Статті в журналах: "Cox-2 expression"

1

Laino, Charlene. "COX-2 Inhibitorsʼ Effect Dependent on COX-2 Tumor Expression". Oncology Times 26, № 11 (червень 2004): 24. http://dx.doi.org/10.1097/01.cot.0000292129.98424.b1.

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2

Laino, Charlene. "COX-2 inhibitorsʼ effect dependent on COX-2 tumour expression". Oncology Times 1, № 6 (липень 2004): 13. http://dx.doi.org/10.1097/01434893-200407000-00007.

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3

Karim, Mohammed Mohibul, Yoshitake Hayashi, Masanori Inoue, Yukihiro Imai, Hiroshi Ito, and Misao Yamamoto. "Cox-2 expression in retinoblastoma." American Journal of Ophthalmology 129, no. 3 (March 2000): 398–401. http://dx.doi.org/10.1016/s0002-9394(99)00355-4.

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4

Telliez, Aurelie, Christophe Furman, Nicole Pommery, and Jean-Pierre Henichart. "Mechanisms Leading to COX-2 Expression and COX-2 Induced Tumorigenesis: Topical Therapeutic Strategies Targeting COX-2 Expression and Activity." Anti-Cancer Agents in Medicinal Chemistry 6, no. 3 (May 1, 2006): 187–208. http://dx.doi.org/10.2174/187152006776930891.

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5

Hazar, Burhan, Melek Ergin, Ertuğrul Seyrek, Şeyda Erdoğan, ılhan Tuncer, and Sibel Hakverdi. "Cyclooxygenase-2 (Cox-2) Expression in Lymphomas." Leukemia & Lymphoma 45, no. 7 (July 2004): 1395–99. http://dx.doi.org/10.1080/10428190310001654032.

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6

Mungo, David V., Xinping Zhang, Regis J. O'Keefe, Randy N. Rosier, J. Edward Puzas, and Edward M. Schwarz. "COX-1 and COX-2 expression in osteoid osteomas." Journal of Orthopaedic Research 20, no. 1 (January 2002): 159–62. http://dx.doi.org/10.1016/s0736-0266(01)00065-1.

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7

Menczer, Joseph, Letizia Schreiber, Oleg Sukmanov, Vladimir Kravtsov, Esther Berger, Abraham Golan, and Tally Levy. "COX-2 expression in uterine carcinosarcoma." Acta Obstetricia et Gynecologica Scandinavica 89, no. 1 (January 2010): 120–25. http://dx.doi.org/10.3109/00016340903342006.

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8

Gatalica, Zoran, and Brian Loggie. "COX-2 expression in pseudomyxoma peritonei." Cancer Letters 244, no. 1 (November 2006): 86–90. http://dx.doi.org/10.1016/j.canlet.2005.12.013.

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9

Menczer, Joseph. "Cox-2 expression in ovarian malignancies." European Journal of Obstetrics & Gynecology and Reproductive Biology 146, no. 2 (October 2009): 129–32. http://dx.doi.org/10.1016/j.ejogrb.2009.05.030.

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10

Kawamoto, Toru, Tohru Asano, Junichi Shoda, Mira Datta, Takeshi Todoroki, Naomi Tanaka, Takashi Fukao, and Masanao Miwa. "Immunohistochemical expression of cyclooxygenase-2 (COX-2) in gallbladder carcinoma — Association of enhanced COX-2 expression with tumor progression." Gastroenterology 118, no. 4 (April 2000): A189. http://dx.doi.org/10.1016/s0016-5085(00)82830-9.

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11

Lilly, Michael B., Leslie Drapiza, Milan Sheth, Marina Zemskova, Svetlana Bashkirova, and Joan Morris. "Expression of Cyclooxygenase-2 (COX-2) in Human Leukemias and Hematopoietic Cells." Blood 104, no. 11 (November 16, 2004): 4336. http://dx.doi.org/10.1182/blood.v104.11.4336.4336.

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Abstract COX-2 has been implicated in the development of many epithelial cancers, as well as in tumor angiogenesis. COX-2 inhibitors have been shown to have anti-tumor activity in experimental cancer. Little information exists, however, on the expression or role of COX-2 in hematologic malignancies. We have use a variety of immunochemical assays to document expression of COX-2 in human and murine leukemias and hematopoietic cells. The factor-dependent murine cell lines FDCP1 and 32D expressed COX-2 when growing continuously in the presence of IL-3; expression declined markedly when growth factor was removed. FDCP1 cells constitutively expressing bcl-2, pim-1, or bcr-abl had markedly elevated levels of COX-2, and continued to express this enzyme even after removal of growth factor. To assess COX-2 expression in human hematopoietic cells we developed a flow cytometry assay using a FITC-labelled anti-COX-2 MoAb (Cayman). Cells were washed once in serum-free medium, fixed briefly in 1% paraformaldehyde, permeabilized with PBS/0.2% Triton X100, then stained with antibody. Negative control samples were processed similarly but stained with antibody that had been preincubated with immunizing peptide. Specific COX-2 staining was interpreted as the difference between the histograms from blocked versus unblocked anti-COX-2 antibody, as determined by Kolmogorov-Smirnoff analysis. In buffy coat preparations from normal donors, we found constitutive expression of COX-2 in lymphocytes (both B-cells and T-cells). In contrast little or no COX-2 was detected in unstimulated neutrophils or monocytes. In human acute myelogenous leukemia (AML) cell lines we found COX-2 expression to be universal and easily detected. In several cell lines we confirmed the results of our flow cytometry assay with immunoblotting. We further examined 25 cryopreserved samples of human acute leukemia blasts obtained from peripheral blood. COX-2 expression was variable, but universal. Levels generally were less than those seen in immortalized cell lines, and did not correlate with blasts morphology (AML, ALL, APL, AMoL, CML-BT). To determine if COX-2 inhibitors could play a role in the treatment of acute leukemias, we performed cytotoxicity assays using the COX-2 specific inhibitors, celecoxib and NS398. Survival and growth of human AML cell lines were inhibited by both agents. These data demonstrate that 1) a variety of oncogenes can induce expression of COX-2 in hematopoietic cells, 2) clinical human acute leukemias uniformly express COX-2 in circulating blasts, and 3) COX-2 inhibitors are cytotoxic for human leukemia cells. Combination therapies for acute leukemias may evaluate the incorporation of COX-2 inhibitors for added cytotoxic effects or angiogenesis inhibition.

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12

Owen, Roger G., Im Fan, Sheila J. M. O’Connor, Faith E. Davies, Rebecca A. Rollett, J. Anthony Child, and Andy C. Rawstron. "Cyclooxygenase-2 (COX-2) in Multiple Myeloma: Prognostic Marker or Therapeutic Target?." Blood 108, no. 11 (November 16, 2006): 5051. http://dx.doi.org/10.1182/blood.v108.11.5051.5051.

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Abstract Cyclooxygenase-2 (COX-2) is the key enzyme involved in prostaglandin synthesis. It appears to support the growth of a number of solid tumours including colon, breast, ovary, lung and uterine cervix and may be an important therapeutic target in at least some of these tumours. COX-2 expression has recently been evaluated (by immunohistochemistry using polyclonal anti-COX-2 antibodies) in multiple myeloma (MM) where expression was documented in 33–57% of patients. COX-2 expression in these studies was strongly associated with an adverse outcome. In addition there is some emerging data to suggest that the use of aspirin in MM may improve survival rates. In order to further evaluate this we have used a monoclonal antibody (Clone SP21, Labvision, Fremont, Ca) to assess COX-2 expression in both normal and neoplastic plasma cells. 52 specimens were assessed using standard streptavidin-biotin immunoperoxidase techniques using a known COX-2+ colon cancer as a positive control. Strong uniform COX-2 expression was seen in 32/33 (97%) of myeloma patients assessed and was also documented in all patients with MGUS (n=10). COX-2 expression was also documented in reactive plasmacytic lesions (oral mucosa, skin and lymph node, n=6) as well as normal bone marrow plasma cells (n=6). Megakaryocytes stained positively in all bone marrow biopsies examined and provided a useful positive internal control while erythroid, myeloid and lymphoid cells were consistently negative. We would conclude that COX-2 is strongly expressed by both normal and neoplastic plasma cells suggesting that COX-2 is a potential therapeutic target in MM. The apparent increase in the proportion of myeloma patients expressing COX-2 in the present study reflects the use of a monoclonal antibody in our immunohistology studies. The fact that polyclonal antibodies identify a lower proportion of patients who appear to have an inferior outcome suggests that the level of expression is of prognostic significance rather than its presence or absence. This is worthy of further study using more appropriate techniques such as RQ-PCR.

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13

An, Min-Sung, Sang-Hyo Kim, Hye-Kyoung Yoon, and Woon-Won Kim. "Cox-2 Expression in Malignant Breast Tumors." Journal of the Korean Surgical Society 77, no. 6 (2009): 371. http://dx.doi.org/10.4174/jkss.2009.77.6.371.

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14

Menczer, Joseph, Letizia Schreiber, Oleg Sukmanov, Bernard Czernobilsky, Esther Berger, Abraham Golan, and Tally Levi. "COX-2 Expression in Nonepithelial Ovarian Malignancies." International Journal of Gynecological Pathology 30, no. 1 (January 2011): 41–45. http://dx.doi.org/10.1097/pgp.0b013e3181f29c6e.

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15

Lavalle, G. E., A. C. Bertagnolli, W. L. F. Tavares, and G. D. Cassali. "Cox-2 Expression in Canine Mammary Carcinomas." Veterinary Pathology 46, no. 6 (July 15, 2009): 1275–80. http://dx.doi.org/10.1354/vp.08-vp-0226-c-fl.

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16

Gaffney, David K., Joseph Holden, Karen Zempolich, Kelley J. Murphy, Adam P. Dicker, and Mark Dodson. "Elevated COX-2 Expression in Cervical Carcinoma." American Journal of Clinical Oncology 24, no. 5 (October 2001): 443–46. http://dx.doi.org/10.1097/00000421-200110000-00006.

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17

Nassar, Aziza, Anu Radhakrishnan, Isabel A. Cabrero, George Cotsonis, and Cynthia Cohen. "COX-2 Expression in Invasive Breast Cancer." Applied Immunohistochemistry & Molecular Morphology 15, no. 3 (September 2007): 255–59. http://dx.doi.org/10.1097/01.pai.0000213130.63417.b3.

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18

Young, Lisa E., Ashleigh E. Moore, and Dan A. Dixon. "429 MicroRNA Control of COX-2 Expression." Gastroenterology 134, no. 4 (April 2008): A—61—A—62. http://dx.doi.org/10.1016/s0016-5085(08)60291-7.

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19

Forones, Nora Manoukian, Kharen Yaemi Kawamura, Helena Regina Comodo Segreto, Ricardo Artigiani Neto, Gustavo Rubino de Azevedo Focchi, and Celina Tizuko Fujiyama Oshima. "Expression of COX-2 in Stomach Carcinogenesis." Journal of Gastrointestinal Cancer 39, no. 1-4 (March 2008): 4–10. http://dx.doi.org/10.1007/s12029-008-9039-6.

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20

Lysitsa, Stella, Jacky Samson, Christine Gerber-Wicht, Ursula Lang, and Tommaso Lombardi. "COX-2 Expression in Oral Lichen Planus." Dermatology 217, no. 2 (2008): 150–55. http://dx.doi.org/10.1159/000137672.

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21

Sokołowski, Grzegorz, Agata Bałdys-Waligórska, Małgorzata Trofimiuk, Dariusz Adamek, Alicja Hubalewska-Dydejczyk, and Filip Gołkowski. "Expression of cyclooxygenase-2 (COX-2) in pituitary tumours." Medical Science Monitor 18, no. 4 (2012): CR252—CR259. http://dx.doi.org/10.12659/msm.882625.

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22

Rossmeisl, J. H., J. L. Robertson, K. L. Zimmerman, M. A. Higgins, and D. A. Geiger. "Cyclooxygenase-2 (COX-2) expression in canine intracranial meningiomas." Veterinary and Comparative Oncology 7, no. 3 (September 2009): 173–80. http://dx.doi.org/10.1111/j.1476-5829.2009.00188.x.

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23

Onguru, Onder, Mehmet Gamsizkan, Cuneyt Ulutin, and Omer Gunhan. "Cyclooxygenase-2 (Cox-2) expression and angiogenesis in glioblastoma." Neuropathology 28, no. 1 (February 2008): 29–34. http://dx.doi.org/10.1111/j.1440-1789.2007.00828.x.

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24

L'Eplattenier, Henry F., Chen Li Lai, René Ham, Jan Mol, Frederick Sluijs, and Erik Teske. "Regulation of COX-2 Expression in Canine Prostate Carcinoma: Increased COX-2 Expression is Not Related to Inflammation." Journal of Veterinary Internal Medicine 21, no. 4 (July 2007): 776–82. http://dx.doi.org/10.1111/j.1939-1676.2007.tb03021.x.

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25

McGeer, Patrick L., Edith G. McGeer, and Koji Yasojima. "Expression of COX-1 and COX-2 mRNAs in atherosclerotic plaques." Experimental Gerontology 37, no. 7 (July 2002): 925–29. http://dx.doi.org/10.1016/s0531-5565(02)00028-1.

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26

Queiroga, F. L., A. Alves, I. Pires, and C. Lopes. "Expression of Cox-1 and Cox-2 in Canine Mammary Tumours." Journal of Comparative Pathology 136, no. 2-3 (February 2007): 177–85. http://dx.doi.org/10.1016/j.jcpa.2007.01.010.

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27

Saito, Takayuki, Ian W. Rodger, Hani Shennib, Fu Hu, Lara Tayara, and Adel Giaid. "Cyclooxygenase-2 (COX-2) in acute myocardial infarction: cellular expression and use of selective COX-2 inhibitor." Canadian Journal of Physiology and Pharmacology 81, no. 2 (February 1, 2003): 114–19. http://dx.doi.org/10.1139/y03-023.

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Our previous work has shown strong expression of COX-2 in the myocardium of patients with end-stage ischemic heart failure. The purpose of this study was to determine the cellular expression of this enzyme in the setting of acute myocardial infarction (AMI) and determine the role of COX-2 in experimental animals using a selective COX-2 inhibitor. Experimental AMI was induced in rats by ligating the left coronary artery. Animals were either treated with a selective COX-2 inhibitor (5 mg·kg1·day1) or vehicle. Three days after ligation, cardiac function was assessed and infarct size was determined. Myocardial specimens were immunostained with antiserum to COX-2. Plasma concentration of prostanoids was measured by enzyme immunoassay. There was strong expression of COX-2 in the myocytes, endocardium, vascular endothelial cells, and macrophages in the infarcted zone of the myocardium. In contrast, little expression was seen in the myocardium of control rats. Animals treated with the COX-2 inhibitor showed a significant improvement in left ventricular (LV) end-diastolic pressure (P < 0.05) and LV systolic pressure (P < 0.01), and a reduction in infarct size (P < 0.05). Inhibition of COX-2 significantly decreased plasma concentration of thromboxane B2 (P < 0.05); however, it did not affect 6-keto-prostaglandin F1α. Induction of COX-2 during AMI appears to contribute to myocardial injury, and treatment with the specific inhibitor of the enzyme ameliorated the course of the disease.Key words: cyclooxygenase-2, inhibitor, acute myocardial infarction.

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28

GÖKSU EROL, Y. Azize, Çiğdem TOKYOL, Öner ÖZDEMİR, Mehmet YILMAZER, Dağıstan Tolga ARIÖZ, and Fatma AKTEPE. "VEGF and COX-2 Expression in Endometrial Carcinoma." Turkiye Klinikleri Journal of Medical Sciences 32, no. 1 (2012): 80–87. http://dx.doi.org/10.5336/medsci.2010-22258.

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29

Radi, Zaher A., and Robert Ostroski. "Pulmonary and Cardiorenal Cyclooxygenase-1 (COX-1), -2 (COX-2), and Microsomal Prostaglandin E Synthase-1 (mPGES-1) and -2 (mPGES-2) Expression in a Hypertension Model." Mediators of Inflammation 2007 (2007): 1–8. http://dx.doi.org/10.1155/2007/85091.

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Hypertensive mice that express the human renin and angiotensinogen genes are used as a model for human hypertension because they develop hypertension secondary to increased renin-angiotensin system activity. Our study investigated the cellular localization and distribution of COX-1, COX-2, mPGES-1, and mPGES-2 in organ tissues from a mouse model of human hypertension. Male (n=15) and female (n=15) double transgenic mice (h-Ang 204/1 h-Ren 9) were used in the study. Lung, kidney, and heart tissues were obtained from mice at necropsy and fixed in 10%neutral buffered formalin followed by embedding in paraffin wax. Cut sections were stained immunohistochemically with antibodies to COX-1, COX-2, mPGES-1, and mPGES-2 and analyzed by light microscopy. Renal expression of COX-1 was the highest in the distal convoluted tubules, cortical collecting ducts, and medullary collecting ducts; while proximal convoluted tubules lacked COX-1 expression. Bronchial and bronchiolar epithelial cells, alveolar macrophages, and cardiac vascular endothelial cells also had strong COX-1 expression, with other renal, pulmonary, or cardiac microanatomic locations having mild-to-moderate expression. mPGES-2 expression was strong in the bronchial and bronchiolar epithelial cells, mild to moderate in various renal microanatomic locations, and absent in cardiac tissues. COX-2 expression was strong in the proximal and distal convoluted tubules, alveolar macrophages, and bronchial and bronchiolar epithelial cells. Marked mPGES-1 was present only in bronchial and bronchiolar epithelial cells; while mild-to-moderate expression was present in other pulmonary, renal, or cardiac microanatomic locations. Expression of these molecules was similar between males and females. Our work suggests that in hypertensive mice, there are (a) significant microanatomic variations in the pulmonary, renal, and cardiac distribution and cellular localization of COX-1, COX-2, mPGES-1, and mPGES-2, and (b) no differences in expression between genders.

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30

Kotnik, Primož, Jakob Nielsen, Tae-Hwan Kwon, Ciril Kržišnik, Jørgen Frøkiær, and Søren Nielsen. "Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus." American Journal of Physiology-Renal Physiology 288, no. 5 (May 2005): F1053—F1068. http://dx.doi.org/10.1152/ajprenal.00114.2004.

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Prostaglandins have an important role in renal salt and water reabsorption. PGE2 is the main kidney prostaglandin and is thought to be mainly produced in the kidney inner medulla (IM). There are indications that PGE2 synthesis in nephrogenic (NDI) and central (CDI) diabetes insipidus is altered. We hypothesize that the expression of the major PGE2 synthesis enzymes cyclooxygenases 1 and 2 (COX-1, COX-2) and membrane-associated PGE2 synthase (mPGES) is altered in the kidneys of rats with NDI and CDI. Wistar rats treated with lithium for 4 wk were used as the NDI model. One-half of the NDI model rats were additionally dehydrated for 48 h. Brattleboro (BB) rats that lack endogenous antidiuretic hormone were used as the CDI model. Expression and localization of COX-1, COX-2, and mPGES in IM, inner stripe of outer medulla (ISOM), and cortex were determined by immunoblotting and immunohistochemistry. In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM. In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered. COX-2 expression was undetected in ISOM and marginally increased in cortex. Consistent with this, the density of COX-2-expressing cells in macula densa was significantly increased, indicating differential regulation of COX-2 in IM and cortex. Dehydration of NDI rats resulted in a marked increase in COX-2 immunolabeling in IM interstitial cells, and there was no significant change in COX-1 and mPGES expression in any kidney zone. Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM. In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased. These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI. Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.

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31

Paneesha, S., E. Leung, Anton Borg, Peter Rose, and Alan G. Morris. "Cycloxygenase-2 (COX-2) Expression Is More in Clonal Plasma Cells." Blood 106, no. 11 (November 16, 2005): 5103. http://dx.doi.org/10.1182/blood.v106.11.5103.5103.

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Abstract Multiple myeloma is characterised by deregulated cytokine network with secretion of inflammatory cytokines. Recent studies have showed the independent poor prognostic value of COX-2 expression in myeloma. We have here studied the COX-2 expression in plasma cells from patients with myeloma, monoclonal gammopathy of undetermined significance (MGUS), Waldenstrom’s Macroglobulinemia (WM) and compared with the COX-2 expression by normal plasma cells. Methods: Our study included bone marrow samples from 34 patients (Lymphoma: 15; myeloma: 10; MGUS: 7; WM: 1; Amyloidosis: 1). Mononuclear cells were harvested from the bone marrow samples by density gradient sedimentation using Lymphoprep TM from Axis-Shield, Norway. Mononuclear cells were stained with PE conjugated CD 38 (BD Bioscience) and APC conjugated CD138 (BD Bioscience). FITC conjugated IgG against human COX-2 (Cayman Chemical) was used to study the expression of cycloxygenase-2 following permeabilization with fix and perm kit (Caltag). Flow cytometry was performed on a Becton Dickinson FACS vantage with appropriate isotype controls. The colorectal cell line HT- 29 and human myeloma cell line RPMI 8226 were used as positive controls and the flow results are validated by western blotting and Prostaglandin E2 EIA assay (Cayman Chemical). Results: HT-29 cell line showed a peak fluorescence of 58 for COX-2, where as RPMI 8226 cell line revealed peak fluorescence of 141. Median plasma cell count in bone marrow of patients with MGUS was 2 %( range 2–6%). Plasma cells from MGUS patients revealed median peak fluorescence for COX-2 was 37(range: 9–74). Median plasma cell count in bone marrow of patients with myeloma was 25% (range: 10–59%). Median peak fluorescence for COX-2 in plasma cells from patients with myeloma was 24(range: 10–85). Median plasma cell count in bone marrow of patients with lymphoma was 1 %( range1–4%). Median peak fluorescence for COX-2 in plasma cells from patients with lymphoma was 11(range: 2–38). Conclusions: Our study reveals COX-2 expression is more in clonal plasma cells as compared to normal plasma cells. Studies are needed to ascertain the role of COX-2 in oncogenesis in myeloma and to discover how COX-2 expression leads to poor outcome in patients with myeloma. This information may lead to the therapeutic role of selective COX-2 inhibitors in the therapy of myeloma.

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32

To, KF, FKL Chan, WK Leung, and JY Sung. "Expression of cyclooxygenase 1 (Cox-1) and 2 (Cox-2) in H. Pylori associated gastritis." Gastroenterology 114 (April 1998): A310. http://dx.doi.org/10.1016/s0016-5085(98)81260-2.

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33

Nassar, Mahmoud Ismail Ahmed, Shaimaa M. M. Bebars, Rasha Mohamed Samir Said, and Taghreed Mohammed Amin Mustafa. "Immunohistochemical Expression of Cyclooxygenase-2 (COX-2) in Breast Cancer." Egyptian Journal of Hospital Medicine 75, no. 3 (April 1, 2019): 2397–405. http://dx.doi.org/10.21608/ejhm.2019.30955.

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34

Prayson, Richard A., Elias A. Castilla, Michael A. Vogelbaum, and Gene H. Barnett. "Cyclooxygenase-2 (COX-2) expression by immunohistochemistry in glioblastoma multiforme." Annals of Diagnostic Pathology 6, no. 3 (June 2002): 148–53. http://dx.doi.org/10.1053/adpa.2002.33900.

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35

Fujihara, Clarice Kazue, Gláucia Rutigliano Antunes, A. N. A. Lúcia Mattar, Natalie Andreoli, Denise Maria Avancini, Costa Malheiros, Irene Lourdes Noronha, and Roberto Zatz. "Cyclooxygenase-2 (COX-2) inhibition limits abnormal COX-2 expression and progressive injury in the remnant kidney." Kidney International 64, no. 6 (December 2003): 2172–81. http://dx.doi.org/10.1046/j.1523-1755.2003.00319.x.

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36

Rossiello, Luigi, Eleonora Ruocco, Giuseppe Signoriello, Pietro Micheli, Monica Rienzo, Claudio Napoli, and Raffaele Rossiello. "Evidence of COX-1 and COX-2 expression in Kaposi’s sarcoma tissues." European Journal of Cancer 43, no. 8 (May 2007): 1232–41. http://dx.doi.org/10.1016/j.ejca.2007.03.016.

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37

Hayes, A., T. Scase, J. Miller, S. Murphy, A. Sparkes, and V. Adams. "COX-1 and COX-2 Expression in Feline Oral Squamous Cell Carcinoma." Journal of Comparative Pathology 135, no. 2-3 (August 2006): 93–99. http://dx.doi.org/10.1016/j.jcpa.2006.06.001.

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38

Keum, Hyo Sub, Yong Seop Lee, Kyung Rae Kim, Chul Won Park, Kyung Tae, and Seung Sam Paik. "Expression of COX-2 in Salivary Gland Tumor." Journal of Clinical Otolaryngology Head and Neck Surgery 17, no. 1 (May 2006): 66–72. http://dx.doi.org/10.35420/jcohns.2006.17.1.66.

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DO CARMO, ANDRÉIA FERREIRA, AMANDA KATARINNY GOES GONZAGA, MARIA LUIZA DINIZ DE SOUSA LOPES, CASSIANO FRANCISCO WEEGE NONAKA, LÉLIA MARIA GUEDES QUEIROZ, ÉRICKA JANINE DANTAS DA SILVEIRA, and ANA MIRYAM COSTA DE MEDEIROS. "IMMUNOHISTOCHEMICAL EXPRESSION OF COX-2 IN ACTINIC CHEILITIS." Oral Surgery, Oral Medicine, Oral Pathology and Oral Radiology 124, no. 2 (August 2017): e131. http://dx.doi.org/10.1016/j.oooo.2017.05.356.

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Kim, Sang Jin, Jae Hak Lee, Ji Sung Yoon, Ji O. Mok, Yeo Joo Kim, Hyeong Kyu Park, Chul Hee Kim, Dong Won Byun, Kyo Il Suh, and Myung Hi Yoo. "Immunohistochemical Expression of COX-2 in Thyroid Nodules." Korean Journal of Internal Medicine 18, no. 4 (December 31, 2003): 225–29. http://dx.doi.org/10.3904/kjim.2003.18.4.225.

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Giordano, Giovanna, Nicoletta Campanini, Vittoria Donofrio, Patrizia Bertolini, Jessica Falleti, Chiara Grassani, and Guido Pettinato. "Analysis of Cox-2 expression in Wilms’ tumor." Pathology - Research and Practice 204, no. 12 (December 2008): 875–82. http://dx.doi.org/10.1016/j.prp.2008.06.008.

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42

Tanaka, Shinji, Jack R. Wands, and Shigeki Arii. "Induction of Angiopoietin-2 gene expression by COX-2: A novel role for COX-2 inhibitors during hepatocarcinogenesis." Journal of Hepatology 44, no. 1 (January 2006): 233–35. http://dx.doi.org/10.1016/j.jhep.2005.09.012.

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43

Lipari, L., A. Mauro, S. Gallina, S. Tortorici, M. Buscemi, S. Tetè, and A. Gerbino. "Expression of Gelatinases (MMP-2, MMP-9) and Cyclooxygenases (COX-1, COX-2) in Some Benign Salivary Gland Tumors." International Journal of Immunopathology and Pharmacology 25, no. 1 (January 2012): 107–15. http://dx.doi.org/10.1177/039463201202500113.

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Salivary gland tumors, most of which are rare benign tumors, represent a histologically heterogenous group with the greatest diversity of morphological and cellular features. The aim of this study is to analyse the expression and possible interactions between gelatinases (MMP-2, MMP-9) and cyclooxygenases (COX-1, COX-2) in some benign salivary gland tumors. We investigated the expression of gelatinases and cyclooxigenases in control salivary gland, Pleomorphic adenoma and Warthin's tumor through immunohistochemistry and Reverse Transcription – Polymerase Chain Reaction (PCR). We identified the expression of both classes of enzyme in normal samples and in the two types of pathological samples without any quantitative differences. From the present data no significant differences emerge in the expression of these enzymes among the different pathologies examined. Nevertheless, due to the small number of samples included in this study, general statements regarding correlation between the degree of severity of the tumoral pathology and the quantitative expression of these potential tumoral markers can not be made.

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44

Nakano, Masashi, Naoyuki Denda, Misako Matsumoto, Michiko Kawamura, Yasuaki Kawakubo, Ko Hatanaka, Yoshisuke Hiramoto, Yu-ichi Sato, Makoto Noshiro, and Yoshiteru Harada. "Interaction between cyclooxygenase (COX)-1- and COX-2-products modulates COX-2 expression in the late phase of acute inflammation." European Journal of Pharmacology 559, no. 2-3 (March 2007): 210–18. http://dx.doi.org/10.1016/j.ejphar.2006.11.080.

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45

Raghav, Kanwal Pratap Singh, Syed Mohammad Ali Kazmi, Aditya V. Shetty, Melissa W. Taggart, Keith F. Fournier, Richard E. Royal, Paul F. Mansfield, Cathy Eng, Robert A. Wolff, and Michael J. Overman. "Prognostic and predictive effect of COX-2 expression in appendiceal adenocarcinomas." Journal of Clinical Oncology 30, no. 4_suppl (February 1, 2012): 526. http://dx.doi.org/10.1200/jco.2012.30.4_suppl.526.

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526 Background: Cyclooxygenase-2 (COX-2), an inducible isoenzyme, is upregulated in inflammation and involved in cancer progression by promoting angiogenesis, cell proliferation and migration and by inhibiting apoptosis. COX-2 is implicated in colorectal tumorigenesis and by extension COX-2 expression testing and therapeutic inhibition has been considered in appendiceal adenocarcinomas (AAs). However, its role in this setting has never been well studied. The purpose of our study was to investigate COX-2 expression in AAs and to evaluate its prognostic and predictive significance. Methods: We performed a retrospective review of 607 patients with AAs treated at MD Anderson Cancer Center between 2002 and 2010. Immunohistochemistry was performed for COX-2 expression (COX2 mAb Clone CX229, Cayman Chemical) in 49 (8%) patients. Thirty (61%) stained positive and 19 (39%) showed no staining. Kaplan-Meier product limit method and log-rank test were used to estimate overall survival (OS) and to determine association between OS, COX-2 expression and other characteristics. Results: Median age at diagnosis was 47 yrs (range 34-78 yrs). Grade (P = 0.003), completeness of cytoreduction score (P = 0.010) and stage (P = 0.023) were significantly associated with OS. Median OS for patients with COX-2 positive and COX-2 negative tumors was 58.3 and 42.8 months, respectively (P = 0.232). Nine COX-2 positive patients received celecoxib (selective COX-2 inhibitor) in combination with other chemotherapy. Mean treatment duration was 5.5 months with best radiographic response being stable disease in 7 patients. Reduction in tumor markers (CEA or CA19-9) was seen in 7 cases (median reduction of 30%). Similar treatment duration (6.6 months), rate of stable disease (6/8 pts) and tumor marker reduction (7/8 pts) was seen on the preceding non-celecoxib containing chemotherapy in these patients. Median OS, with and without COX-2 inhibition, was 55.7 and 57.6 months respectively (P = 0.57). Conclusions: In this cohort, COX-2 expression is not a significant prognostic factor in AAs. Benefit from COX-2 inhibition in COX-2 expressing AAs is unclear. Current data does not support the routine use of either COX-2 testing or COX-2 inhibition therapy in AAs.

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Haworth, Richard, Keli Oakley, Nicola McCormack, and Andrew Pilling. "Differential Expression of COX-1 and COX-2 in the Gastrointestinal Tract of the Rat." Toxicologic Pathology 33, no. 2 (February 2005): 239–45. http://dx.doi.org/10.1080/01926230590906512.

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The aim of this study was to use immunohistochemistry with morphometry to investigate COX-1 and COX-2 expression in the normal rat gastrointestinal (GI) tract and examine if sites of ulceration previously observed with long-term COX-2 inhibitor administration in mice correlate with differential COX-1/COX-2 expression. COX-2 positive cells were observed predominantly in the apical lamina propria of intestinal villi with fewer cells in the mucosal epithelium. The highest level of COX-2 expression was observed at the ileocaecal junction (ICJ). COX-2 expression was also present in parasympathetic ganglia of the submucosa and muscularis. In the stomach, the highest grade of COX-2 expression was observed in the apical lamina propria of the fundus adjacent to the junctional ridge. In contrast, COX-1 positive cells within the lamina propria were evenly distributed along the GI tract but were present in higher numbers than COX-2 positive cells. The mean level of COX-1 expression at the ICJ was not significantly different from the ileum and caecum. Evidence that the highest level of COX-2 expression in normal rats is located on the ileal side of the ICJ provides the first mechanism to explain spontaneous ulceration and perforation of the distal ileum in COX-2−/− animals.

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Higashi, Yuko, Takuro Kanekura, and Tamotsu Kanzaki. "Enhanced expression of cyclooxygenase (COX)-2 in human skin epidermal cancer cells: Evidence for growth suppression by inhibiting COX-2 expression." International Journal of Cancer 86, no. 5 (June 1, 2000): 667–71. http://dx.doi.org/10.1002/(sici)1097-0215(20000601)86:5<667::aid-ijc10>3.0.co;2-y.

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48

Athavale, R., K. Clooney, J. O'HAGAN, H. Shawki, A. H. Clark, and J. A. Green. "COX-1 and COX-2 expression in stage I and II invasive cervical carcinoma: relationship to disease relapse and long-term survival." International Journal of Gynecologic Cancer 16, no. 3 (2006): 1303–8. http://dx.doi.org/10.1136/ijgc-00009577-200605000-00053.

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COX-1 and COX-2 are members of the cyclooxygenase (COX) family, which influence tumor invasion and apoptosis. The objective of the study was to assess the relationship between COX-1 and COX-2 expression in early-stage disease and subsequent disease relapse and long-term survival. Women with FIGO stage I and II cervical carcinoma, younger than 50 years, treated between 1981 and 1990 were included. COX-1 and COX-2 expressions in the tumors were assessed by immunohistochemistry. COX-1 and COX-2 were expressed in 61% (17/28) and 57% (16/28) of tumors, respectively. COX-1 nonexpressers showed an improved overall survival compared to expressers (log-rank test, P = 0.09). There was no significant difference in the overall survival in COX-2 nonexpressers compared to expressers (P = 0.6). Out of eight women with disease relapse, COX-1 or COX-2 expression was noted in six of eight tumors, and both were expressed in five of eight tumors. Our preliminary data suggest an adverse prognosis with COX-1 expression in early-stage cervical carcinoma and a trend toward COX-1 expression in disease relapse. The association between COX-2 expression and a worse prognosis was not proven in this study.

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Ogata, S., Y. Kubota, T. Yamashiro, H. Takeuchi, T. Ninomiya, Y. Suyama та K. Shirasuna. "Signaling Pathways Regulating IL-1α-induced COX-2 Expression". Journal of Dental Research 86, № 2 (лютий 2007): 186–91. http://dx.doi.org/10.1177/154405910708600215.

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Interleukin-1α(IL-1α) stimulates the production of prostaglandin E2 (PGE2) in odontogenic keratocyst fibroblasts. However, the signaling pathways remain obscure. In this study, we investigated IL-1αsignaling pathways that regulate cyclooxygenase-2 (COX-2) expression in odontogenic keratocyst fibroblasts. IL-1αincreased the expression of COX-2 mRNA and protein, and PGE2 secretion in the fibroblasts. IL-1αincreased the phosphorylation of extracellular signal-regulated protein kinase-1/2 (ERK1/2), p38 mitogen-activated protein kinase (MAPK), and c-Jun N-terminal kinase (JNK). PD-98059, SB-203580, SP-600125, and PDTC—which are inhibitors of ERK1/2, p38, JNK, and nuclear factor-κB (NF-κB), respectively—attenuated the IL-1α-induced COX-2 mRNA expression and activated protein kinase C PGE2 secretion. IL-1α(PKC), and PKC inhibitor staurosporine inhibited IL-1α-induced phosphorylation of ERK1/2, p38, and JNK, and decreased IL-1α-induced COX-2 mRNA expression. Thus, in odontogenic keratocyst fibroblasts, IL-1αmay stimulate COX-2 expression both through the PKC-dependent activation of ERK1/2, p38, and JNK signaling pathways, and through the NF-κB cascade.

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50

Zarrilli, Raffaele, Concetta Tuccillo, Marietta Santangelo, Gerardo Nardone, and Marco Romano. "Increased COX-2, But Not COX-1, mRNA Expression in Helicobacter pylori Gastritis." American Journal of Gastroenterology 94, no. 11 (November 1999): 3376–78. http://dx.doi.org/10.1111/j.1572-0241.1999.03376.x.

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