Ignet

Gene Information

Gene symbol: PTGS1

Gene name: prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase)

HGNC ID: 9604

Synonyms: COX1, PGHS-1, PTGHS

Related Genes

#	Gene Symbol	Number of hits
1	AKR1B1	1 hits
2	ALOX12	1 hits
3	ALOX5	1 hits
4	AVP	1 hits
5	CASP3	1 hits
6	CEBPB	1 hits
7	CNR1	1 hits
8	CNR2	1 hits
9	COX8A	1 hits
10	FOS	1 hits
11	GP6	1 hits
12	HTR2B	1 hits
13	IL1B	1 hits
14	IL6	1 hits
15	INS	1 hits
16	LEP	1 hits
17	MMP9	1 hits
18	MT-CO3	1 hits
19	NOS1	1 hits
20	NOS2A	1 hits
21	NOS3	1 hits
22	NPC1	1 hits
23	P2RY2	1 hits
24	P2RY4	1 hits
25	P2RY6	1 hits
26	PLA2G1B	1 hits
27	PTGDS	1 hits
28	PTGES	1 hits
29	PTGIS	1 hits
30	PTGS2	1 hits
31	PVALB	1 hits
32	SIRT1	1 hits
33	TIMP1	1 hits
34	TNF	1 hits

Related Sentences

#	PMID	Sentence
1	7620513	Prostacyclin formation by endothelial cells in atherosclerosis and diabetes is reviewed and the synthesis of prostacyclin by cyclooxygenase 1 and 2 (COX-1 and COX-2) is discussed.
2	9051726	Expression of constitutive cyclo-oxygenase (COX-1) in rats with streptozotocin-induced diabetes; effects of treatment with evening primrose oil or an aldose reductase inhibitor on COX-1 mRNA levels.
3	9051726	Evening primrose oil (EPO) treatment increased COX-1 mRNA in nerve and retina to levels in diabetic rats that were higher than those of non-diabetic controls (1.21 +/- 0.28 for nerve and 0.065 +/- 0.017 for retina, where control retinae gave 0.031 +/- 0.020-see above for nerve).
4	9051726	Treatment of diabetic rats with an aldose reductase inhibitor was without effect on COX-1 mRNA levels in the tissues examined.
5	9051726	Apart from providing arachidonate as substrate for COX, EPO stimulates COX-1 expression in some tissues.
6	9051726	Expression of constitutive cyclo-oxygenase (COX-1) in rats with streptozotocin-induced diabetes; effects of treatment with evening primrose oil or an aldose reductase inhibitor on COX-1 mRNA levels.
7	9051726	Evening primrose oil (EPO) treatment increased COX-1 mRNA in nerve and retina to levels in diabetic rats that were higher than those of non-diabetic controls (1.21 +/- 0.28 for nerve and 0.065 +/- 0.017 for retina, where control retinae gave 0.031 +/- 0.020-see above for nerve).
8	9051726	Treatment of diabetic rats with an aldose reductase inhibitor was without effect on COX-1 mRNA levels in the tissues examined.
9	9051726	Apart from providing arachidonate as substrate for COX, EPO stimulates COX-1 expression in some tissues.
10	9051726	Expression of constitutive cyclo-oxygenase (COX-1) in rats with streptozotocin-induced diabetes; effects of treatment with evening primrose oil or an aldose reductase inhibitor on COX-1 mRNA levels.
11	9051726	Evening primrose oil (EPO) treatment increased COX-1 mRNA in nerve and retina to levels in diabetic rats that were higher than those of non-diabetic controls (1.21 +/- 0.28 for nerve and 0.065 +/- 0.017 for retina, where control retinae gave 0.031 +/- 0.020-see above for nerve).
12	9051726	Treatment of diabetic rats with an aldose reductase inhibitor was without effect on COX-1 mRNA levels in the tissues examined.
13	9051726	Apart from providing arachidonate as substrate for COX, EPO stimulates COX-1 expression in some tissues.
14	9051726	Expression of constitutive cyclo-oxygenase (COX-1) in rats with streptozotocin-induced diabetes; effects of treatment with evening primrose oil or an aldose reductase inhibitor on COX-1 mRNA levels.
15	9051726	Evening primrose oil (EPO) treatment increased COX-1 mRNA in nerve and retina to levels in diabetic rats that were higher than those of non-diabetic controls (1.21 +/- 0.28 for nerve and 0.065 +/- 0.017 for retina, where control retinae gave 0.031 +/- 0.020-see above for nerve).
16	9051726	Treatment of diabetic rats with an aldose reductase inhibitor was without effect on COX-1 mRNA levels in the tissues examined.
17	9051726	Apart from providing arachidonate as substrate for COX, EPO stimulates COX-1 expression in some tissues.
18	9465095	Basal expression of cyclooxygenase-2 and nuclear factor-interleukin 6 are dominant and coordinately regulated by interleukin 1 in the pancreatic islet.
19	9465095	The enzyme cyclooxygenase (COX)-1 is constitutive whereas COX-2 is regulated in virtually all tissues.
20	9465095	To assess whether this dogma holds true in the pancreatic islet, we examined basal and interleukin (IL)-1-regulated expression of COX-2 in HIT-T15 cells, Syrian hamster and human islets, and other Syrian hamster tissues.
21	9465095	We found that COX-2, and not COX-1, gene expression is dominant in pancreatic islet tissue under both basal and IL-1-stimulated conditions.
22	9465095	Basal and IL-1-stimulated prostaglandin E2 synthesis were blocked by a specific COX-2 inhibitor.
23	9465095	IL-1 stimulation had a biphasic effect on COX-2 mRNA levels with an initial mild increase at 2-4 hr followed by a more dramatic decrease below basal level by 24 hr.
24	9465095	The IL-1-induced increase in COX-2 mRNA levels was accompanied by a parallel increase in NF-kappaB binding to COX-2 promoter elements.
25	9465095	The subsequent decrease in COX-2 mRNA levels was accompanied by a parallel decrease in NF-IL-6 binding activity and COX-2 promoter activity.
26	9465095	Specific mutation of the NF-IL-6 binding motif within the COX-2 promoter reduced basal promoter activity by 50% whereas mutation of the NF-kappaB motif had no effect.
27	9465095	These studies provide documentation of NF-IL-6 in the pancreatic islet and that COX-2, rather than COX-1, is dominantly expressed.
28	9465095	They suggest coordinate regulation by IL-1 of COX-2 mRNA, NF-kappaB, and NF-IL-6 and raise the issue of whether intrinsically high levels of COX-2 gene expression predisposes the normal islet for microenvironmentally induced overproduction of islet prostaglandin E2.
29	9465095	Basal expression of cyclooxygenase-2 and nuclear factor-interleukin 6 are dominant and coordinately regulated by interleukin 1 in the pancreatic islet.
30	9465095	The enzyme cyclooxygenase (COX)-1 is constitutive whereas COX-2 is regulated in virtually all tissues.
31	9465095	To assess whether this dogma holds true in the pancreatic islet, we examined basal and interleukin (IL)-1-regulated expression of COX-2 in HIT-T15 cells, Syrian hamster and human islets, and other Syrian hamster tissues.
32	9465095	We found that COX-2, and not COX-1, gene expression is dominant in pancreatic islet tissue under both basal and IL-1-stimulated conditions.
33	9465095	Basal and IL-1-stimulated prostaglandin E2 synthesis were blocked by a specific COX-2 inhibitor.
34	9465095	IL-1 stimulation had a biphasic effect on COX-2 mRNA levels with an initial mild increase at 2-4 hr followed by a more dramatic decrease below basal level by 24 hr.
35	9465095	The IL-1-induced increase in COX-2 mRNA levels was accompanied by a parallel increase in NF-kappaB binding to COX-2 promoter elements.
36	9465095	The subsequent decrease in COX-2 mRNA levels was accompanied by a parallel decrease in NF-IL-6 binding activity and COX-2 promoter activity.
37	9465095	Specific mutation of the NF-IL-6 binding motif within the COX-2 promoter reduced basal promoter activity by 50% whereas mutation of the NF-kappaB motif had no effect.
38	9465095	These studies provide documentation of NF-IL-6 in the pancreatic islet and that COX-2, rather than COX-1, is dominantly expressed.
39	9465095	They suggest coordinate regulation by IL-1 of COX-2 mRNA, NF-kappaB, and NF-IL-6 and raise the issue of whether intrinsically high levels of COX-2 gene expression predisposes the normal islet for microenvironmentally induced overproduction of islet prostaglandin E2.
40	10102698	Neither hyperglycemia nor diabetes altered COX-1 expression, but embryonic COX-2 expression was diminished on gestational day 10.
41	11285308	We explored COX-1 and COX-2 expression and hemodynamic responses to the COX-1 inhibitor valeryl salicylate (VS) or the COX-2 inhibitor NS398 in moderately hyperglycemic, streptozotocin-diabetic (D) and control (C) rats.
42	11285308	In conclusion, we documented an increase in renal cortical COX-2 protein expression associated with a different renal hemodynamic response to selective systemic COX-2 inhibition in D as compared with C animals, indicating a role of COX-2-derived PG in pathological renal hemodynamic changes in diabetes.
43	11427483	We have investigated the possible functional relationships between cellular invasion pathways induced by trefoil factors (TFFs), src, and the cyclooxygenases COX-1 and COX-2.
44	11427483	Pharmacological inhibitors of the Rho small GTPase (C3 exoenzyme), phospholipase C (U-73122), cyclooxygenases (SC-560, NS-398), and the thromboxane A2 receptor (TXA2-R) antagonist SQ-295 completely abolished invasion induced by intestinal trefoil factor, pS2, and src in kidney and colonic epithelial cells MDCKts.src and PCmsrc.
45	11427483	Ectopic overexpression of pS2 cDNA and protein in MDCKts.src-pS2 cells and human colorectal cancer cells HCT8/S11-pS2 initiate distinct invasion signals that are Rho independent and COX and TXA2-R dependent.
46	11427483	This led to activation of the TXA2-R-dependent invasion pathway, which is monitored via a Rho- and Galpha12/Galpha13-independent mechanism using the Galphaq/PKC signaling cascade.
47	11597987	Moreover, the specific contributions of the different isoforms (PGHS-1 and PGHS-2) are discussed.
48	11788351	Peroxynitrite increases iNOS through NF-kappaB and decreases prostacyclin synthase in endothelial cells.
49	11788351	The endothelium-derived enzymes nitric oxide synthase (NOS) and prostaglandin H synthase (PGHS) mediate vascular reactivity and contain oxidant-sensitive isoforms (iNOS and PGHS-2) that can be induced by nuclear factor (NF)-kappaB activation.
50	11788351	We hypothesized that peroxynitrite will increase levels of iNOS and PGHS-2 through activation of NF-kappaB.
51	11788351	Western immunoblots of endothelial cells show that 3-morpholinosydnonimine (SIN-1; 0.5 mM), a peroxynitrite donor, increased iNOS protein mass, which can be inhibited by pyrroline dithiocarbamate (an NF-kappaB inhibitor) (167 +/- 24.2 vs. 78 +/- 19%, P < 0.05, n = 6).
52	11788351	Endothelial NOS, PGHS-1, and PGHS-2 protein levels were not altered by SIN-1.
53	11906326	Cyclooxygenase, the rate-limiting enzyme in prostaglandin synthesis, is expressed in constitutive (COX-1) and inducible (COX-2) isoforms.
54	11906326	High mucin COX-2 from goblet cells may increase luminal prostaglandin synthesis, alter epithelial permeability, modulate intestinal immune responses and modify functional properties of the lymphocytes in the GALT, which all may be important for the initiation of the autoimmune phenomenon in the NOD mice.
55	12145179	The effects of nonselective COX inhibition with flurbiprofen were contrasted with selective COX-2 inhibition with meloxicam, administered alone and in combination with ALC in nondiabetic (ND) and streptozotocin-induced diabetic (STZ-D) rats.
56	12145179	Western blot analysis showed unchanged sciatic nerve COX-1 protein but increased COX-2 protein abundance in STZ-D versus ND rats.
57	12145179	These results imply 1) a tonic role of the COX-1 pathway in the regulation of nerve osmolytes and Na,K-ATPase activity and the maintenance of NBF in ND animals and 2) activation of the COX-2 pathway as an important mediator of NBF and MNCV deficits in EDN.
58	12145179	The effects of nonselective COX inhibition with flurbiprofen were contrasted with selective COX-2 inhibition with meloxicam, administered alone and in combination with ALC in nondiabetic (ND) and streptozotocin-induced diabetic (STZ-D) rats.
59	12145179	Western blot analysis showed unchanged sciatic nerve COX-1 protein but increased COX-2 protein abundance in STZ-D versus ND rats.
60	12145179	These results imply 1) a tonic role of the COX-1 pathway in the regulation of nerve osmolytes and Na,K-ATPase activity and the maintenance of NBF in ND animals and 2) activation of the COX-2 pathway as an important mediator of NBF and MNCV deficits in EDN.
61	12184997	With the use of long primers (43 bp) derived from regions of homology between zebrafish and rainbow trout COX-2 genes, a 600-bp product was amplified from SRG and was found to be almost equally homologous to mammalian COX-1 and COX-2 (65%).
62	12184997	The longest open reading frame encodes a 593-amino acid protein that has 68 and 64% homology to mammalian COX-1 and COX-2, respectively.
63	12184997	The key residues in the active site (Try(385), His(388), and Ser(530)) are conserved between the shark and mammalian COX. sCOX contains Val(523) that has been shown to be a key residue determining the sensitivity to COX-2-specific inhibitors including NS-398.
64	12184997	With the use of long primers (43 bp) derived from regions of homology between zebrafish and rainbow trout COX-2 genes, a 600-bp product was amplified from SRG and was found to be almost equally homologous to mammalian COX-1 and COX-2 (65%).
65	12184997	The longest open reading frame encodes a 593-amino acid protein that has 68 and 64% homology to mammalian COX-1 and COX-2, respectively.
66	12184997	The key residues in the active site (Try(385), His(388), and Ser(530)) are conserved between the shark and mammalian COX. sCOX contains Val(523) that has been shown to be a key residue determining the sensitivity to COX-2-specific inhibitors including NS-398.
67	12397372	Unlike most other mammalian cells, beta-cells of Langerhans constitutively express cyclooxygenase (COX)-2 rather than COX-1.
68	12397372	Immunostaining showed that COX-2 is expressed in islet-infiltrating macrophages, and that the expression of insulin and COX-2 disappeared concomitantly from the beta-cells when NOD mice progressed toward overt diabetes.
69	12397372	Also cultured INS-1E cells coexpressed insulin and COX-2 but clearly in different subcellular compartments.
70	12397372	The effects of celecoxib on INS-1E cells suggest that PGE(2) and other downstream products of COX-2 may contribute to the regulation of insulin release from the beta-cells.
71	12576525	Role of cyclooxygenases COX-1 and COX-2 in modulating adipogenesis in 3T3-L1 cells.
72	12576525	Two COX isoforms have been identified, COX-1, the constitutive form, and COX-2, the inducible form.
73	12576525	COX-2 was found to be expressed in undifferentiated 3T3-L1 cells and down-regulated during differentiation, whereas the cellular level of COX-1 remained relatively constant.
74	12576525	Tumor necrosis factor-alpha (TNFalpha) significantly up-regulated COX-2 expression ( approximately 2-fold) in differentiating 3T3-L1 cells, whereas similar effect was not observed with COX-1 expression.
75	12576525	Abrogating the induced COX-2 activity reversed the TNFalpha-induced inhibition of differentiation by approximately 70%, implying a role for COX-2 in mediating TNFalpha signaling.
76	12576525	Hence, both COX isoforms were involved in the negative modulation of adipocyte differentiation.
77	12576525	COX-2 appeared to be the main isoform mediating at least part of the negative effects of TNFalpha.
78	12576525	Role of cyclooxygenases COX-1 and COX-2 in modulating adipogenesis in 3T3-L1 cells.
79	12576525	Two COX isoforms have been identified, COX-1, the constitutive form, and COX-2, the inducible form.
80	12576525	COX-2 was found to be expressed in undifferentiated 3T3-L1 cells and down-regulated during differentiation, whereas the cellular level of COX-1 remained relatively constant.
81	12576525	Tumor necrosis factor-alpha (TNFalpha) significantly up-regulated COX-2 expression ( approximately 2-fold) in differentiating 3T3-L1 cells, whereas similar effect was not observed with COX-1 expression.
82	12576525	Abrogating the induced COX-2 activity reversed the TNFalpha-induced inhibition of differentiation by approximately 70%, implying a role for COX-2 in mediating TNFalpha signaling.
83	12576525	Hence, both COX isoforms were involved in the negative modulation of adipocyte differentiation.
84	12576525	COX-2 appeared to be the main isoform mediating at least part of the negative effects of TNFalpha.
85	12576525	Role of cyclooxygenases COX-1 and COX-2 in modulating adipogenesis in 3T3-L1 cells.
86	12576525	Two COX isoforms have been identified, COX-1, the constitutive form, and COX-2, the inducible form.
87	12576525	COX-2 was found to be expressed in undifferentiated 3T3-L1 cells and down-regulated during differentiation, whereas the cellular level of COX-1 remained relatively constant.
88	12576525	Tumor necrosis factor-alpha (TNFalpha) significantly up-regulated COX-2 expression ( approximately 2-fold) in differentiating 3T3-L1 cells, whereas similar effect was not observed with COX-1 expression.
89	12576525	Abrogating the induced COX-2 activity reversed the TNFalpha-induced inhibition of differentiation by approximately 70%, implying a role for COX-2 in mediating TNFalpha signaling.
90	12576525	Hence, both COX isoforms were involved in the negative modulation of adipocyte differentiation.
91	12576525	COX-2 appeared to be the main isoform mediating at least part of the negative effects of TNFalpha.
92	12576525	Role of cyclooxygenases COX-1 and COX-2 in modulating adipogenesis in 3T3-L1 cells.
93	12576525	Two COX isoforms have been identified, COX-1, the constitutive form, and COX-2, the inducible form.
94	12576525	COX-2 was found to be expressed in undifferentiated 3T3-L1 cells and down-regulated during differentiation, whereas the cellular level of COX-1 remained relatively constant.
95	12576525	Tumor necrosis factor-alpha (TNFalpha) significantly up-regulated COX-2 expression ( approximately 2-fold) in differentiating 3T3-L1 cells, whereas similar effect was not observed with COX-1 expression.
96	12576525	Abrogating the induced COX-2 activity reversed the TNFalpha-induced inhibition of differentiation by approximately 70%, implying a role for COX-2 in mediating TNFalpha signaling.
97	12576525	Hence, both COX isoforms were involved in the negative modulation of adipocyte differentiation.
98	12576525	COX-2 appeared to be the main isoform mediating at least part of the negative effects of TNFalpha.
99	12590952	In healthy volunteers (age, 42+/-11 years; BMI, 28.4+/-4.8 kg/m(2); n=28), the ingestion of G. biloba extract significantly increased fasting insulin and C-peptide (10+/-4 vs. 12+/-6 microU/ml, p<0.007 and 1.3+/-0.8 vs. 2.1+/-1.1 ng/ml, p<0.001, respectively) and significantly reduced collagen but not PAF-mediated platelet aggregation, converting 21 of 28 subjects with [COL+/EPI+] platelets to the [COL-/EPI+] phenotype.
100	12590952	G. biloba-induced reduction of both classes of prostanoid metabolites in healthy volunteers, but not in T2DM subjects, may suggest a nonselective inhibition of COX-1-mediated TXA(2) in platelets and COX-2-mediated PGI(2) production by the endothelial cells and perhaps platelet-enriched levels of arachidonic acid or COX-1 activity, or both, in T2DM subjects.
101	12837757	COX-2 protein and its product PGE2 were also increased, whereas COX-1 expression was unaffected.
102	12837757	S100b-induced COX-2 mRNA was blocked by an anti-RAGE antibody and by inhibitors of NF-kappa B (Bay11-7082), oxidant stress, protein kinase C, ERK, and p38 MAPKs.
103	12837757	Additionally, S100b-induced adherence of THP-1 monocytes to vascular smooth muscle cells was blocked by the COX-2 inhibitor NS-398, Bay11-7082, inhibitors of ERK and p38 MAPK, and protein kinase C thereby indicating functional relevance.
104	14514642	We first confirmed that incubation of HMC with 30 mmol/l glucose significantly increased COX-2 mRNA but not COX-1 mRNA, compared with 5.6 mmol/l glucose.
105	14514642	Similarly, incubation of HMCs with 30 mmol/l glucose significantly increased mitochondrial membrane potential, intracellular ROS production, COX-2 protein expression, and PGE2 synthesis, and these events were completely suppressed by thenoyltrifluoroacetone or carbonyl cyanide m-chlorophenylhydrazone, inhibitors of mitochondrial metabolism, or by overexpression of uncoupling protein-1 or manganese superoxide dismutase.
106	14514642	In addition, hyperglycemia induced activation of the COX-2 gene promoter, which was completely abrogated by mutation of two nuclear factor kappaB (NF-kappaB) binding sites in the promoter region.
107	14514642	Our results suggest that hyperglycemia increases mitochondrial ROS production, resulting in NF-kappaB activation, COX-2 mRNA induction, COX-2 protein production, and PGE2 synthesis.
108	14642793	Six major groups of rats with gastric ulcers were used: (1) vehicle (saline); (2) streptozotocin alone; (3) insulin (4 IU/day intraperitoneally); (4) streptozotocin plus insulin; (5) pentoxifylline, an inhibitor of synthesis and release of tumor necrosis factor-alpha (TNF alpha); and (6) aspirin, a non-selective inhibitor of cyclooxygenase-1 (COX-1) and cyclooxygenase-2 (COX-2), and rofecoxib, the highly selective COX-2.
109	14642793	The prolongation of the healing in diabetic animals was associated with an increase in gastric mucosal expression and release of TNFalpha, interleukin-1 beta (IL-1 beta), suppression of the vascular endothelial growth factor (VEGF), platelet endothelial cell adhesion molecule-1 (PECAM-1) and the mucosal overexpression of heat shock protein 70 (HSP 70).
110	14642793	Administration of insulin reversed the delay in ulcer healing and significantly decreased the expression of IL-1 beta and TNF-alpha, while producing the rise in the expression of VEGF and PECAM.
111	14642793	We conclude that: (1) Experimental diabetes dramatically impairs ulcer healing, depending upon the increased release of proinflammatory cytokines and the attenuation of angiogenesis that can limit the ulcer healing effects of locally produced HSP 70 and TNF-alpha. (2) Insulin reversed this impairment of ulcer healing in diabetic rats, mainly due to the enhancement of angiogenesis and reduction in expression of cytokines in the ulcer area. (3) Classic non-steroidal anti-inflammatory drugs such as aspirin prolonged ulcer healing under diabetic conditions due to suppression of endogenous prostaglandins and the fall in the microcirculation at the ulcer margin and these effects were mimicked by selective, so called "safe" COX-2 inhibitor, rofecoxib, suggesting that both COX isoforms are important sources of prostaglandins that are essential in the ulcer healing in diabetes.
112	14749287	In most tissues, COX-1 is a constitutive enzyme involved in prostaglandin-mediated physiological processes, whereas COX-2 is thought to be induced by inflammatory stimuli.
113	14749287	However, it has previously been reported that COX-2 is the dominant isoform in islets and an insulin-secreting beta-cell line under basal conditions.
114	14749287	We have investigated the relative abundance of COX-1 and COX-2 mRNAs in MIN6 cells, a mouse insulin-secreting cell line, and in primary mouse and human islets.
115	14749287	We found that COX-2 was the dominant isoform in MIN6 cells, but that COX-1 mRNA was more abundant than that of COX-2 in freshly isolated mouse islets.
116	14749287	In most tissues, COX-1 is a constitutive enzyme involved in prostaglandin-mediated physiological processes, whereas COX-2 is thought to be induced by inflammatory stimuli.
117	14749287	However, it has previously been reported that COX-2 is the dominant isoform in islets and an insulin-secreting beta-cell line under basal conditions.
118	14749287	We have investigated the relative abundance of COX-1 and COX-2 mRNAs in MIN6 cells, a mouse insulin-secreting cell line, and in primary mouse and human islets.
119	14749287	We found that COX-2 was the dominant isoform in MIN6 cells, but that COX-1 mRNA was more abundant than that of COX-2 in freshly isolated mouse islets.
120	14749287	In most tissues, COX-1 is a constitutive enzyme involved in prostaglandin-mediated physiological processes, whereas COX-2 is thought to be induced by inflammatory stimuli.
121	14749287	However, it has previously been reported that COX-2 is the dominant isoform in islets and an insulin-secreting beta-cell line under basal conditions.
122	14749287	We have investigated the relative abundance of COX-1 and COX-2 mRNAs in MIN6 cells, a mouse insulin-secreting cell line, and in primary mouse and human islets.
123	14749287	We found that COX-2 was the dominant isoform in MIN6 cells, but that COX-1 mRNA was more abundant than that of COX-2 in freshly isolated mouse islets.
124	14988266	The cyclooxygenase (COX)-2 enzyme has been implicated in the pathogenesis of several inflammatory diseases.
125	14988266	High glucose treatment of THP-1 monocytic cells led to a significant three- to fivefold induction of COX-2 mRNA and protein expression but not COX-1 mRNA.
126	14988266	High glucose-induced COX-2 mRNA was blocked by inhibitors of nuclear factor-kappaB (NF-kappaB), protein kinase C, and p38 mitogen-activated protein kinase.
127	14988266	In addition, an antioxidant and inhibitors of mitochondrial superoxide, NADPH oxidase, and glucose metabolism to glucosamine also blocked high glucose-induced COX-2 expression to varying degrees.
128	14988266	Promoter deletion analyses and inhibition of transcription by NF-kappaB superrepressor and cAMP-responsive element binding (CREB) mutants confirmed the involvement of NF-kappaB and CREB transcription factors in high glucose-induced COX-2 regulation.
129	15613743	Healing of chronic gastric ulcers in diabetic rats treated with native aspirin, nitric oxide (NO)-derivative of aspirin and cyclooxygenase (COX)-2 inhibitor.
130	15613743	Four weeks after STZ injection, gastric ulcers were induced using the acetic acid method and rats with gastric ulcers received the treatment with 1) aspirin (ASA, 30 mg/kg-d i.g.), 2) NO-ASA applied in equimolar dose of 50 mg/kg-d i.g., 3) rofecoxib (5 mg/kg-d i.g.), the selective cyclooxygenase-(COX)-2 inhibitor and 4) SNAP (5 mg/kg-d i.g.), a donor of NO, combined with ASA (30 mg/kg-d i.g.).
131	15613743	Ten days after the induction of the ulcers, the healing rate and the gastric blood flow (GBF) were measured by planimetry and hydrogen (H(2))-gas clearance method, respectively and the plasma cytokine such as IL-1beta, TNF-alpha and IL-10 were determined.
132	15613743	The prolongation of the healing in diabetic animals was associated with an increase in the plasma cytokine (IL-1beta, TNF-alpha and IL-10) levels.
133	15613743	ASA and rofecoxib, that significantly suppressed the mucosal prostaglandin (PG) E(2) generation in ulcer area, delayed significantly the rate of ulcer healing and decreased the GBF at ulcer margin, while elevating plasma IL-1beta, TNF-alpha and IL-10 concentrations in non-diabetic rats and these alterations were significantly augmented in diabetic animals.
134	15613743	In contrast to ASA, the treatment with NO-ASA failed to influence both, the ulcer healing and GBF at ulcer margin and significantly attenuated the plasma levels of IL-1beta, TNF-alpha and IL-10 as compared to those recorded in ASA- or rofecoxib-treated animals.
135	15613743	We conclude that: 1) ulcer healing is dramatically impaired in experimental diabetes and this effect involves the fall in the gastric microcirculation at the ulcer margin and increased release of proinflammatory cytokines; 2) classic NSAID such as ASA and selective COX-2 inhibitors such as rofecoxib, prolong ulcer healing under diabetic conditions probably due to suppression of endogenous PG and the fall in the GBF at the ulcer margin suggesting that both COX isoforms, namely, COX-1 and COX-2, are important sources of PG during ulcer healing in diabetes; and 3) NO-ASA counteracts the impairment of ulcer healing in diabetic rats induced by ASA, mainly due to the release of NO that compensates for PG deficiency resulting in enhancement in the GBF at ulcer margin and suppression of cytokine release in the ulcer area.
136	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
137	15644490	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.
138	15644490	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.
139	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
140	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
141	15644490	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.
142	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
143	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
144	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
145	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
146	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
147	15644490	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.
148	15644490	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.
149	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
150	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
151	15644490	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.
152	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
153	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
154	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
155	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
156	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
157	15644490	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.
158	15644490	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.
159	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
160	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
161	15644490	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.
162	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
163	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
164	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
165	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
166	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
167	15644490	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.
168	15644490	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.
169	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
170	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
171	15644490	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.
172	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
173	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
174	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
175	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
176	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
177	15644490	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.
178	15644490	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.
179	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
180	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
181	15644490	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.
182	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
183	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
184	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
185	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
186	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
187	15644490	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.
188	15644490	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.
189	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
190	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
191	15644490	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.
192	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
193	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
194	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
195	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
196	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
197	15644490	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.
198	15644490	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.
199	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
200	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
201	15644490	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.
202	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
203	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
204	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
205	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
206	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
207	15644490	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.
208	15644490	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.
209	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
210	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
211	15644490	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.
212	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
213	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
214	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
215	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
216	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
217	15644490	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.
218	15644490	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.
219	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
220	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
221	15644490	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.
222	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
223	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
224	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
225	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
226	15644490	Altered expression of COX-1, COX-2, and mPGES in rats with nephrogenic and central diabetes insipidus.
227	15644490	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.
228	15644490	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.
229	15644490	In lithium-induced NDI, expression of COX-1, COX-2, and mPGES was markedly decreased in IM.
230	15644490	In ISOM and cortex, COX-1 expression was marginally reduced and mPGES expression was unaltered.
231	15644490	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.
232	15644490	Treatment of DDAVP in BB rats for 6 days resulted in a markedly increased expression of COX-1, COX-2, and mPGES in IM.
233	15644490	In the cortex, there were no changes in the expression of COX-1 and mPGES, whereas COX-2 expression was decreased.
234	15644490	These results identify markedly reduced expression of COX-1, COX-2, and mPGES in IM in lithium-induced NDI.
235	15644490	Furthermore, there were major changes in the expression of COX-1, COX-2, and mPGES in rats with CDI.
236	15855344	Those wounds were characterized by a reduced expression of COX-1 and the presence of strongly elevated levels of COX-2 when compared with conditions observed in healthy animals.
237	15855344	Resolution of the diabetic and impaired wound-healing phenotype by systemic administration of leptin into ob/ob mice increased COX-1 expression in wound margin keratinocytes and decreased COX-2 expression in inner wound areas to levels found in wild-type animals.
238	15855344	Notably, improved wound healing was characterized by a marked increase in PGE2/PGD2 biosynthesis that colocalized with induced COX-1 in new tissue at the margin of the wound.
239	15855344	COX-2 expression did not significantly contribute to PGE2/PGD2 production in impaired wound tissue.
240	15855344	Accordingly, only late wound tissue from SC-560-treated (selective COX-1 inhibitor) but not celecoxib-treated (selective COX-2 inhibitor) ob/ob mice exhibited a severe loss in PGE2, PGD2, and prostacyclin at the wound site, and this change was associated with reduced keratinocyte numbers in the neo-epithelia.
241	15855344	Those wounds were characterized by a reduced expression of COX-1 and the presence of strongly elevated levels of COX-2 when compared with conditions observed in healthy animals.
242	15855344	Resolution of the diabetic and impaired wound-healing phenotype by systemic administration of leptin into ob/ob mice increased COX-1 expression in wound margin keratinocytes and decreased COX-2 expression in inner wound areas to levels found in wild-type animals.
243	15855344	Notably, improved wound healing was characterized by a marked increase in PGE2/PGD2 biosynthesis that colocalized with induced COX-1 in new tissue at the margin of the wound.
244	15855344	COX-2 expression did not significantly contribute to PGE2/PGD2 production in impaired wound tissue.
245	15855344	Accordingly, only late wound tissue from SC-560-treated (selective COX-1 inhibitor) but not celecoxib-treated (selective COX-2 inhibitor) ob/ob mice exhibited a severe loss in PGE2, PGD2, and prostacyclin at the wound site, and this change was associated with reduced keratinocyte numbers in the neo-epithelia.
246	15855344	Those wounds were characterized by a reduced expression of COX-1 and the presence of strongly elevated levels of COX-2 when compared with conditions observed in healthy animals.
247	15855344	Resolution of the diabetic and impaired wound-healing phenotype by systemic administration of leptin into ob/ob mice increased COX-1 expression in wound margin keratinocytes and decreased COX-2 expression in inner wound areas to levels found in wild-type animals.
248	15855344	Notably, improved wound healing was characterized by a marked increase in PGE2/PGD2 biosynthesis that colocalized with induced COX-1 in new tissue at the margin of the wound.
249	15855344	COX-2 expression did not significantly contribute to PGE2/PGD2 production in impaired wound tissue.
250	15855344	Accordingly, only late wound tissue from SC-560-treated (selective COX-1 inhibitor) but not celecoxib-treated (selective COX-2 inhibitor) ob/ob mice exhibited a severe loss in PGE2, PGD2, and prostacyclin at the wound site, and this change was associated with reduced keratinocyte numbers in the neo-epithelia.
251	15855344	Those wounds were characterized by a reduced expression of COX-1 and the presence of strongly elevated levels of COX-2 when compared with conditions observed in healthy animals.
252	15855344	Resolution of the diabetic and impaired wound-healing phenotype by systemic administration of leptin into ob/ob mice increased COX-1 expression in wound margin keratinocytes and decreased COX-2 expression in inner wound areas to levels found in wild-type animals.
253	15855344	Notably, improved wound healing was characterized by a marked increase in PGE2/PGD2 biosynthesis that colocalized with induced COX-1 in new tissue at the margin of the wound.
254	15855344	COX-2 expression did not significantly contribute to PGE2/PGD2 production in impaired wound tissue.
255	15855344	Accordingly, only late wound tissue from SC-560-treated (selective COX-1 inhibitor) but not celecoxib-treated (selective COX-2 inhibitor) ob/ob mice exhibited a severe loss in PGE2, PGD2, and prostacyclin at the wound site, and this change was associated with reduced keratinocyte numbers in the neo-epithelia.
256	15983217	Immunoblots showed a 73% reduction in PGI2 synthase (PGIS) expression in ZDF vessels compared with lean vessels, and there was no change in cyclooxygenase (COX) and BK channel expressions.
257	15983217	Real-time PCR studies showed that mRNA levels of PGIS, COX-1, and COX-2 were similar between lean and ZDF vessels.
258	16411374	The concentration of PGE2, the gene expression of cyclooxygenases (COX-1 and COX-2) and level of apoptosis (measured by caspase-3 activity) are assessed during organogenesis in the embryos of streptozotocin-induced diabetic rats.
259	16493486	Polymorphisms of COX-1 and GPVI associate with the antiplatelet effect of aspirin in coronary artery disease patients.
260	17050798	The inhibitory activity of cyclooxygenases was evaluated indirectly by the determination of prostaglandin E2 (COX-2) and thromboxane B2 (COX-1) using the sigmoidal inhibitory Emax model.
261	17112505	Intrathecally administered COX-2 but not COX-1 or COX-3 inhibitors attenuate streptozotocin-induced mechanical hyperalgesia in rats.
262	17112505	Intrathecal administrations of the COX-2 inhibitors SC-58125 (7-100 microg) and NS-398 (7-60 microg), as well as a high dose (100 microg) of the COX-1 inhibitor SC-560 attenuated hyperalgesia, whereas intrathecal administrations of a low dose (10 microg) of SC-560 and the COX-3 inhibitor acetaminophen (1-7 mg) did not.
263	17112505	Intrathecally administered COX-2 but not COX-1 or COX-3 inhibitors attenuate streptozotocin-induced mechanical hyperalgesia in rats.
264	17112505	Intrathecal administrations of the COX-2 inhibitors SC-58125 (7-100 microg) and NS-398 (7-60 microg), as well as a high dose (100 microg) of the COX-1 inhibitor SC-560 attenuated hyperalgesia, whereas intrathecal administrations of a low dose (10 microg) of SC-560 and the COX-3 inhibitor acetaminophen (1-7 mg) did not.
265	17130490	Activated monocytes express cyclooxygenase (COX)-2, promoting prostaglandin-E(2) (PGE(2)) secretion, whereas COX-1 expression is constitutive.
266	17130490	Isolated CD14(+) monocytes were analyzed for COX mRNA and protein expression from identical twins (discordant for type 1 diabetes) and control subjects.
267	17130490	After LPS, twins and control subjects showed a COX mRNA isoform switch with decreased COX-1 mRNA (P < 0.01), increased COX-2 mRNA (P < 0.01), and increased COX-2 protein expression (P < 0.01).
268	17130490	Compared with control subjects, both diabetic and nondiabetic twins showed greater LPS-induced downregulation of monocyte COX-1 mRNA (P = 0.02), reduced upregulation of COX-2 mRNA and protein (P < 0.03), and greater inhibition by the COX-2 inhibitor di-isopropylfluorophosphate (DFP) of monocyte PGE(2) (P < 0.007).
269	17130490	We demonstrate an alteration in monocyte COX mRNA expression as well as monocyte COX-2 and PGE(2) production after LPS in type 1 diabetic patients and their nondiabetic twins.
270	17130490	Activated monocytes express cyclooxygenase (COX)-2, promoting prostaglandin-E(2) (PGE(2)) secretion, whereas COX-1 expression is constitutive.
271	17130490	Isolated CD14(+) monocytes were analyzed for COX mRNA and protein expression from identical twins (discordant for type 1 diabetes) and control subjects.
272	17130490	After LPS, twins and control subjects showed a COX mRNA isoform switch with decreased COX-1 mRNA (P < 0.01), increased COX-2 mRNA (P < 0.01), and increased COX-2 protein expression (P < 0.01).
273	17130490	Compared with control subjects, both diabetic and nondiabetic twins showed greater LPS-induced downregulation of monocyte COX-1 mRNA (P = 0.02), reduced upregulation of COX-2 mRNA and protein (P < 0.03), and greater inhibition by the COX-2 inhibitor di-isopropylfluorophosphate (DFP) of monocyte PGE(2) (P < 0.007).
274	17130490	We demonstrate an alteration in monocyte COX mRNA expression as well as monocyte COX-2 and PGE(2) production after LPS in type 1 diabetic patients and their nondiabetic twins.
275	17130490	Activated monocytes express cyclooxygenase (COX)-2, promoting prostaglandin-E(2) (PGE(2)) secretion, whereas COX-1 expression is constitutive.
276	17130490	Isolated CD14(+) monocytes were analyzed for COX mRNA and protein expression from identical twins (discordant for type 1 diabetes) and control subjects.
277	17130490	After LPS, twins and control subjects showed a COX mRNA isoform switch with decreased COX-1 mRNA (P < 0.01), increased COX-2 mRNA (P < 0.01), and increased COX-2 protein expression (P < 0.01).
278	17130490	Compared with control subjects, both diabetic and nondiabetic twins showed greater LPS-induced downregulation of monocyte COX-1 mRNA (P = 0.02), reduced upregulation of COX-2 mRNA and protein (P < 0.03), and greater inhibition by the COX-2 inhibitor di-isopropylfluorophosphate (DFP) of monocyte PGE(2) (P < 0.007).
279	17130490	We demonstrate an alteration in monocyte COX mRNA expression as well as monocyte COX-2 and PGE(2) production after LPS in type 1 diabetic patients and their nondiabetic twins.
280	17191216	Since the discovery of a second isoform of COXs, it has been shown that PGF2alpha can be formed in vivo from arachidonic acid through both isoforms of COXs, namely cyclooxygenase-1 (COX-1) and cyclooxygenase-2 (COX-2).
281	17192482	The roles played by arachidonic acid and its cyclooxygenase (COX)-generated and lipoxygenase (LOX)-generated metabolites have been studied using rodent islets and insulin-secreting cell lines, but very little is known about COX and LOX isoform expression and the effects of modulation of arachidonic acid generation and metabolism in human islets.
282	17192482	We have used RT-PCR to identify mRNAs for cytosolic phospholipase A(2) (cPLA(2)), COX-1, COX-2, 5-LOX, and 12-LOX in isolated human islets.
283	17192482	Perifusion experiments with human islets indicated that PLA(2) inhibition inhibited glucose-stimulated insulin secretion, whereas inhibitors of COX-2 and 12-LOX enzymes enhanced basal insulin secretion and also secretory responses induced by 20 mmol/l glucose or by 50 mumol/l arachidonic acid.
284	17192482	Inhibition of COX-1 with 100 mumol/l acetaminophen did not significantly affect glucose-stimulated insulin secretion.
285	17192482	These data indicate that the stimulation of insulin secretion from human islets in response to arachidonic acid does not require its metabolism through COX-2 and 5-/12-LOX pathways.
286	17192482	The products of COX-2 and LOX activities have been implicated in cytokine-mediated damage of beta-cells, so selective inhibitors of these enzymes would be expected to have a dual protective role in diabetes: they would minimize beta-cell dysfunction while maintaining insulin secretion through enhancing endogenous arachidonic acid levels.
287	17192482	The roles played by arachidonic acid and its cyclooxygenase (COX)-generated and lipoxygenase (LOX)-generated metabolites have been studied using rodent islets and insulin-secreting cell lines, but very little is known about COX and LOX isoform expression and the effects of modulation of arachidonic acid generation and metabolism in human islets.
288	17192482	We have used RT-PCR to identify mRNAs for cytosolic phospholipase A(2) (cPLA(2)), COX-1, COX-2, 5-LOX, and 12-LOX in isolated human islets.
289	17192482	Perifusion experiments with human islets indicated that PLA(2) inhibition inhibited glucose-stimulated insulin secretion, whereas inhibitors of COX-2 and 12-LOX enzymes enhanced basal insulin secretion and also secretory responses induced by 20 mmol/l glucose or by 50 mumol/l arachidonic acid.
290	17192482	Inhibition of COX-1 with 100 mumol/l acetaminophen did not significantly affect glucose-stimulated insulin secretion.
291	17192482	These data indicate that the stimulation of insulin secretion from human islets in response to arachidonic acid does not require its metabolism through COX-2 and 5-/12-LOX pathways.
292	17192482	The products of COX-2 and LOX activities have been implicated in cytokine-mediated damage of beta-cells, so selective inhibitors of these enzymes would be expected to have a dual protective role in diabetes: they would minimize beta-cell dysfunction while maintaining insulin secretion through enhancing endogenous arachidonic acid levels.
293	17513496	Nitric oxide- and/or endothelium-derived hypolarizing factor-mediated relaxation and the protein expressions of phospho-endothelial nitric oxide synthase (Ser1177) and extracellular superoxide dismutase were also reduced in OLETF.
294	17513496	The ACh-induced productions of thromboxane A(2) and PGE(2) were greater in OLETF than LETO rats, as were the mesenteric artery COX-1 and COX-2 protein expressions.
295	17989504	We examined a possible involvement of cyclooxygenase (COX) and nitric oxide synthase (NOS) products in hyperalgesia occurring during streptozotocin (STZ)-induced diabetes.
296	17989504	Indomethacin and celecoxib were used as relatively selective inhibitors of COX-1 and COX-2, respectively.
297	17989504	NOS inhibitors included: non-specific inhibitor N(G)-nitro-L-arginine and L-N(6)-(1-iminoethyl)lysine preferentially acting on inducible NOS (iNOS) as well as 7-nitroindazole relatively specific inhibitor neuronal NOS (nNOS).
298	17989504	The results of the study suggest participation of COX-1, COX-2 and iNOS, but not nNOS, in transmission of pain stimuli in STZ-induced diabetic hyperalgesia.
299	17989504	We examined a possible involvement of cyclooxygenase (COX) and nitric oxide synthase (NOS) products in hyperalgesia occurring during streptozotocin (STZ)-induced diabetes.
300	17989504	Indomethacin and celecoxib were used as relatively selective inhibitors of COX-1 and COX-2, respectively.
301	17989504	NOS inhibitors included: non-specific inhibitor N(G)-nitro-L-arginine and L-N(6)-(1-iminoethyl)lysine preferentially acting on inducible NOS (iNOS) as well as 7-nitroindazole relatively specific inhibitor neuronal NOS (nNOS).
302	17989504	The results of the study suggest participation of COX-1, COX-2 and iNOS, but not nNOS, in transmission of pain stimuli in STZ-induced diabetic hyperalgesia.
303	18406713	Most of the nonsteroidal antiinflammatory drugs are more effective in inhibiting activity of COX-1 compared with COX-2.
304	18641273	Both metformin and 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside [AICAR, an AMP-activated protein kinase (AMPK) activator that is also activated by metformin] 1) diminished the tendency for the relaxation to reverse at high ACh concentrations and 2) suppressed both ACh-induced EDCF-mediated contraction and ACh-stimulated production of prostanoids (thromboxane A2 and PGE2).
305	18641273	Metformin did not alter the protein expressions of endothelial nitric oxide synthase (eNOS), phospho-eNOS (Ser1177), or COX-1, but it increased COX-2 protein.
306	18810243	The effect of CB-1 and CB-2 receptor agonists, as well as an influence of a non-selective inhibitor of nitric oxide synthase (NOS), L-NOArg, and an inhibitor acting preferentially on cyclooxygenase-1 (COX-1), indomethacin, on the action of cannabinoid receptor agonists in a streptozotocin (STZ)-induced neuropathic model was investigated.
307	18810243	When administered alone, a non-selective cannabinoid receptor agonist, WIN 55,212-2, a potentially selective CB-1 cannabinoid receptor agonist, Met-F-AEA, and a selective CB-2 cannabinoid receptor agonist, AM1241, dose-dependently reduced STZ-induced hyperalgesia.
308	18810243	The results of the present study also demonstrated that inhibitors of COX and NOS increase antihyperalgesic activity of low doses of CB-1 and CB-2 receptor agonists.
309	19164460	In OLETF rats [compared with age-matched control Long-Evans Tokushima Otsuka (LETO) rats]: 1) acetylcholine (ACh)-induced (endothelium-dependent) relaxation was impaired, 2) NO- and EDHF-mediated relaxations and nitrite production were reduced, and 3) ACh-induced EDCF-mediated contraction, production of prostanoids, and the protein expressions of COX-1 and COX-2 were all increased.
310	19164460	When OLETF rats received chronic EPA treatment long-term (300 mg/kg/day p.o. for 4 weeks), their isolated mesenteric arteries exhibited: 1) improvements in ACh-induced NO- and EDHF-mediated relaxations and COX-mediated contraction, 2) reduced EDCF- and arachidonic acid-induced contractions, 3) normalized NO metabolism, 4) suppressed production of prostanoids, 5) reduced COX-2 expression, and 6) reduced phosphoextracellular signal-regulated kinase (ERK) expression.
311	19164460	We propose that EPA ameliorates endothelial dysfunction in OLETF rats by correcting the imbalance between endothelium-derived factors, at least partly, by inhibiting ERK, decreasing NF-kappaB activation, and reducing COX-2 expression.
312	19553934	As scientific understanding progressed, it became evident that two isoforms of COX exist: COX-1 and COX-2.
313	19553934	COX-1 was initially considered to be the "good," constitutive isoform, whereas COX-2 appeared to be mainly a "bad" inducible enzyme involved in inflammatory responses.
314	19553934	As scientific understanding progressed, it became evident that two isoforms of COX exist: COX-1 and COX-2.
315	19553934	COX-1 was initially considered to be the "good," constitutive isoform, whereas COX-2 appeared to be mainly a "bad" inducible enzyme involved in inflammatory responses.
316	19693696	Cyclooxygenase (COX), which have the isoforms of COX-1 and COX-2, is the key enzyme of prostaglandins biosynthesis.
317	19693696	We investigated the changes of COX-1 and COX-2 mRNA expression and protein level in diabetic rat kidney after RSV treatment.
318	19693696	Therefore, different therapy strategies such as combination with other antidiabetic drugs may tried in STZ induced animal model for reducing diabetic symptoms and altering COX-1 and COX-2 mRNA or protein levels.
319	19693696	Cyclooxygenase (COX), which have the isoforms of COX-1 and COX-2, is the key enzyme of prostaglandins biosynthesis.
320	19693696	We investigated the changes of COX-1 and COX-2 mRNA expression and protein level in diabetic rat kidney after RSV treatment.
321	19693696	Therefore, different therapy strategies such as combination with other antidiabetic drugs may tried in STZ induced animal model for reducing diabetic symptoms and altering COX-1 and COX-2 mRNA or protein levels.
322	19693696	Cyclooxygenase (COX), which have the isoforms of COX-1 and COX-2, is the key enzyme of prostaglandins biosynthesis.
323	19693696	We investigated the changes of COX-1 and COX-2 mRNA expression and protein level in diabetic rat kidney after RSV treatment.
324	19693696	Therefore, different therapy strategies such as combination with other antidiabetic drugs may tried in STZ induced animal model for reducing diabetic symptoms and altering COX-1 and COX-2 mRNA or protein levels.
325	19755160	In arteries from diabetic rabbits, eNOS, iNOS and COX-1 expression and testosterone-induced release of thromboxane A(2) and prostacyclin were not significantly different from those observed in control rabbits.
326	19832117	NSAIDs depress prostaglandins synthesis through inhibition of COX-1 that is involved in maintaining cell integrity and COX-2 that, although presents particularly in the kidneys, is overexpressed in response to inflammation.
327	19832117	Introduction of COX-2-selective inhibitors has improved the safety profile of the drugs with regard to their most common side effect which occurs at the gastrointestinal level but has not rendered them less cardio-nephrotoxic.
328	20082610	Altered arachidonic acid metabolism via COX-1 and COX-2 contributes to the endothelial dysfunction of penile arteries from obese Zucker rats.
329	20506110	PA-induced activation of CB(1)R is prevented by the treatment of AACOCF(3) (a cPLA(2) inhibitor), indomethacin and NS398 (a COX 2 inhibitors).
330	20506110	Indeed, PA increased cPLA(2), and COX-2 but not COX-1.
331	20506110	Furthermore, PA decreased GRP78 expression and induced increases in the endoplasmic reticulum (ER) stress signaling pathways p-PERK, p-eIF2α, p-ATF4, and CHOP, which were blocked by AM251 treatment.
332	20506110	Moreover, PA increased the Bax/Bcl-2 ratio, cleaved PARP, and caspase-3 levels.
333	20531983	We exposed cultured podocytes to FFSS, and studied changes in actin cytoskeleton, prostaglandin E(2) (PGE(2)) production and expression of cyclooxygenase-1 and-2 (COX-1, COX-2).
334	20886180	Plaque macrophages synthesise PGH2/PGG2 via COX-2; these potent prostanoids can trigger platelet activation and aggregation despite COX-1 inhibition by aspirin.
335	21856926	In arteries from GK rats (vs. those from Wistar rats), 1) ATP- and UTP-induced contractions, which were blocked by the nonselective P2 antagonist suramin, were enhanced, and these enhancements were suppressed by endothelial denudation, by cyclooxygenase (COX) inhibitors, or by a cytosolic phospholipase A(2) (cPLA(2)) inhibitor; 2) both nucleotides induced increased release of PGE(2) and PGF(2α); 3) nucleotide-stimulated cPLA(2) phosphorylations were increased; 4) COX-1 and COX-2 expressions were increased; and 5) neither P2Y2 nor P2Y6 receptor expression differed, but P2Y4 receptor expression was decreased.
336	21856926	Mesenteric arteries from GK rats treated with losartan exhibited (vs. untreated GK) 1) reduced nucleotide-induced contractions, 2) suppressed UTP-induced release of PGE(2) and PGF(2α), 3) suppressed UTP-stimulated cPLA(2) phosphorylation, 4) normalized expressions of COX-2 and P2Y4 receptors, and 5) reduced superoxide generation.
337	21856926	Our data suggest that the diabetes-related enhancement of ATP-mediated vasoconstriction was due to P2Y receptor-mediated activation of the cPLA(2)/COX pathway and, moreover, that losartan normalizes such contractions by a suppressing action within this pathway.
338	22179968	The effects of resveratrol on cyclooxygenase-1 and -2, nuclear factor kappa beta, matrix metalloproteinase-9, and sirtuin 1 mRNA expression in hearts of streptozotocin-induced diabetic rats.
339	22179968	We investigated cyclooxygenase-1 (COX-1), COX-2, nuclear factor κB (NF-κB), matrix metalloproteinase-9 (MMP-9), and sirtuin 1 (SIRT1) mRNA expression levels in heart tissue after RSV treatment in streptozotocin (STZ)-induced diabetic rats.
340	22179968	At the end of the experiment, all rats were sacrificed and heart tissues were stored at -80°C; mRNA expression levels of COX-1, COX-2, NF-κB, MMP-9, and SIRT1 genes were analyzed with quantitative real-time PCR.
341	22179968	We did not find any significant effect of RSV on MMP-9, COX-1, COX-2, or NF-κB mRNA levels among the groups.
342	22179968	The effects of resveratrol on cyclooxygenase-1 and -2, nuclear factor kappa beta, matrix metalloproteinase-9, and sirtuin 1 mRNA expression in hearts of streptozotocin-induced diabetic rats.
343	22179968	We investigated cyclooxygenase-1 (COX-1), COX-2, nuclear factor κB (NF-κB), matrix metalloproteinase-9 (MMP-9), and sirtuin 1 (SIRT1) mRNA expression levels in heart tissue after RSV treatment in streptozotocin (STZ)-induced diabetic rats.
344	22179968	At the end of the experiment, all rats were sacrificed and heart tissues were stored at -80°C; mRNA expression levels of COX-1, COX-2, NF-κB, MMP-9, and SIRT1 genes were analyzed with quantitative real-time PCR.
345	22179968	We did not find any significant effect of RSV on MMP-9, COX-1, COX-2, or NF-κB mRNA levels among the groups.
346	22179968	The effects of resveratrol on cyclooxygenase-1 and -2, nuclear factor kappa beta, matrix metalloproteinase-9, and sirtuin 1 mRNA expression in hearts of streptozotocin-induced diabetic rats.
347	22179968	We investigated cyclooxygenase-1 (COX-1), COX-2, nuclear factor κB (NF-κB), matrix metalloproteinase-9 (MMP-9), and sirtuin 1 (SIRT1) mRNA expression levels in heart tissue after RSV treatment in streptozotocin (STZ)-induced diabetic rats.
348	22179968	At the end of the experiment, all rats were sacrificed and heart tissues were stored at -80°C; mRNA expression levels of COX-1, COX-2, NF-κB, MMP-9, and SIRT1 genes were analyzed with quantitative real-time PCR.
349	22179968	We did not find any significant effect of RSV on MMP-9, COX-1, COX-2, or NF-κB mRNA levels among the groups.
350	22491820	Drugs indirectly modulating these signals, including COX-1/COX-2 inhibitors, have proven to play major roles in the atherothrombotic process.
351	22948792	The inhibitory effect of infusion of α-methyl 5-HT (5 µg/kg/min) was abolished in the presence of indomethacin (2 mg/kg), a non-selective cyclooxygenase (COX) inhibitor, or FR 122047 (1.5 mg/kg) or nimesulide (1.5 mg/kg), two selective COX-1 and COX-2 inhibitors, respectively, in long-term-diabetic pithed rats.
352	22948792	Our results indicate that 5-HT inhibition of the pressor responses induced by electrical stimulation is mediated both by the NO and COX pathways in long-term-diabetic rats.
353	23660496	Changes of calcium binding proteins, c-Fos and COX in hippocampal formation and cerebellum of Niemann-Pick, type C mouse.
354	23660496	Thus, we used immunohistochemistry to assess the expression levels of calcium binding proteins (calbindin D28K, parvalbumin, and calretinin), c-Fos and cyclooxygenase-1,2 (COX-1,2) in the hippocampal formation and cerebellum of 4 and 8 week old NPC+/+, NPC+/-, and NPC-/- mice.
355	23660496	Parvalbumin, COX-1,2 or c-Fos-immunoreactive neurons were widely detected in the CA1, CA3, and DG of the hippocampus, but the immunoreactivities were decreased sharply in all areas of hippocampus of NPC-/- compared to NPC+/+ and NPC+/- mice.
356	23660496	Changes of calcium binding proteins, c-Fos and COX in hippocampal formation and cerebellum of Niemann-Pick, type C mouse.
357	23660496	Thus, we used immunohistochemistry to assess the expression levels of calcium binding proteins (calbindin D28K, parvalbumin, and calretinin), c-Fos and cyclooxygenase-1,2 (COX-1,2) in the hippocampal formation and cerebellum of 4 and 8 week old NPC+/+, NPC+/-, and NPC-/- mice.
358	23660496	Parvalbumin, COX-1,2 or c-Fos-immunoreactive neurons were widely detected in the CA1, CA3, and DG of the hippocampus, but the immunoreactivities were decreased sharply in all areas of hippocampus of NPC-/- compared to NPC+/+ and NPC+/- mice.
359	23755196	The LOE treatment improved endothelium-dependent relaxations, abolished endothelium-dependent contractions to acetylcholine in the aorta, and normalized the increased vascular oxidative stress and expression of NADPH oxidase, cyclooxygenases, angiotensin II, angiotensin type 1 receptors and peroxynitrite and the decreased expression of endothelial NO synthase in db/db mice.
360	23755196	LOE also inhibited the activity of purified ACE, COX-1 and COX-2 in a dose-dependent manner.