Relevant bibliographies by topics / Cyclooxygenase (COX)

Academic literature on the topic 'Cyclooxygenase (COX)'

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Published: 4 June 2021
Last updated: 11 March 2023

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Journal articles on the topic "Cyclooxygenase (COX)"

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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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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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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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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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Belton, Orina, and Desmond J. Fitzgerald. "Cyclooxygenase isoforms and atherosclerosis." Expert Reviews in Molecular Medicine 5, no. 9 (March 7, 2003): 1–18. http://dx.doi.org/10.1017/s1462399403005842.

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Nonsteroidal anti-inflammatory drugs (NSAIDs) are widely used in the treatment of arthritis and pain. However, their long-term use is limited by gastrointestinal (GI) side effects such as gastric ulcers. NSAIDs act by inhibiting an enzyme called cyclooxygenase. Cyclooxygenase (COX) catalyses the generation of prostaglandins from arachidonic acid. Two isoforms of the enzyme exist – COX-1 and COX-2 – both of which are targets for NSAIDs. Although they are associated with GI toxicity, NSAIDs have important antithrombotic and anti-inflammatory effects. The GI injury has been attributed to COX-1 inhibition and the anti-inflammatory effects to COX-2 inhibition. As COX-2 is traditionally viewed as an inducible enzyme, selective inhibition of COX-2 by ‘coxibs’ (selective COX-2 inhibitors) has been employed to achieve anti-inflammatory and analgesic effects without GI side effects. However, recently there have been suggestions that chronic administration of coxibs might increase the risk of cardiovascular events, such as atherosclerosis, compared with traditional NSAIDs. In vascular disease, there is increased expression of both COX-1 and COX-2, resulting in enhanced prostaglandin generation. The specific role of COX-1 and COX-2 in vascular regulation is still unknown but such knowledge is essential for the effective use of coxibs. Although more evidence is pointing to selective COX-1 inhibition as a therapeutic measure in inflammatory atherosclerosis, there are some studies that suggest that inhibition of COX-2 might have a potential benefit on atherosclerosis.
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Brannon, Timothy S., Amy N. MacRitchie, Marina A. Jaramillo, Todd S. Sherman, Ivan S. Yuhanna, Linda R. Margraf, and Philip W. Shaul. "Ontogeny of cyclooxygenase-1 and cyclooxygenase-2 gene expression in ovine lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 274, no. 1 (January 1, 1998): L66—L71. http://dx.doi.org/10.1152/ajplung.1998.274.1.l66.

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Prostacyclin is a key mediator of pulmonary vascular and parenchymal function during late fetal and early postnatal life, and its synthesis in whole lung increases during that period. The rate-limiting enzyme in prostacyclin synthesis in the developing lung is cyclooxygenase (COX). We investigated the ontogeny and cellular localization of COX-1 (constitutive) and COX-2 (inducible) gene expression in lungs from late-gestation fetal lambs, 1-wk-old newborn lambs (NB1), and 1- to 4-mo-old newborn lambs (NB2). COX-1 mRNA abundance rose progressively from fetal to NB1 to NB2, increasing 12-fold overall. In parallel, immunoblot analysis revealed a progressive increase in COX-1 protein, rising fourfold from fetal lambs to NB2. COX-2 mRNA levels increased fivefold from fetal to NB1 but were similar in NB1 and NB2. However, COX-2 protein was not detectable by immunoblot analysis in any age group. Immunohistochemistry for COX-1 showed intense immunostaining in endothelial cells at all ages. COX-1 was also expressed in airway epithelium at all ages, with a greater number of epithelial cells staining positively in NB2 compared with fetal and NB1 groups. In addition, COX-1 was expressed in airway smooth muscle from NB1. COX-2 immunostaining was absent in all age groups. These findings indicate that there is differential expression of COX-1 and COX-2 in the developing lung and that the enzymes are expressed in a cell-specific manner. The developmental upregulation in COX-1 may optimize the capacity for prostaglandin-mediated vasodilation, bronchodilation, and surfactant synthesis in the newborn lung.
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Odau, Simone, Christoph Gabler, Christoph Holder, and Ralf Einspanier. "Differential expression of cyclooxygenase 1 and cyclooxygenase 2 in the bovine oviduct." Journal of Endocrinology 191, no. 1 (October 2006): 263–74. http://dx.doi.org/10.1677/joe.1.06761.

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The aim of the present study was to investigate the enzymes for the local prostaglandin (PG) biosynthesis present in the bovine oviduct during the estrous cycle to influence early reproductive events. Bovine oviducts were classified into four phases: pre-ovulatory, post-ovulatory, early-to-mid luteal, and late luteal phase, subdivided further into ipsi- or contralateral site and separated into ampulla or isthmus. Oviductal cells were gained by flushing the oviductal regions. Quantitative real-time reverse transcriptase-PCR was performed for the secretory and cytosolic phospholipases A2 (sPLA2IB, cPLA2α, and cPLA2β) and cyclooxygenases (COX-1 and COX-2) as the first step enzymes of PG synthesis. COX-1 and cPLA2β showed significant highest mRNA expression around and before ovulation compared with the luteal phase respectively. sPLA2IB and cPLA2α mRNA expression was unregulated during the estrous cycle. Regional differences in mRNA content were found for sPLA2IB with higher mRNA expression in the ampulla than in the isthmus. Western blot analysis revealed the highest COX-1 protein content in the early-to-mid luteal phase. Immunohistochemistry demonstrated that COX-1 was localized in epithelial and smooth muscle cells, whereas COX-2 was only localized in epithelial cells. COX-2 showed a differential distribution within the epithelial cell layer suggesting a regulation on a cellular level, although the COX-2 mRNA and protein amounts did not vary throughout the estrous cycle. A COX activity assay of oviductal cells revealed that COX activity originated predominantly from COX-1 than from COX-2. Treatment of primary oviductal cells with 10 pg/ml 17β-estradiol or 10 ng/ml progesterone resulted in a higher expression of COX-2 and cPLA2α, but not of the other enzymes. The expression pattern of these enzymes suggests that an estrous-cycle dependent and region-specific PG synthesis in the bovine oviduct may be required for a successful reproduction.
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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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Ray, Neelanjana, Margaret E. Bisher, and L. W. Enquist. "Cyclooxygenase-1 and -2 Are Required for Production of Infectious Pseudorabies Virus." Journal of Virology 78, no. 23 (December 1, 2004): 12964–74. http://dx.doi.org/10.1128/jvi.78.23.12964-12974.2004.

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ABSTRACT We have recently shown that cyclooxygenase-2 (COX-2) transcription is markedly induced after herpes simplex virus type 1 and pseudorabies virus (PRV) infections of rat embryonic fibroblast (REF) cells (N. Ray and L. W. Enquist, J. Virol. 78:3489-3501, 2004). For this study, we investigated the role of cyclooxygenase induction in the replication and growth of PRV. We demonstrate here a concordant increase in COX-2 mRNA and protein levels after the infection of REF cells. Inhibitors blocking the activity of cyclooxygenases caused a dramatic reduction in PRV growth. Viral growth could be restored if prostaglandin E2, the final product of COX-2 activity, was added simultaneously with the COX inhibitors. Immediate-early protein IE180, major capsid protein VP5, and glycoprotein expression were slightly reduced in the presence of COX-2 inhibitors, but expression of the early protein EP0 was not affected by COX inhibition. Viral DNA replication was marginally reduced in the presence of a COX-1/2 inhibitor, but there was no defect in viral DNA cleavage. Electron microscopy analysis revealed an increased number of unusual empty capsid structures in the nuclei of cells infected with PRV in the presence of a COX-1/2 inhibitor. These capsid structures shared some characteristics with procapsids but had a novel appearance by negative staining. Our data establish a role for COX-1 and COX-2 in facilitating the efficient growth and replication of PRV in primary cells.
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Maloney, Christopher G., William A. Kutchera, Kurt H. Albertine, Thomas M. McIntyre, Stephen M. Prescott, and Guy A. Zimmerman. "Inflammatory Agonists Induce Cyclooxygenase Type 2 Expression by Human Neutrophils." Journal of Immunology 160, no. 3 (February 1, 1998): 1402–10. http://dx.doi.org/10.4049/jimmunol.160.3.1402.

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Abstract The synthesis of prostanoids is regulated by cyclooxygenases (prostaglandin H synthases), which catalyze the conversion of arachidonic acid to PGH2. Cyclooxygenases are the target of aspirin and other nonsteroidal anti-inflammatory agents. In this study, we found that human polymorphonuclear leukocytes (PMNs) express the inducible isoform of cyclooxygenase, COX-2, when stimulated by LPS whereas the protein was not detectable in freshly isolated human PMNs. We also found by immunohistochemical analysis that COX-2 is expressed in PMNs in inflamed human tissues. COX-2 was induced in a time- and concentration-dependent fashion when isolated human PMNs were exposed to LPS; COX-2 was also induced, or its expression was increased, by TNF-α, IL-1, and IL-8. Expression of COX-2 in stimulated PMNs was paralleled by secretion of PGE2. The release of PGE2 was blocked by a selective nonsteroidal inhibitor of COX-2, indicating that the enzyme is responsible for the prostanoids produced, and was inhibited by dexamethasone. The time course of LPS-induced COX-2 expression and other features were different in freshly isolated PMNs, monocytes, and macrophages, indicating that COX-2 expression is differentially regulated in myeloid cells of different lineages and degrees of maturation. Consistent with this, IL-4 and IL-10, which suppressed LPS-induced COX-2 expression in monocytes, had little effect on this response by PMNs. These experiments demonstrate that PMNs express COX-2 when appropriately stimulated. Thus, they may actively influence the eicosanoid composition of the acute inflammatory milieu.
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Dissertations / Theses on the topic "Cyclooxygenase (COX)"

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Sun, Haipeng. "Regulation of Cyclooxygenase Gene Expression by Glucocorticoids in Cardiomyocytes." Diss., The University of Arizona, 2007. http://hdl.handle.net/10150/194896.

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Glucocorticoids (GCs) are endogenous steroid hormones that regulate a number of critical physiological processes. Psychological stress increases the level of GCs in the circulating system. The biological effect of elevated GCs on the heart is not well understood. We found that GCs induced Cyclooxygenase-1 (COX-1) and COX-2 gene expression in cardiomyocytes. COX-1 or COX-2 encodes the rate-limiting enzyme in the biosynthesis of prostanoids, which modulate crucial physiological and pathophysiological responses. The present studies aim to elucidate the signaling transduction pathway and the mechanism underlying GC induced COX expression.Our data demonstrate that GCs activate COX-1 gene expression through transcriptional regulation. COX-1 gene promoter studies support a role of Sp binding site in CT induced COX-1 gene expression. The nuclear protein binding to this site appears to be Sp3 transcription factor. Co-immunoprecipitation assays indicated a physical interaction between GR and Sp3 protein. Silencing of Sp3 transcription factor with small interfering RNA suppressed CT-induced COX-1 promoter activation. These data suggest that the activated GR interacts with Sp3 transcription factor that binds to COX-1 promoter to up-regulate COX-1 gene expression in cardiomyocytes.We also found that administration of GC in adult mice increased the level of COX-2 in the ventricles. With isolated neonatal cardiomyocytes, corticosterone (CT) induces the transcription of COX-2 gene. This response appears to be cardiomyocyte cell type specific and GC receptor (GR)-dependent. CT causes activation of p38 MAPK and subsequently CREB phosphorylation that mediates COX-2 gene expression. Mifepristone, a GR antagonist, failed to inhibit p38 and CREB activation and p38 inhibition failed to prevent activation of GR. These data suggest that two parallel signaling pathways, GR and p38 MAPK, act in concert to regulate the expression of COX-2 gene in cardiomyocytes.In addition to the investigation of mechanism and signaling transduction pathway, I have explored pharmacological agents that modulate COX expression. LY294002, a commonly used PI3K inhibitor, inhibited COX-2 gene expression via a PI3K-independent mechanism. Whereas GSK-3 inhibitors, such as lithium chloride, upregulated COX-2 gene expression, but suppressed GC-induced COX-1 expression. These data have paved the foundation for pharmacological manipulation of COX-1 and COX-2 gene expression in the heart.
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Tarantino, E. "THE ROLE OF CYCLOOXYGENASE-1 (COX-1) AND CYCLOOXYGENASE-2 (COX-2) IN A VENOUS THROMBOSIS MOUSE MODEL." Doctoral thesis, Università degli Studi di Milano, 2016. http://hdl.handle.net/2434/353697.

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Background: Deep vein thrombosis (DVT) is a serious national health problem, and pulmonary thromboembolism (PE) represents the life-threatening most common complication. Venous thromboembolism (VTE), including both these conditions, is traditionally treated with anticoagulant drugs. In particular, vitamin K antagonists and heparins are usually used in the reduction of thrombus development and in secondary prevention. However, the use of these drugs has several limitations: wide variability dose/response relationship between patients and in the same patient, multiple interactions with other drugs/foods, variability of daily doses, need of periodic withdrawals of blood during therapy, problems of overdosing. Then, the discovery of new drugs for VTE needs. The cyclooxygenase isoenzymes, COX-1 and COX-2, catalyse the formation of prostaglandins and, thromboxane from arachidonic acid, and play a critical role in thrombosis. Recent meta-analysis suggests that low-dose aspirin (ASA) reduces the rate of VTE recurrence. In contrast, the clinical use of COX-2 inhibitors seems associated with increased risk of venous thrombosis. However, the role of COX-1 and COX-2 in venous thrombosis remain unclear. Aim: We investigated the impact of COX-1 and COX-2 enzymes in venous thrombosis in order to identify the molecular mechanisms responsible for this effect and develop new therapeutic strategies to prevent venous thrombosis. In particular, we focused on the impact of inhibition of COX-pathway on leukocyte activation, important regulators of formation and propagation of venous thrombus. Methods and Results: Using in vivo and in vitro approaches, we provide evidence that: a) thromboxane, produced by platelets, triggers activation of leukocytes, with consequent development and propagation of venous thrombus induced by inferior vena cava ligation. In particular, we showed that ASA, by inhibiting irreversibly platelet COX-1, prevents platelet thromboxane production resulting in decreased venous thrombosis. b) COX-2 deletion induces platelet hyper-activity and hyper-coagulation state, associated with a reduced fibrinolysis and formation of bigger thrombi. In this scenario, the high levels of tissue factor observed in leukocytes of COX-2KO mouse may explain the positive association observed between administration of COX-2 inhibitors and VTE. Thanking advantage of an accurate, and clinically relevant, technique such as ultrasonography, we are setting a method helpful to monitor thrombus growing and to better understand the pathophysiology of venous thromboembolism. Conclusion: In conclusion, data obtained show that the inhibition of COX-1 and COX-2 in a venous thrombosis mouse model could lead to opposite effect on the thrombus development, stabilization and resolution. In particular, COX-1 inhibition is responsible of an impairment development and growth of venous thrombus, with a mechanism most likely dependent of TXA2/TP pathway. In contrast, COX-2 inhibition caused an increased in thrombus development, growing accompanied with reduction in the thrombus resolution. All data obtained support evidences that both COX-1 and COX-2 play a key role in DVT, opening the way to novel therapeutic approaches.
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Hunter, John Cameron. "Multiple Recoding Mechanisms Produce Cyclooxygenase and Cyclooxygenase-Related Proteins from Frameshift-Containing COX-3/COX-1b Transcripts in Rat and Human." BYU ScholarsArchive, 2012. https://scholarsarchive.byu.edu/etd/6149.

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To increase diversity of enzymes and proteins, cells mix and match exonic and intronic regions retained in mature mRNAs by alternative splicing. An estimated 94% of all multi-exon genes express one or more alternatively spliced transcripts generating proteins with similar or modified functions. Cyclooxygenase is a signaling enzyme that catalyzes the rate-limiting step in the synthesis of diverse bioactive lipids termed prostaglandins. Prostaglandins are involved in myriad physiological and pathopysiological processes including vasoregulation, stomach mucosal maintenance, parturition, pain, fever, inflammation, neoplasia and angiogenesis and are inhibited by aspirin-like drugs known as NSAIDs. In 2002 an alternatively spliced, intron-1 retaining variant of COX-1 was cloned from canine brain tissue. This new variant, termed COX-3 or COX-1b, is an enzymatically active prostaglandin synthase expressed at relatively high levels in a tissue and cell type dependant manner in all species examined. In humans and most rodent species intron-1 is 94 and 98 nucleotides long respectively. Retention of the intron in these species introduces a frameshift and is predicted to result in translation of a very small 8-16kD protein with little similarity to either 72kD COX-1 or COX-2, calling into question the role of this variant. In this dissertation, I present my results from cloning and ectopically expressing a complete and accurate COX-3 cDNA from both rat and human. I confirmed that COX-3 mRNA encodes multiple large molecular weight cyclooxygenase-like proteins in the same reading frame as COX-1. Translation of these proteins relies on several recoding mechanisms including cap-independent translation initiation, alternative start site selection, and ribosomal frameshifting. Using siRNA and Western blotting I have identified some of these proteins in tissues and cells. Two COX-3 encoded proteins are active prostaglandin synthase enzymes with activities similar to COX-1 and represent novel targets of NSAIDs. Other COX-3 proteins have unknown function, but their size and cellular location suggest potential roles as diverse as cytosolic enzymes and nuclear factors.
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Chen, Suzi Su-Hsin, and suzi chen@med monash edu au. "Cyclooxygenase Expression in Human Diabetes." RMIT University. Medical Sciences, 2007. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20080206.121439.

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Cyclooxygenase (COX) is the rate limiting enzyme that catalyses the production of prostanoids, which are crucial to vascular homeostasis. Evidence suggests that endothelial dysfunction and inflammation play a role in vascular complications in aging and diabetes. Previous animal studies by our laboratory at RMIT University reported enhanced COX expression with aging in rat aortas, platelets and monocytes. Potentially, alteration in COX expression may result in an imbalanced prostanoid production favoring the synthesis of vasoconstrictors and hence increase the risk of cardiovascular events in the aging population. The regulation of altered COX expression in aging, however, is not clear. It has been suggested that histone hyperacetylation may be an important mechanism that regulates COX levels during the aging process as increased histone acetylation has been shown to occur with aging. Thus, we hypothesized that COX expression is modulated by histone hyperacetylati on. This was investigated by measuring COX expression in histone hyperacetylated cultured endothelial cells. In the case of diabetes, studies have reported that the development of diabetes and its complications is associated with persistent inflammatory activity, evident with increased inflammatory markers in the circulation. COX-mediated pathways may be involved in this inflammatory process in diabetes. Furthermore, the formation of advanced glycation end products (AGEs) is accelerated in diabetes. AGEs can bind to receptors for AGEs (RAGE), which has also been suggested to play a role in inflammation in diabetes. We hypothesized that COX- and RAGE-mediated pathways contribute to increased inflammation in diabetes and potentiate the development of diabetic vascular complications. This was investigated by measuring changes in COX-mediated pathways in both rat and human diabetic models. The current thesis reports: 1) in cultured endothelial cells, histone hyperacetylation was associated with increased COX expression; 2) an overall increase in inflammation was observed in diabetes involving COX- and RAGE-mediated pathways. This was supported by increased platelet COX-1 and monocyte COX-2 levels in Zucker rats, increased monocyte COX-2 in human Type 1 diabetes and elevated plasma TXB2 and PGE2 levels in both human Type 1 and Type 2 diabetic subjects. Up-regulation of RAGE expression was further found in platelets and monocytes in both human diabetes types. When treated with NSAIDs, plasma prostanoid levels, COX and RAGE expression were reduced significantly in both platelets and monocytes in human diabetic subjects. 3) It is unclear how COX and RAGE expression was regulated, but histone modifications may be one of the mechanisms. Data from cultured cells indicated that increased COX expression was associated with increased histone acetylation levels induced by TSA. Concurrent increases in histone acetylation and COX-2 levels were also observed in human Type 1 diabetes, but similar findings were not observed in human Type 2 diabetes. In addition, we failed to find an age-dependent increase in monocyte histone H4 acetylation in human Type 2 diabetes despite an age-dependent increase in monocyte COX-2 expression. Thus, whether histone hyperacetylation modulates COX expression and in what conditions require further investigation.
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Kellogg, Aaron. "Effect of Cyclooxygenase (COX)-2 Activation on Diabetic Neuropathy." University of Toledo Health Science Campus / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=mco1211909697.

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Bühler, Nico Martin. "Selektive COX-2 Inhibitoren und Nierenschädigung bei salzsensitiver Hypertonie /." [S.l.] : [s.n.], 2009. http://opac.nebis.ch/cgi-bin/showAbstract.pl?sys=000297941.

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Kim, Janet Heejung. "Cyclooxygenase-2 Expression in Post-Mastectomy Chest Wall Relapse." Yale University, 2006. http://ymtdl.med.yale.edu/theses/available/etd-06282006-104942/.

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The purpose of this study was to assess the prognostic significance and clinical correlations of cyclooxgenase-2 expression (COX) in a cohort of patients treated with radiation (RT) for post-mastectomy chest wall relapse (PMCWR). Between 1975 and 1999, 113 patients were treated for isolated PMCWR. All patients were treated with biopsy and/or excision of the CWR followed by RT. Median follow-up was 10 years. All clinical data including demographics, pathology, staging, receptor status, HER-2/neu status, and adjuvant therapy were entered into a computerized database. Paraffin-embedded CWR specimens were retrieved from 42 patients, of which 38 were evaluated, created into a tissue microarray, stained by immunohistochemical methods for COX, and graded 0-3+. A score of 2-3+ was considered positive. Overall survival from original diagnosis for the entire cohort was 44% at 10 years. Survival rate after chest wall recurrence was 28% at 10 years. The distant metastasis-free survival rate after CWR was 40% at 10 years. Local-regional control of disease was achieved in 79% at 10 years after CWR. COX was considered positive in 13 of 38 cases. COX was inversely correlated with ER (p= .045) and PR (p = .028), and positively correlated with HER-2/neu (p =.003). COX was also associated with a shorter time to PMCWR. The distant metastasis-free rate for COX negative patients was 70% at 10 years, compared with 31% at 10 years for COX-2 positive patients (p = 0.029). COX positive had a poorer local-regional progression-free rate of 19% at 10 years, compared with 81% at 10 years for COX negative (p = 0.003). Outcome following RT for PMCWR is relatively poor. Positive COX correlated with other markers of poor outcome including a shorter time to local relapse, negative ER/PR and positive Her-2/neu status. Positive COX correlated with higher distant metastasis and lower local-regional control of disease. If confirmed with larger studies, these data have implications with respect to the concurrent use of COX-2 inhibitors and radiation for PMCWR.
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Vijitruth, Rattanavijit. "ROLES OF CYCLOOXYGENASE-2 IN MICROGLIAL ACTIVATION AND DOPAMINERGIC CELL DEATH." UKnowledge, 2006. http://uknowledge.uky.edu/gradschool_diss/237.

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Accumulating evidence suggests that inflammation plays an important role in the progression ofParkinson's disease (PD). Among many inflammatory factors found in the PD brain, cyclooxygenase(COX), especially the inducible isoform, COX-2, is believed to be the critical enzyme in theinflammatory response. Induction of COX-2 is also found in an experimental model of PD producedby administration of 1-methy-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). To investigate whetherinhibition of COX-2 by valdecoxib or deficiency in COX-2 could prevent dopaminergic neuronaltoxicity and locomotor activity impairment, we injected MPTP into valdecoxib-treated C57BL/6N miceand COX-2 deficient mice, respectively. Both automated total distance and vertical activitymeasurements of the open-field test were significantly reduced in the vehicle-treated mice at two weekspost-MPTP injection. In contrast, valdecoxib treatment significantly attenuated these deficits.Similarly, COX-2 deficiency attenuated MPTP-induced loss of coordination on a rotarod assay.Valdecoxib or deficiency of COX-2 reduced microglial activation while preventing loss of tyrosinehydroxylase (TH)-positive neurons in the substantia nigra pars compacta (SNpc). The total number ofactivated microglia in the SNpc had a strong positive correlation with the level of COX-2 anddopaminergic neurodegeneration. The results of this study indicate that reducing the activity of COX-2can mitigate the progressive loss of dopaminergic neurons as well as the motor deficits caused byMPTP neurotoxicity, possibly by suppressing the activation of microglia in the SNpc.
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Mukherjee, Kamalika. "ROLE OF CYCLOOXYGENASE-2 IN ABDOMINAL AORTIC ANEURYSMS IN MICE." UKnowledge, 2012. http://uknowledge.uky.edu/pharmacy_etds/29.

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Abdominal aortic aneurysm (AAA) is a chronic inflammatory disease with no available pharmacological treatment. AAA formation reduces the structural integrity of the vessel and increases the susceptibility to rupture. The inflammatory response within human aneurysmal tissue is characterized by increased expression of cyclooxygenase-2 (COX-2). Similarly, in a mouse model of the disease induced by chronic Angiotensin II (AngII) infusion, we have shown that COX-2 expression in the abdominal aortic smooth muscle layer increases early in the development of the disease. Furthermore, genetic or pharmacological inactivation of COX-2 prior to disease initiation reduces AAA incidence. The current study utilized nonhyperlipidemic mice to determine the effectiveness of COX-2 inhibition initiated after AAA formation. COX-2 inhibitor treatment was initiated 5 days after beginning the AngII infusion, a time-point where significant aneurysmal pathology is observed. COX-2 inhibition with celecoxib significantly reduced the incidence as well as severity of AAAs as compared to the control group. Celecoxib treatment also protected the mice from aortic rupture and death. AAA development is characterized by degradation of the aortic smooth muscle layer with loss of the contractile phenotype. We found that the effectiveness of celecoxib was associated with significantly increased mRNA expression of alpha-actin, SM22alpha and desmin, all of which are markers of a differentiated smooth muscle cell phenotype. Celecoxib treatment also decreased mRNA expression of a marker of dedifferentiated smooth muscle (hyaluronic acid synthase 2). We also examined the role of altered expression of COX-2 in the increased susceptibility of the abdominal segment to AAA formation. We found a prolonged and greater induction of COX-2 in the abdominal aortic smooth muscle layer in contrast to a transient induction of COX-2 in the other regions of the aorta throughout disease progression. Overall, these findings suggest that COX-2 plays an important role in AAA development in mice, and COX-2 inhibition with celecoxib attenuates progression of aneurysm development by maintaining a differentiated phenotype in abdominal aortic smooth muscle cells.
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Kim, Youngsoo. "Molecular characterization of cyclooxygenase-2 (COX-2) expression in murine skin carcinoma cells /." Digital version accessible at:, 1998. http://wwwlib.umi.com/cr/utexas/main.

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Books on the topic "Cyclooxygenase (COX)"

1

Masline, Shelagh Ryan. Celebrex: Cox-2 inhibitors--the amazing new pain fighters. New York: Avon Books, 1999.

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R, Vane John, Botting Regina M, William Harvey Research Conference (1997 : Phuket, Thailand), and William Harvey Research Conference (1998 : Boston, Mass.), eds. Clinical significance and potential of selective COX-2 inhibitors: The combined proceedings of the William Harvey Conferences held in Phuket, Thailand, on 18-19 September, 1997 and in Boston, USA, on 23-24 April, 1998, supported by an educational grant from Boehringer Ingelheim. London: William Harvey Press, 1998.

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The Cox-2 connection: Natural breakthrough treatment for arthritis, Alzheimer's, and cancer. Rochester, Vt: Healing Arts Press, 2001.

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E, Harris Randall, ed. Inflammation in the pathogenesis of chronic diseases: The COX-2 controversy. New York: Springer, 2007.

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G, Bazán Nicolás, Botting Jack H, and Vane John R, eds. New targets in inflammation: Inhibitors of COX-2 or adhesion molecules : proceedings of a conference held on April 15-16, 1996, in New Orleans, USA, supported by an educational grant from Boehringer Ingelheim. Dordrecht: Kluwer Academic Publishers, 1996.

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Barragry, Thomas B. N.S.A.I.D.S./toxicity: COX 2 developments. [Dublin]: [University College Dublin, Department of Small Animal Studies], 1998.

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Vane, John R. Improved non-steroid anti-flammatory drugs COX-2 enzyme inhibitors: Proceedings of a conference held on October 10-11, 1995, at Regent's College, London. Dordrecht: Kluwer Academic Publishers, 1996.

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William Harvey Conference (1995 London, England). Improved non-steroid anti-inflammatory drugs: COX-2 enzyme inhibitors : proceedings of a conference held on October 10-11, 1995, at Regent's College, London. Dordrecht: Kluwer Academic, 1996.

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Vane, Sir John, ed. Clinical Significance And Potential Of Selective Cox-2 Inhibitors. WILLIAM HARVEY PRESS, 1998.

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Sir John R. Vane (Editor) and Jack H. Botting (Editor), eds. Selective COX-2 Inhibitors: Pharmacology, Clinical Effects and Therapeutic Potential. Springer, 1998.

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Book chapters on the topic "Cyclooxygenase (COX)"

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F�rstenberger, G., F. Marks, and K. M�ller-Decker. "Cyclooxygenase-2 and Skin Carcinogenesis." In COX-2, 72–89. Basel: KARGER, 2003. http://dx.doi.org/10.1159/000071367.

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DuBois, R. N. "Cyclooxygenase-2 and Colorectal Cancer." In COX-2, 124–37. Basel: KARGER, 2003. http://dx.doi.org/10.1159/000071370.

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Dubinett, S. M., S. Sharma, M. Huang, M. Dohadwala, M. Pold, and J. T. Mao. "Cyclooxygenase-2 in Lung Cancer." In COX-2, 138–62. Basel: KARGER, 2003. http://dx.doi.org/10.1159/000071371.

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Rodger, Ian W., and Chi-Chung Chan. "Inducible Cyclooxygenase (COX-2)." In Neuroinflammation, 355–71. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-473-3_14.

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Patrono, C., F. Cipollone, G. Renda, and P. Patrignani. "Cyclooxygenase enzymes in human vascular disease." In Selective COX-2 Inhibitors, 73–78. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-4872-6_7.

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Saha, D., and H. Choy. "Potential for Combined Modality Therapy of Cyclooxygenase Inhibitors and Radiation." In COX-2, 193–209. Basel: KARGER, 2003. http://dx.doi.org/10.1159/000071374.

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Gately, S., and R. Kerbel. "Therapeutic Potential of Selective Cyclooxygenase-2 Inhibitors in the Management of Tumor Angiogenesis." In COX-2, 179–92. Basel: KARGER, 2003. http://dx.doi.org/10.1159/000071373.

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Hawk, E. T., J. L. Viner, and A. Umar. "Non-Steroidal Anti-Inflammatory and Cyclooxygenase-2-Selective Inhibitors in Clinical Cancer Prevention Trials." In COX-2, 210–42. Basel: KARGER, 2003. http://dx.doi.org/10.1159/000071375.

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Browner, M. F. "The structure of human cyclooxygenase-2 and selective inhibitors." In Selective COX-2 Inhibitors, 19–26. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-4872-6_2.

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Altorki, N. K., K. Subbaramaiah, and A. J. Dannenberg. "Cyclooxygenase-2: A Target for the Prevention and Treatment of Cancers of the Upper Digestive Tract." In COX-2, 107–23. Basel: KARGER, 2003. http://dx.doi.org/10.1159/000071369.

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Conference papers on the topic "Cyclooxygenase (COX)"

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Branković, Jovica, Vesna Milovanović, and Vladimir P. Petrović. "CYCLOOXYGENASE-2 AS „IN SILICO“ TARGET OF PHENOLIC HYDRAZONE- TYPE DERIVATIVES." In 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac, 2021. http://dx.doi.org/10.46793/iccbi21.324b.

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In the present work, a series of phenolic hydrazone analogs were investigated in silico for their potential inhibitory activity toward COX-2. These examinations were based on the capability of hydrazone-based compounds to interact with numerous enzymes, as well as on their versatile biological features and therapeutical applications. COX-2 was selected due to its involvement in the inflammation and carcinogenesis processes. Regarding this, COX-2 represents a valid target for the development of compounds that could block the formation of harmful inflammation mediators.
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Damayanti, Sophi, Andhika Bintang Mahardhika, Slamet Ibrahim, Wei Lim Chong, Vannajan Sanghiran Lee, and Daryono Hadi Tjahjono. "O-desmethylquinine as a cyclooxygenase-2 (COX-2) inhibitors using AutoDock Vina." In 3RD INTERNATIONAL CONFERENCE ON FUNDAMENTAL AND APPLIED SCIENCES (ICFAS 2014): Innovative Research in Applied Sciences for a Sustainable Future. AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4898452.

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Killian, Megan L., Barbara Zielinska, and Tammy L. Haut Donahue. "Role of IL-1 on Aggrecanase and COX-2 Gene Expression of Meniscal Explants Following Dynamic Compression." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19110.

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The menisci within the knee likely respond to adverse loading conditions, leading to aggravated cartilage damage and fissuring [1]. Upregulation of catabolic molecules such as interleukin-1α (IL-1α), metalloproteinases (MMPs), aggrecanases (ADAMTS-4 and -5), and cyclooxygenase-2 (COX-2), as well as release of proteoglycans [2], have been shown in vitro for meniscal explants following dynamic loading [3]. A crucial event in matrix degradation is the loss of aggrecan, caused by the ADAMTS family [4]. In osteoarthritic cartilage, IL-1 has been shown to influence COX-2 activity, leading to increased synthesis of prostaglandin E2 and subsequent proteinase activity [5].
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Beteringhe, Adrian, and Flavia Corina Mitroi Symeonidis. "Molecular Docking Technique for selection of some naproxen derivatives as inhibitors of cyclooxygenase 2 (COX-2)." In 2015 7th International Conference on Electronics, Computers and Artificial Intelligence (ECAI). IEEE, 2015. http://dx.doi.org/10.1109/ecai.2015.7301240.

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Veisi, Zeinab, Muhammet Ceylan, Anil Mahapatro, and Ramazan Asmatulu. "An Electrospun Polyaniline Nanofiber as a Novel Platform for Real-Time COX-2 Biomarker Detection." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-65269.

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The presence of Cyclooxygenase-2 (COX-2) biomarker has been associated with the development of certain types of cancer such as breast cancer. Moreover, reliable quantification of COX-2 as an enzyme responsible for pain and inflammation is vital. Here we demonstrate the feasibility of sensitive COX-2 detection via integration of nanoporous polyaniline fibers on the microfabricated platform to develop a label-free biosensor. Highly porous polyaniline nanofibers were fabricated in different diameters and integrated on the interdigitated microelectrodes to develop electrochemical platforms. Characterization results revealed that the smaller diameter improved the sensitivity of the biosensor due to enhancement in the specific surface area. The developed biosensor was able to detect analyte as low as 0.1pg/mL with a large dynamic linear range of 10fg/mL to 1μg/mL. The fabricated sensor showed remarkable sensitivity towards COX-2 antigen suggesting the significant contribution of this nanofiber based platform to the enhanced sensitivity in COX-2 analyte detection.
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Premprasert, C., S. Tewtrakul, and J. Wungsintaweekul. "Plaunol A isolated from Croton stellatopilosus suppress inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2)." In 67th International Congress and Annual Meeting of the Society for Medicinal Plant and Natural Product Research (GA) in cooperation with the French Society of Pharmacognosy AFERP. © Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-3400145.

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Daham, K., WL Song, A. Gulich, J. Lawson, S. Dahlen, GF FitzGerald, and B. Dahlen. "Prostaglandin (PG) D2Formation in Subjects with Asthma Occurs Via the Cyclooxygenase-1 (COX-1) Pathway at Baseline." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2773.

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Lin, Shih-Chieh, and Shaw-Jenq Tsai. "Abstract 3083: Dual-specificity phosphatase-2 (DUSP2) negatively control cyclooxygenase-2 (COX-2) expression in cancer cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3083.

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Gavala, Monica L., Loren C. Denlinger, Arturo Guadarrama, Lei Shi, Lisa Y. Lenertz, William W. Busse, Ronald L. Sorkness, Nizar N. Jarjour, and Paul J. Bertics. "Induction Of Monocyte Cyclooxygenase (COX) Expression And Prostaglandin E2 (PGE2) Production As A Biomarker Of Asthma Severity." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3931.

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Liu, Fei, Margarita M. Suarez Velandia, Emeka Ifedigbo, Aleksandar Marinkovic, Xiaoli Liu, Daniel J. Tschumperlin, and Laura E. Fredenburgh. "Pathologic Matrix Stiffening Promotes Cyclooxygenase (COX)-2-Dependent Mechanobiological Feedback Amplification Of Vascular Remodeling In Pulmonary Arterial Hypertension." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a2622.

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Reports on the topic "Cyclooxygenase (COX)"

1

Splitter, Gary, Zeev Trainin, and Yacov Brenner. Lymphocyte Response to Genetically Engineered Bovine Leukemia Virus Proteins in Persistently Lymphocytic Cattle from Israel and the U.S. United States Department of Agriculture, July 1995. http://dx.doi.org/10.32747/1995.7570556.bard.

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The goal of this proposal was to identify proteins of BLV recognized by lymphocyte subpopulations and determine the contribution of these proteins to viral pathogenesis. Our hypothesis was that BLV pathogenesis is governed by the T-cell response and that the immune system likely plays an important role in controlling the utcome of infection. Our studies presented in ths final report demonstrate that T cell competency declines with advancing stages of infection. Dramatic differences were observed in lymphocyte proliferation to recombinant proteins encoded by BLV gag (p12, p15, and p24) and env (gp30 and gp15) genes in different disease stages. Because retroviruses are known to mutate frequently, examinatin of infected cattle from both Israel and the United States will likely detect variability in the immune response. This combined research approach provides the first opportunity to selectively address the importance of T-cell proliferation to BLV proteins and cytokines produced during different stages of BLV infection. Lack of this information regarding BLV infection has hindered understanding lympocyte regulation of BLV pathogenesis. We have developed the essential reagents necessary to determine the prominence of different lymphocyte subpopulations and cytokines produced during the different disease stages within the natural host. We found that type 1 cytokines (IL-2 and IFN-g) increased in PBMCs from animals in early disease, and decreasd in PBMCs from animals in late disease stages of BLV infection, while IL-10, increased with disease progression. Recently, a dichotomy between IL-12 and IL-10 has emerged in regards to progression of a variety of diseases. IL-12 activates type 1 cytokine production and has an antagonistic effect on type 2 cytokines. Here, using quantitative competitive PCR, we show that peripheral blood mononuclear cells from bovine leukemia virus infected animals in the alymphocytotic disease stage express increased amount of IL-12 p40 mRNA. In contrast, IL-12 p40 mRNA expression by PL animals was significantly decreased compared to normal and alymphocytotic animals. To examine the functions of these cytokines on BLV expression, BLV tax and pol mRNA expression and p24 protein production were quantified by competitive PCR, and by immunoblotting, respectively. IL-10 inhibited BLV tax and pol mRNA expression by BLV-infected PBMCs. In addition, we determined that macrophages secret soluble factor(s) that activate BLV expression, and that secretion of the soluble factor(s) could be inhibited by IL-10. In contrast, IL-2 increased BLV tax and pol mRNA, and p24 protein production. These findings suggest that macrophages have a key role in regulating BLV expression, and IL-10 produced by BLV-infected animals in late disease stages may serve to control BLV expression, while IL-2 in the early stage of disease may activate BLV expression. PGE2 is an important immune regulator produced only by macrophages, and is known to facilitate HIV replication. We hypothesized that PGE2 may regulate BLV expression. Here, we show that cyclooxygenase-2 (COX-2) mRNA expression was decreased in PBMCs treated with IL-10, while IL-2 enhanced COX-2 mRNA expression. In contrast, addition of PGE2 stimulated BLV tax and pol mRNA expression. In addition, the specific COX-2 inhibitor, NS-398, inhibited BLV expression, while addition of PGE2 increased BLV tax expression regardless of NS-398. These findings suggest that macrophage derived cyclooxygenase -2 products, such as PGE2, may regulate virus expression and disease rogression in BLV infection, and that cytokines (IL-2 and IL-10) may regulate BLV expression through PGE2 production.
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Fields, Michael J., Mordechai Shemesh, and Anna-Riitta Fuchs. Significance of Oxytocin and Oxytocin Receptors in Bovine Pregnancy. United States Department of Agriculture, August 1994. http://dx.doi.org/10.32747/1994.7568790.bard.

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Oxytocin has multiple actions in bovine reproductive tract and it was our purpose to determine the nature of these actions and their significance for the physiology of bovine reproduction. The bovine oxytocin receptors (OTR) gene was cloned and its expression studied during the cycle and pregnancy. OTR mRNA changed in parallel with OTR with control occurring mainly at the transcriptional level. However, the endocrine regulation of OTR were found in endometrium and cervical mucosa at estrus and at parturition. In both tissues OTR were suppressed in the luteal phase and early pregnancy. Whereas cervical OTR remained suppressed throughout pregnancy, endometrial OTR began to increase soon after implantation and reached higher concentrations in midpregnancy than at estrus. OTR in caruncles did not increase until third trimester, and OTR in cervical mucosa, cotyledons and fetal membranes increased only at term. Myometrial OTR showed less variation and OTR were present throughout the cycle and pregnancy but increased significantly during mid- and late pregnancy. OTR were localized in endometrial epithelial cells and lumina epithelial cells of cervical mucosa as determined by immunohistochemistry. Endometrial OTR were functional throughout pregnancy and mediated PGF release from day 50 onwards in a receptor density related manner. OTR in cervical mucosa mediated PGE release both in vivo and in vitro, as shown in cyclic cows. The ontogeny of uterine OTR was studied from third trimester fetal stage until puberty. OTR were present in endometrium and cervical mucosa in high concentrations throughout this period; myometrial OTR began to increase somewhat later but also reached adult values by 6-mo of age. In the prepuberal heifers OT injections failed to initiate PGF2a, release. The influence of steroids on the effect of OT was examined. Ovariectomy and E2 were without effect, but P4 with or without E2 induced a massive PGF2a release in response to OT in spite of reduced OTR. Bovine cyclooxygenases (COX-1 and COX-2) were cloned and their expression studied in the endometrium of prepuberal heifers and pregnant cows. Untreated and E2 treated prepuberal heifers did not express COX-2 but P4 treated heifers did express the mRNA for COX-2, albeit weakly. During the second half of pregnancy COX-2 mRNA was strongly expressed in cotyledons and somewhat less in caruncles, whereas endometrium, myometrium and cervical mucosa showed only weak, if any, COX-2 mRNA under basal conditions. However, 2 h after OT injection significant increases in COX-2 mRNA were found in endometrial RNA. Thus OT is capable of inducing the expression of the inducible COX-2 gene, and hence the conversion of arachidonic acid to prostanoids. The results indicate that the functions of OT are numerous and probably essential for successful pregnancy and parturition.
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