br />the endothelial cells due to shear stress and forms prostacyclins. Both thromboxanes and prostacyclins maintain<br />the homeostasis of the vascular wall. During vascular injury prostacyclin production decreases as a result of which<br />thromboxane synthesis increases in the platelets which leads to platelet aggregation. Although, being strongly<br />associated with cardiovascular risks, NSAIDs are still prescribed to the patients to prevent pain according to their<br />condition. So this review aims to summarise the mechanism of cyclooxygenase pathway, possible mechanism of<br />action of NSAIDs and the risks of cardiovascular events associated with the use of NSAIDs.</p>

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Ohara, Maria, Teiji Sawa, Kiyoyasu Kurahashi, Jeanine P. Wiener-Kronish, Vatsal Doshi, Ichidai Kudoh, and Michael A. Gropper. "Induction of Cyclooxygenase-2 in Alveolar Macrophages after Acid Aspiration." Anesthesiology 88, no. 4 (April 1, 1998): 1014–22. http://dx.doi.org/10.1097/00000542-199804000-00022.

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Background Gastric acid aspiration can result in acute lung injury. In this study, the authors determined whether alveolar macrophages express cyclooxygenase-2 as a source of inflammatory mediators after acid aspiration. Methods Seventy-five microliters of hydrochloric acid solution, pH 1.15, was instilled into one lung in mice. After exposure, alveolar macrophages were harvested, and competitive polymerase chain reaction and enzyme-linked immunosorbent assay were performed to measure expression of cyclooxygenase-1 and -2, interleukin-1beta and -6, tumor necrosis factor-alpha, and inducible nitric oxide synthase (iNOS). The authors used immunocytochemistry to demonstrate expression of cyclooxygenase-2 in alveolar macrophages. Selective cyclooxygenase-2 blockade using N-2(-cyclohexyloxy-4-nitrophenyl) methane-sulphonamide was done to characterize prostaglandin-cytokine interaction. Results Acid aspiration induced upregulation of cyclooxygenase-2 and interleukin-6. Tumor necrosis factor-alpha and iNOS were not upregulated. Interleukin-1beta was upregulated even with saline instillation but could not be detected in the supernatant of the cell culture. Alveolar macrophages harvested from mice instilled with acid showed a trend toward more production of prostaglandin E2 and produced higher concentrations of interleukin-6 compared with alveolar macrophages from mice instilled with saline. Selective cyclooxygenase-2 blockade significantly decreased release of interleukin-6 from alveolar macrophages harvested from mice instilled with acid. Conclusions Acid aspiration induces strong expression of cyclooxygenase-2 and production of interleukin-6 in alveolar macrophages. Selective cyclooxygenase-2 blockade reduced production of interleukin-6 by acid-stimulated alveolar macrophages. These studies suggest that the induction of cyclooxygenase-2 plays an important role in the systemic inflammatory response induced by acid aspiration.

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ßahin, Mehmet, Emel ßahin, and Saadet Gümüşlü. "Cyclooxygenase-2 in Cancer and Angiogenesis." Angiology 60, no. 2 (May 27, 2008): 242–53. http://dx.doi.org/10.1177/0003319708318378.

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Tumor angiogenesis is a process where new blood vessels are formed from preexisting ones, resulting in several pathologies. Solid tumors induce angiogenesis to obtain the required nutrients and oxygen. Otherwise, tumors do not grow beyond 2 to 3 mm in diameter. Cyclooxygenase-2, an inducible enzyme important in inflammation, catalyzes the production of prostanoids from arachidonic acid. Cyclooxygenase-2 plays an important role in several cancer types, including colorectal, gastric, prostate, breast, lung, and endometrial cancer. Besides, cyclooxygenase-2 has been implicated in the progression and angiogenesis of cancers. Cyclooxygenase-2 inhibitors have been used to block angiogenesis and tumor proliferation. In this review, the recent studies related to the role of cyclooxygenase-2 in several cancer types and tumor-induced angiogenesis were compiled.

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Stenson, William F., Zhi Zhang, Terrence Riehl, and Samuel L. Stanley. "Amebic Infection in the Human Colon Induces Cyclooxygenase-2." Infection and Immunity 69, no. 5 (May 1, 2001): 3382–88. http://dx.doi.org/10.1128/iai.69.5.3382-3388.2001.

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ABSTRACT We sought to determine if infection of the colon withEntamoeba histolytica induces the expression of cyclooxygenase-2 and, if it does, to determine the contribution of prostaglandins produced through cyclooxygenase-2 to the host response to amebic infection. Human fetal intestinal xenografts were implanted subcutaneously in mice with severe combined immunodeficiency and allowed to grow; the xenografts were then infected with E. histolytica trophozoites. Infection with E. histolytica resulted in the expression of cyclooxygenase-2 in epithelial cells and lamina propria macrophages. Infection with E. histolytica increased prostaglandin E2(PGE2) levels 10-fold in the xenografts and resulted in neutrophil infiltration, as manifested by an 18-fold increase in myeloperoxidase activity. Amebic infection also induced an 18-fold increase in interleukin 8 (IL-8) production and a >100-fold increase in epithelial permeability. Treatment of the host mouse with indomethacin, an inhibitor of cyclooxygenase-1 and cyclooxygenase-2, or with NS-398, a selective inhibitor of cyclooxygenase-2, resulted in (i) decreased PGE2 levels, (ii) a decrease in neutrophil infiltration, (iii) a decrease in IL-8 production, and (iv) a decrease in the enhanced epithelial permeability seen with amebic infection. These results indicate that amebic infection in the colon induces the expression of cyclooxygenase-2 in epithelial cells and macrophages. Moreover, prostaglandins produced through cyclooxygenase-2 participate in the mediation of the neutrophil response to infection and enhance epithelial permeability.

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Glomb, Teresa, Benita Wiatrak, Katarzyna Gębczak, Tomasz Gębarowski, Dorota Bodetko, Żaneta Czyżnikowska, and Piotr Świątek. "New 1,3,4-Oxadiazole Derivatives of Pyridothiazine-1,1-Dioxide with Anti-Inflammatory Activity." International Journal of Molecular Sciences 21, no. 23 (November 30, 2020): 9122. http://dx.doi.org/10.3390/ijms21239122.

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Numerous studies have confirmed the coexistence of oxidative stress and inflammatory processes. Long-term inflammation and oxidative stress may significantly affect the initiation of the neoplastic transformation process. Here, we describe the synthesis of a new series of Mannich base-type hybrid compounds containing an arylpiperazine residue, 1,3,4-oxadiazole ring, and pyridothiazine-1,1-dioxide core. The synthesis was carried out with the hope that the hybridization of different pharmacophoric molecules would result in a synergistic effect on their anti-inflammatory activity, especially the ability to inhibit cyclooxygenase. The obtained compounds were investigated in terms of their potencies to inhibit cyclooxygenase COX-1 and COX-2 enzymes with the use of the colorimetric inhibitor screening assay. Their antioxidant and cytotoxic effect on normal human dermal fibroblasts (NHDF) was also studied. Strong COX-2 inhibitory activity was observed after the use of TG6 and, especially, TG4. The TG11 compound, as well as reference meloxicam, turned out to be a preferential COX-2 inhibitor. TG12 was, in turn, a non-selective COX inhibitor. A molecular docking study was performed to understand the binding interaction of compounds at the active site of cyclooxygenases.

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Moraga, F. A., and N. Urriola-Urriola. "Acetylcholine produces contractions mediated by the cyclooxygenase pathway in arterial vessels in the Chilean frog (Calyptocephalella gayi)." Brazilian Journal of Biology 77, no. 4 (May 25, 2017): 781–86. http://dx.doi.org/10.1590/1519-6984.00816.

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Abstract Previous studies performed in marine fish (I. conceptionis and G. laevifrons) showed that indomethacin blocked arterial contraction mediated by acetylcholine (ACh). The objective of this study was to determine if contraction induced by acetylcholine is mediated by the cyclooxygenase pathway in several arterial vessels in the Chilean frog Calyptocephalella gayi. Arteries from the pulmonary (PA), dorsal (DA), mesenteric (MA) and iliac (IA) regions were dissected from 6 adult specimens, and isometric tension studies were done using dose response curves (DRC) for ACh (10-13 to 10-3 M) in presence of a muscarinic antagonist (Atropine 10-5 M) and an unspecific inhibitor of cyclooxygenases (Indomethacin, 10-5M). All the studied arteries exhibited vasoconstriction mediated by ACh. This vasoconstriction was abolished in the presence of atropine in DA, MA and IA and attenuated in PA. Indomethacin abolished the vasoconstriction in MA and attenuated the response in PA, DA and IA. Similar to marine fish, C. gayi have an ACh-mediated vasoconstrictor pattern regulated by muscarinic receptors that activate a cyclooxygenase contraction pathway. These results suggest that the maintenance in vasoconstrictor mechanisms mediated by ACh→COX →vasoconstriction is conserved from fish to frogs.

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Lai, Zhen-Zhen, Hui-Li Yang, Si-Yao Ha, Kai-Kai Chang, Jie Mei, We-Jie Zhou, Xue-Min Qiu, et al. "Cyclooxygenase-2 in Endometriosis." International Journal of Biological Sciences 15, no. 13 (2019): 2783–97. http://dx.doi.org/10.7150/ijbs.35128.

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