ABSTRACT
Two complexes of Zn(II) and Ni(II) ions with the urea derivative, 2-benzimidazolyl-urea (BZIMU), of formulae [ZnBZIMU)2(H2O)](NO3)2 (1) and [Ni(BZIMU)2(CH3CH2OH)2](NO3)2 (2) were synthesized and characterized by their melting point, elemental analysis, spectroscopic techniques (FTIR, UV-Vis and 1H-NMR), High-resolution mass spectroscopy (HRMS), molar conductivity and thermogravimetric analysis. The crystal structures of 1-2 were determined by X-ray diffraction analysis. The antiproliferative activity of 1-2 was tested in vitro against human adenocarcinoma cell lines: cervix (HeLa) and breast (MCF-7). Their toxicity was surveyed against normal human fetal lung fibroblast cells (MRC-5). The bioactivity mechanism of 1-2 and their related analogues of copper and silver metallodrugs are rationalized by the means of computations. The antimicrobial activity of 1-2 against Escherichia coli (E. coli) is also evaluated. The complexes [ZnBZIMU)2(H2O)](NO3)2 (1) and [Ni(BZIMU)2(CH3CH2OH)2](NO3)2 (2) (BZIMU= 2-Benzimidazolyl-urea), were tested in vitro against HeLa and MCF-7 cells. Their toxicity was surveyed against normal MRC-5 cells. The association of the microbiota with the antiproliferative activity of 1-2 was investigated against Escherichia coli.
Subject(s)
Anti-Infective Agents/chemistry , Anti-Infective Agents/pharmacology , Antineoplastic Agents/chemistry , Antineoplastic Agents/pharmacology , Nickel/chemistry , Urea/analogs & derivatives , Urea/chemistry , Zinc/chemistry , Coordination Complexes/chemistry , Crystallography, X-Ray , Dose-Response Relationship, Drug , Humans , Hydrogen Bonding , Lipid Bilayers , Models, Molecular , Molecular Conformation , Molecular Structure , Spectrum AnalysisABSTRACT
A novel proton transfer compound (SMHABT)+(HDPC)- (1) obtained from 2-amino-6-sulfamoylbenzothiazole (SMABT) and 2,6-pyridinedicarboxylic acid (H2DPC) and its Fe(III), Co(II), Ni(II) complexes (2-4), and Fe(II) complex of SMABT (5) have been prepared and characterized by spectroscopic techniques. Additionally, single crystal X-ray diffraction techniques were applied to complexes (2-4). All complexes (2-4) have distorted octahedral conformations and the structure of 5 might be proposed as octahedral according to spectral and analytical results. All compounds, including acetazolamide (AAZ) as the control compound, were also evaluated for their in vitro inhibition effects on human hCA I and hCA II for their hydratase and esterase activities. The synthesized compounds have remarkable inhibitory activities on hCA I and hCA II. Especially, the inhibition potentials of the salt and the metal complexes (1-5) are comparable with AAZ. Inhibition data have been analyzed by using a one-way analysis of variance for multiple comparisons (p < .0001).
Subject(s)
Benzothiazoles/chemistry , Benzothiazoles/pharmacology , Carbonic Anhydrase Inhibitors/pharmacology , Carbonic Anhydrases/drug effects , Cytosol/enzymology , Metals/chemistry , Carbon-13 Magnetic Resonance Spectroscopy , Crystallography, X-Ray , Humans , Protein Conformation , Proton Magnetic Resonance Spectroscopy , Protons , Spectrophotometry, Ultraviolet , Spectroscopy, Fourier Transform InfraredABSTRACT
A novel proton transfer compound (HClABT)(+)(HDPC.H2DPC)(-) (1) and its Fe(III), Co(II), Ni(II) and two different Cu(II) complexes (2-6) have been prepared and characterized by spectroscopic techniques. Additionally, single crystal X-ray diffraction techniques were applied to all complexes. All compounds, including acetazolamide (AAZ) as the control compound, were also evaluated for their in vitro inhibition effects on human hCA I and hCA II for their hydratase and esterase activities. Although there is no inhibition for hydratase activities, all compounds have inhibited the esterase activities of hCA I and II. The comparison of the inhibition studies of 1-6 to parent compounds, ClABT and H2DPC, indicates that 1-6 have superior inhibitory effects. The inhibition effects of 2-6 are also compared to the inhibitory properties of the simple metal complexes of ClABT and H2DPC, revealing an improved transfection profile. Data have been analysed by using a one-way analysis of variance for multiple comparisons.
Subject(s)
Carbonic Anhydrase II/antagonists & inhibitors , Carbonic Anhydrase I/antagonists & inhibitors , Carbonic Anhydrase Inhibitors/chemical synthesis , Coordination Complexes/chemical synthesis , Protons , Pyridines/chemistry , Carbonic Anhydrase I/isolation & purification , Carbonic Anhydrase II/isolation & purification , Carbonic Anhydrase Inhibitors/chemistry , Carbonic Anhydrase Inhibitors/pharmacology , Coordination Complexes/chemistry , Coordination Complexes/pharmacology , Erythrocytes/enzymology , Humans , Isoenzymes , Molecular Structure , Picolinic Acids , Spectroscopy, Fourier Transform InfraredABSTRACT
A novel proton transfer compound (HABT)(+)(Hdipic)(-) (1) obtained from ABT and H2dipic and its metal complexes (2-5) have been prepared and characterized by spectroscopic techniques. Single crystal X-ray diffraction method has also been applied to 2 and 5. While complex 2 has a distorted octahedral conformation, 5 exhibits a distorted square pyramidal structure. The structures of 3 and 4 might be proposed as octahedral according to experimental data. All compounds were also evaluated for their in vitro inhibition effects on hCA I and II for their hydratase and esterase activities. Although there is no inhibition for hydratase activities, all compounds have inhibited the esterase activities of hCA I and II. The comparison of the inhibition studies of 1-5 to parent compounds indicates that 1-5 have superior inhibitory effects. The inhibition effects of 2-5 are also compared to inhibitory properties of the metal complexes of ABT and H2dipic, revealing an improved transfection profile.
Subject(s)
Benzothiazoles/chemistry , Carbonic Anhydrase II/chemistry , Carbonic Anhydrase I/chemistry , Carbonic Anhydrase Inhibitors/chemistry , Coordination Complexes/chemistry , Protons , Pyridines/chemistry , Carbonic Anhydrase I/isolation & purification , Carbonic Anhydrase II/isolation & purification , Carbonic Anhydrase Inhibitors/chemical synthesis , Coordination Complexes/chemical synthesis , Crystallography, X-Ray , Enzyme Assays , Erythrocytes/chemistry , Erythrocytes/enzymology , Humans , Hydrogen Bonding , Metals, Heavy/chemistry , Picolinic Acids , Salts/chemical synthesis , Salts/chemistry , Structure-Activity RelationshipABSTRACT
A novel proton transfer compound (HMeOABT)(+) (HDPC)(-) (1) and its Fe(III), Co(II), Ni(II) and Cu(II) complexes (2-5) have been prepared and characterized by spectroscopic techniques. Complex 4 has distorted octahedral conformation revealed by single crystal X-ray diffraction method. Structures of the other complexes might be proposed as octahedral according to experimental data. All compounds were also evaluated for their in vitro inhibition effects on hCA I and II for their hydratase and esterase activities. Although there is no inhibition for hydratase activities, all compounds have inhibited the esterase activities of hCA I and II. Data have been analyzed by using a one-way analysis of variance. The comparison of the inhibition studies of 1-5 to parent compounds indicates that 1-5 have superior inhibitory effects. The inhibition effects of 2-5 are also compared to inhibitory properties of the metal complexes of MeOABT and H2DPC, revealing an improved transfection profile.
Subject(s)
Carbonic Anhydrase II/antagonists & inhibitors , Carbonic Anhydrase I/antagonists & inhibitors , Carbonic Anhydrase Inhibitors/pharmacology , Models, Statistical , Organometallic Compounds/pharmacology , Benzothiazoles/chemistry , Carbonic Anhydrase I/isolation & purification , Carbonic Anhydrase I/metabolism , Carbonic Anhydrase II/isolation & purification , Carbonic Anhydrase II/metabolism , Carbonic Anhydrase Inhibitors/chemical synthesis , Carbonic Anhydrase Inhibitors/chemistry , Dose-Response Relationship, Drug , Humans , Isoenzymes/antagonists & inhibitors , Isoenzymes/metabolism , Metals, Heavy/chemistry , Models, Molecular , Molecular Structure , Organometallic Compounds/chemical synthesis , Organometallic Compounds/chemistry , Picolinic Acids/chemistry , Protons , Salts/chemistry , Structure-Activity RelationshipABSTRACT
The title hydrated mol-ecular organic salt, C10H10N2 (2+)·C10H6O6S2 (2-)·2H2O, crystallized with half a bipyridinium cation, half a naphthalene-2,6-di-sulfonate anion and a water mol-ecule in the asymmetric unit. The whole cation and anion are generated by inversion symmetry, the inversion centers being at the center of the bridging C-C bond of the cation, and at the center of the fused C-C bond of the naphthalene group of the anion. In the crystal, the anions and cations stack alternately along the a axis with π-π inter-actions [inter-centroid distance = 3.491â (1)â Å]. The anions are linked via O-Hâ¯O(sulfonate) hydrogen bonds involving two inversion-related water mol-ecules, forming chains along [10-1]. These chains are bridged by bifurcated N-Hâ¯(O,O) hydrogen bonds, forming a three-dimensional framework structure. There are also C-Hâ¯O hydrogen bonds present, reinforcing the framework structure.
ABSTRACT
BACKGROUND: Local anesthetic infiltration along the incision may be used to provide surgical anesthesia or postoperative analgesia. However, the effect of local anesthetics on wound healing remains controversial. In this investigation, we evaluated the effects of levobupivacaine on wound healing. METHODS: Sixty Wistar albino female rats weighing 230±20 g were included, with 10 rats in each group: group early c (early control): 3 mL isotonic saline; group early l1.25 (early levobupivacaine 1.25): 1.25 mg/kg per 3 mL levobupivacaine; group early l2.5 (early levobupivacaine 2.5): 2.5 mg/kg per 3 mL levobupivacaine; group late c (late control): 3 mL isotonic saline; group late l1.25 (late levobupivacaine 1.25): 1.25 mg/kg per 3 mL levobupivacaine; and group late l2.5 (late levobupivacaine 2.5): 2.5 mg/kg per 3 mL levobupivacaine. Rats in groups early c to early l2.5 were euthanized on the 8th day. Rats in groups late c to late l2.5 were euthanized on the 21st day. Wound tension strength, tissue hydroxyproline, and fibrotic index levels of the tissue samples from the early c and early l2.5 and late c and late l2.5 groups, respectively, on the 8th and 21st days were examined. RESULTS: Levobupivacaine decreased wound tension strength on the 8th day, especially a 2.5 mg/kg dose (P<0.001), and increased it on the 21st day (P<0.001). It also increased the inflammatory response (P<0.001) and collagen synthesis (8th day, P=0.109; 21st day, P=0.103) on both the 8th and 21st days. CONCLUSIONS: While levobupivacaine had a positive effect on wound healing during the early period, negative effects were observed thereafter. Additional studies at the molecular level are necessary to determine the cause of these apparently opposite effects.
Subject(s)
Anesthetics, Local/therapeutic use , Wound Healing/drug effects , Wounds and Injuries/pathology , Anesthetics, Local/adverse effects , Animals , Biopsy , Bupivacaine/adverse effects , Bupivacaine/analogs & derivatives , Bupivacaine/therapeutic use , Cell Proliferation , Female , Fibrosis , Hydroxyproline/analysis , Hydroxyproline/metabolism , Levobupivacaine , Postoperative Period , Rats , Rats, Wistar , Skin/chemistry , Sutures , Tensile Strength , Wounds and Injuries/metabolismABSTRACT
Dicamba, paraquat, picloram, clopyralid and linuron are herbicides widely used in agriculture. The aim of the present study is to evaluate the toxicity effects of the herbicides used on survival, fertility and length of Caenorhabditis elegans. Kaplan-Meier Survival Analysis method was used to identify the toxicity effect of herbicides on survival, and ANOVA and Post Hoc tests were used to determine the toxicity effects on fertility and length. In the study, C. elegans was exposed to 5 different concentrations (62.5, 125, 250, 500, 1000 µM) of each herbicide. When the results were evaluated, it was observed that survival (life span) and length (physical growth) were more affected, respectively, by paraquat, dicamba, linuron, picloram and clopyralid herbicides, fertility (egg productivity) were more affected, respectively, by paraquat, linuron, dicamba, picloram and clopyralid herbicides. As a result, it was determined that increasing the dose amounts of herbicides caused many toxic reactions on C. elegans, affecting survival, egg productivity and length.
Subject(s)
Herbicides , Animals , Herbicides/toxicity , Herbicides/analysis , Caenorhabditis elegans , Picloram/pharmacology , Paraquat/toxicity , Dicamba/pharmacology , Linuron/pharmacologyABSTRACT
Two novel proton transfer compounds were prepared between 2,4-dichloro-5-sulphamoylbenzoic acid (lasamide) (Hsba) and ethylenediamine (en), namely ethane-1,2-diaminium 2,4-dichloro-5-sulphamoylbenzoate (1), and also between Hsba and 2-amino-3-methylpyridine (2-amino-3-picoline) (amp), namely 2-amino-3-methylpyridinium 2,4-dichloro-5-sulphamoylbenzoate (2). All these were characterised by elemental, spectral (IR and UV-vis), thermal analyses, and single crystal X-ray diffraction studies. Compounds 1 and 2 crystallised in the P-1 and P21/c space groups, respectively. Intermolecular non-covalent interactions, such as ion pairing, hydrogen bonding, and π-π stacking were observed for these ionic compounds. The free ligands Hsba, en and amp, the products 1 and 2, and acetazolamide (AAZ) as the control compound, were also evaluated for their in vitro inhibitor effects on the human carbonic anhydrase isoenzymes (hCA I and hCA II) purified from erythrocyte cells by affinity chromatography for their hydratase and esterase activities. The half maximal inhibitory concentration (IC(50)) values for products 1 and 2 with respect to hydratase activity are 0.15 and 0.32 µM for hCA I and 0.06 and 0.15 µM for hCA II, respectively. The IC(50) values of the same inhibitors for esterase activity are 0.13 and 0.8 µM for hCA I and 0.14 and 0.1 µM for hCA II, respectively. In relation to esterase activities, the inhibition equilibrium constants (Ki) were also determined and found to be 0.137 and 0.99 µM on hCA I and 0.157 and 0.075 µM on hCA II for 1 and 2, respectively. The comparison of the inhibition studies of the newly synthesised compounds 1 and 2 to the parent compounds Hsba and amp and also to AAZ indicated that 1 and 2 have an effective inhibitory activity on hCA I and II, and might be used as potential inhibitors.
Subject(s)
Carbonic Anhydrase II/antagonists & inhibitors , Carbonic Anhydrase I/antagonists & inhibitors , Carbonic Anhydrase Inhibitors/chemical synthesis , Carbonic Anhydrase Inhibitors/metabolism , Isoenzymes/antagonists & inhibitors , Acetazolamide/metabolism , Acetazolamide/pharmacology , Aminopyridines/chemistry , Animals , Benzoates/chemistry , Carbonic Anhydrase I/isolation & purification , Carbonic Anhydrase I/metabolism , Carbonic Anhydrase II/isolation & purification , Carbonic Anhydrase II/metabolism , Carbonic Anhydrase Inhibitors/pharmacology , Crystallography, X-Ray , Enzyme Assays , Erythrocytes/enzymology , Ethylenediamines/chemistry , Glaucoma/prevention & control , Humans , Inhibitory Concentration 50 , Isoenzymes/metabolism , Kinetics , Mice , Picolines/chemistry , Protons , Spectrum AnalysisABSTRACT
A novel proton transfer compound, pyridin-2-ylmethanaminium 2,4-dichloro-5-sulfamoylbenzoate (1), and a mixed-ligand Zn(II) complex, bis(2,4-dichloro-5-sulfamoylbenzoate)(2-aminomethylpyridine)aquazinc(II) monohydrate (2), have been synthesized from the same free ligands, which are 2,4-dichloro-5-sulfamoylbenzoic acid (Hsba) and 2-aminomethylpyridine (amp). They have been characterized by elemental, spectral ((1)H NMR, IR and UV-vis.) and thermal analyses. Additionally, magnetic measurement and single crystal X-ray diffraction technique were applied to compound 2. In the complex, Zn(II) ion exhibits a distorted octahedral configuration coordinated by O1 and O1(i) atoms of two mono dentante sba anions and N1, N2, N2(i) atoms of bidentante amp anion and a water molecule (O1w). The free ligands Hsba and amp, and the products 1 and 2, and acetazolamide (AAZ) as the control compound, were also evaluated for their in vitro inhibitor effects on human Carbonic Anhydrase isoenzymes (hCA I and hCA II) purified from erythrocyte cell by affinity chromatography for their hydratase and esterase activities. The IC(50) values of products 1 and 2 for hydratase activity are 0.26 and 0.13microM for hCA I and 0.30 and 0.15microM for hCA II, respectively. The IC(50) values of the same inhibitors for esterase activity are 0.32 and 0.045microM for hCA I and 0.29 and 0.23microM for hCA II, respectively. In relation to esterase activities, the inhibition equilibrium constants (K(i)) were also determined and found 0.25 and 0.058microM on hCA I and 0.22 and 0.24microM on hCA II for 1 and 2, respectively. The comparison of the inhibition studies of newly synthesized compounds 1 and 2 to parent compounds Hsba and amp and to AAZ indicated that 1 and 2 have effective inhibitory activity on hCA I and II, and might be used potential inhibitors.
Subject(s)
Carbonic Anhydrase Inhibitors/pharmacology , Glaucoma/drug therapy , Organometallic Compounds/pharmacology , Protons , Zinc/chemistry , Carbonic Anhydrase I/antagonists & inhibitors , Carbonic Anhydrase I/isolation & purification , Carbonic Anhydrase I/metabolism , Carbonic Anhydrase II/antagonists & inhibitors , Carbonic Anhydrase II/isolation & purification , Carbonic Anhydrase II/metabolism , Carbonic Anhydrase Inhibitors/chemical synthesis , Carbonic Anhydrase Inhibitors/chemistry , Crystallography, X-Ray , Erythrocytes/enzymology , Glaucoma/enzymology , Glaucoma/metabolism , Humans , Ligands , Magnetic Resonance Spectroscopy , Models, Molecular , Organometallic Compounds/chemical synthesis , Organometallic Compounds/chemistry , Spectroscopy, Fourier Transform Infrared , Structure-Activity Relationship , TemperatureABSTRACT
In the title compound, [Cu(CH3COO)2(C9H8N2O)2] n , the CuII ion resides on a centre of inversion, displaying a tetra-gonally distorted octa-hedral coordination environment defined by two pairs of N and O atoms of symmetry-related 4-(1H-imidazol-1-yl)phenol ligands and the O atoms of two symmetry-related acetate ligands. The bridging mode of the 4-(1H-imidazol-1-yl)phenol ligands is associated with a very long Cuâ¯O inter-actions involving the phenol O atom of the heterocyclic ligand, which creates chains extending parallel to [100]. In the crystal, the chains are arranged in a distorted hexa-gonal rod packing and are linked via C-Hâ¯O hydrogen bonds and by π-π stacking inter-actions involving centrosymmetrically related pairs of imidazole and phenol rings.
ABSTRACT
BACKGROUND: Colorectal cancer is a serious disease that causes significant morbidity and mortality in developed countries. Genetic changes, such as mutations in proto-oncogenes and DNA repair genes, and loss of function in the tumor suppressor genes cause colorectal cancer development. Abnormal DNA methylation is also known to play a crucial role in colorectal carcinogenesis. OBJECTIVE: In this study, frequencies of KRAS and BRAF mutations, promoter hypermethylation profiles of SFRP2, DAPK1, MGMT, HIC1 and p16 genes, and possible associations between hypermethylation of these genes and KRAS and BRAF mutations were aimed to find out. METHODS: Ninety three colorectal cancer tissues and 14 normal colon mucosas were included in the study. Common twelve KRAS gene mutation were investigated with using reverse-hybridization strip assay method. BRAF V600E mutations were investigated with RFLP method. Hypermethylation status of five tumor suppressor genes were detected by using reverse-hybridization strip assay method after bisulfite modification of DNA. RESULTS: KRAS and BRAF mutation frequencies were determined as 54.84% and 12.9%, respectively. Promoter hypermethylation frequencies of tumor suppressor genes SFRP2, DAPK1, MGMT, HIC1 and p16 were determined as 66.7%, 45.2%, 40.9%, 40.9% and 15.1%, respectively. Statistically significant associations were found between BRAF mutation and SFRP2 and p16 tumor suppressor genes hypermethylation (SFRP2; p= 0.005, p16; p= 0.016). Compared to rectum, SFRP2 (p= 0.017) and MGMT (p= 0.013) genes have statistically significantly higher promoter hypermethylation in colon. CONCLUSIONS: Results of the current study have confirmed that KRAS mutations and SFRP2 hypermethylation can be used as genetic markers in colorectal cancer.
Subject(s)
Colorectal Neoplasms/genetics , DNA Methylation , Mutation , Oncogene Proteins/genetics , Promoter Regions, Genetic , Tumor Suppressor Proteins/genetics , Aged , Aged, 80 and over , Case-Control Studies , Codon , Colorectal Neoplasms/pathology , CpG Islands , DNA Modification Methylases/genetics , DNA Repair Enzymes/genetics , Female , Genes, p16 , Genes, ras , Humans , Male , Middle Aged , Mutation Rate , Proto-Oncogene Proteins B-raf/geneticsABSTRACT
Novel pyrimidine compound bearing disulfide bridge, 5,5'-disulfanediylbis(2-amino-4,6-dimetoxypyrimidine) (3) was synthesized by reduction of 2-amino-4,6-dimethoxy-5-thiocyanatopyrimidine for the first time, and its structure was confirmed by X-ray crystallographic analysis. Novel binuclear antimony(III) compound of (3), {Sb[5,5'-disulfanediylbis(2-amino-4,6-dimetoxypyrimidine)]Cl3}2 (4) and mononuclear antimony(III) compounds, SbL2Cl3, [L: 2-amino-5-thiol-4,6-dimethoxy pyrimidine (2) and 2-amino-5-(1H-tetrazol-5-ylthio)-4,6-dimethoxypyrimidine (6)] were synthesized and characterized with the help of elemental analysis, molecular conductivity, FT-IR, (1)H-NMR and LC-MS techniques. The geometrical structures optimized by a DFT/B3LYP/LANL2DZ method of the compounds, indicated that monomeric compounds have square pyramidal shape. Both antileishmanial activity against Leishmania tropica promastigote and glutathione reductase inhibitory activity were determined in vitro. The results showed that (3) has the best biological activity.
Subject(s)
Antimony/chemistry , Coordination Complexes/chemical synthesis , Pyrimidines/chemistry , Chromatography, High Pressure Liquid , Coordination Complexes/chemistry , Coordination Complexes/pharmacology , Crystallography, X-Ray , Glutathione Reductase/antagonists & inhibitors , Glutathione Reductase/metabolism , Inhibitory Concentration 50 , Leishmania tropica/drug effects , Magnetic Resonance Spectroscopy , Mass Spectrometry , Molecular Conformation , Protein Binding , Spectroscopy, Fourier Transform InfraredABSTRACT
Further elucidation of the molecular mechanisms underlying lung cancer (LC) is essential for the development of new effective therapeutic agents. Recently, involvement of Wnt antagonists in oncogenesis has been demonstrated in several cancers. The investigation of their contribution to lung carcinogenesis is still under investigation. We aimed to investigate whether there is a susceptibility or preventive effect of Wnt antagonist gene polymorphisms on the development and/or prognosis of LC. We investigated 110 LC patients and 160 controls. Single-nucleotide polymorphisms of Wnt antagonist genes including DKK2 (rs17037102), DKK3 (rs3206824), DKK3 intron4 G/C (rs7396187), DKK4 (rs2073664), and sFRP4 (rs1802074) were analyzed using nested polymerase chain reaction and restriction fragment length polymorphism. Results showed that patients with DKK3 AA compared with controls have a decreased risk of LC (adjusted for smoking habit, body mass index, and familial history) (P = 0.02; odds ratio [OR],0.08; 95% confidence interval [95% CI], 0.01-0.7). It was found that, for sFRP4 polymorphism, patients with GG and GA genotypes versus AA genotype controls showed a decreased risk for LC (P = 0.01; [OR, 0.19; 95% CI, 0.05-0.73 for GG genotype]; [OR = 0.18, 95% CI, 0.04-0.72 for GA genotype]). In addition, a decreased risk of LC was also found for the genotype combination of DKK3 (rs3206824) GG and sFRP4 AG + GG (P = 0.004; OR, 0.12; 95% CI, 0.02-0.58). We suggest that these 2 polymorphisms have a protective effect on LC in this study.
Subject(s)
Intercellular Signaling Peptides and Proteins/genetics , Lung Neoplasms/diagnosis , Lung Neoplasms/genetics , Polymorphism, Single Nucleotide/genetics , Proto-Oncogene Proteins/genetics , Wnt Signaling Pathway/genetics , Adaptor Proteins, Signal Transducing , Adult , Aged , Aged, 80 and over , Case-Control Studies , Chemokines , Female , Humans , Male , Middle AgedABSTRACT
OBJECTIVE: To investigate the safety of laparoscopic intervention for diagnosis and treatment at 8 mm Hg pressure in one-hour period on acute peritonitis related intra-abdominal sepsis model. METHODS: In this study, we included 32 female Wistar-Albino rats, weighing 250 +/- 20 g, and divided them into 4 groups. This study was conducted in Istanbul University Experimental Medical Research Institution (DETAE) laboratory from April to May 2009. Intra-abdominal sepsis was created with intraperitoneal (i.p.) one mL (109 CFU/mL) Escherichia coli (E. coli) injection, and pneumoperitoneum was formed with CO2 insufflation at 8 mm Hg pressure for one hour i.p. The rats were administered with: Group 1 - one mL i.p. isotonic saline; Group 2 - one mL i.p. isotonic saline + pneumoperitoneum; Group 3 - i.p E. coli; and Group 4 - i.p. E.coli + pneumoperitoneum. Data were analyzed using the Statistical Package for Social Sciences version 15 for Windows (SPSS Inc, Chicago, IL, USA). RESULTS: Fever and leukocyte values were considered high in Groups 3 and 4 compared with Groups 1 and 2 (p=0.001). The administered reproduction ratio of the E. coli strain was determined as 0% in Groups 1 and 2, and 100% in Groups 3 and 4. CONCLUSION: In this study, as pneumoperitoneum was formed for one hour at 8 mm Hg pressure, in case of intra-abdominal derived sepsis where emergency intervention is needed, we consider that laparoscopic approaches with low pressure may be used safely for diagnosis and treatment.
Subject(s)
Bacterial Translocation , Intestines/blood supply , Ischemia/etiology , Pneumoperitoneum, Artificial/adverse effects , Pressure/adverse effects , Animals , Female , Laparoscopy/adverse effects , Peritonitis , Rats , Rats, WistarABSTRACT
Molecules of the title compound (alternative name p-methoxybenzaldehyde 2-pyridylhydrazone), C(13)H(13)N(3)O, adopt an E configuration about the azomethine C=N double bond. Molecules are almost planar, the dihedral angle between the pyridine and methoxyphenyl rings being only 6.19 (12) degrees. Pairwise N-H.N hydrogen bonds [R(2)(2)(8) in graph-set notation] link centrosymmetrically related molecules into discrete pairs.
ABSTRACT
Molecules of the title compound (alternative name: p-nitrobenzaldehyde phenylhydrazone), C(13)H(11)N(3)O(2), adopt an E configuration about the azomethine C=N double bond. Molecules are approximately planar and the dihedral angle between the planes of the phenyl rings is 11.62 (9) degrees. Hydrogen bonding links molecules related by 4(2) screw axes to form helices with a pitch of 7.7186 (8) A.