Assessment of third ventriculostomy patency with the 3D-SPACE technique: a preliminary multicenter research study

OBJECT The goal of this study was to determine the value of the 3D sampling perfection with application-optimized contrasts using different flip-angle evolutions (3D-SPACE) technique in the evaluation of endoscopic third ventriculostomy (ETV) patency. METHODS Twenty-six patients with ETV were examined using 3-T MRI units. Sagittal-plane 3D-SPACE with variant flip-angle mode, 3D T1-weighted (T1W), and 3D heavily T2-weighted (T2W) images were obtained with isotropic voxel sizes. Also, sagittal-axial plane phase-contrast cine (PC)-MR images were obtained. The following findings were evaluated: diameters of stoma and third ventricle, flow-void sign on 3D-SPACE and PC-MR images, integrity of the third ventricle on heavily T2W images, and quantitative PC-MRI parameters of the stoma. Obtained sequences were evaluated singly, in combination with one another, and all together. RESULTS The mean area, flow, and velocity values measured at the level of stoma in patients with patent stoma were significantly higher than those measured in patients with closed stoma (p < 0.05). There was significant correlation among PC-MRI, 3D-SPACE, and 3D heavily T2W techniques regarding assessment of ETV patency (p < 0.001). The 3D-SPACE technique provided the lowest rate of ambiguous results. CONCLUSIONS The 3D-SPACE technique seems to be the most efficient one for determination of ETV patency. The authors suggest the use of 3D-SPACE as a stand-alone first-line sequence in addition to routine brain MRI protocols in assessing patients with ETV, thereby decreasing scan time and reserving the use of a combination of additional sequences such as PC-MRI and 3D heavily T2W images in suspicious or complex cases

Inhibitory effects of isatin Mannich bases on carbonic anhydrases, acetylcholinesterase, and butyrylcholinesterase

The effects of isatin Mannich bases incorporating (1-[piperidin-1-yl (P1)/morpholin-4-yl (P2)/N-methylpiperazin-1-yl (P3)]methyl)-1H-indole-2,3-dione) moieties against human (h) carbonic anhydrase (CA, EC 4.2.1.1) isoenzymes hCA I and hCA II, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes were evaluated. P1-P3 demonstrated impressive inhibition profiles against AChE and BChE and also inhibited both CAs at nanomolar level. These inhibitory effects were more powerful in all cases than the reference compounds used for all these enzymes. This study suggests that isatin Mannich bases P1-P3 are good candidate compounds especially for the development of new cholinesterase inhibitors since they were 2.2-5.9 times better inhibitors than clinically used drug Tacrine

Synthesis, crystal structure and biological evaluation of spectroscopic characterization of Ni(II) and Co(II) complexes with N‐salicyloil‐N′‐maleoil‐hydrazine as anticholinergic and antidiabetic agents

[Ni(C11H9N2O5)(2)(H2O)(2)]center dot 3(C3H7NO) (1) and [Co(C11H9N2O5)(2)(H2O)(2)]center dot 3(C3H7NO) (2) are synthesized and characterized by elemental analysis, FT-IR spectra, magnetic susceptibility, and thermal analysis. In addition, the crystal structure of Ni(II) complex is presented. Both complexes show distorted octahedral geometry. In 1 and 2, metal ions are coordinated by two oxygen atoms of salicylic residue and two nitrogen atoms of maleic amide residue from two ligands, and two oxygen atoms from two water molecules. In this paper, both compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I, and II, -glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Compounds 1 and 2 had Ki values of 18.36 +/- 4.38 and 26.61 +/- 7.54 nM against hCA I and 13.81 +/- 3.02 and 29.56 +/- 6.52 nM against hCA II, respectively. On the other hand, their Ki values were found to be 487.45 +/- 54.18 and 453.81 +/- 118.61 nM against AChE and 199.21 +/- 50.35 and 409.41 +/- 6.86 nM against BChE, respectively

Investigation of acetylcholinesterase and mammalian DNA topoisomerases, carbonic anhydrase inhibition profiles, and cytotoxic activity of novel bis(-aminoalkyl)phosphinic acid derivatives against human breast cancer

The aim of this study was to evaluate biologically active novel molecules having potentials to be drugs by their antitumor properties and by activities of apoptotic caspase and topoisomerase. Following syntheses of novel eight bis(-aminoalkyl)phosphinic acid derivatives (4a-h) as a result of array of reactions, compounds were evaluated by cytotoxic effects in vitro on human breast cancer (MCF-7) and normal endothelial (HUVEC) cell lines. All phosphinic acid derivatives were effective for cytotoxicity on both MCF-7 and HUVEC lines, while 4c, 4e, and 4f compounds were found significantly more effective. For the evaluation of antitumor properties of compounds in a highly sensitive method, their effects on inhibiting topoisomerases I and II were investigated. Also, some of the bis(-aminoalkyl)phosphinic acid derivatives (4a, 4e-h) showed nice inhibitory action against acetylcholinesterase and human carbonic anhydrase isoforms I and II

Novel amides of 1,1‐bis‐(carboxymethylthio)‐1‐arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties

The thiolation reaction was carried out in a benzene solution at 80 degrees C and p-substituted ketones and mercaptoacetic acid in a molar ratio (1:4) of in the presence of a catalytic amount of toluene sulfonic acids. The enzyme inhibition activities of the novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives were investigated. These novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives showed good inhibitory action against acetylcholinesterase (AChE) butyrylcholinesterase (BChE), and human carbonic anhydrase I and II isoforms (hCA I and II). AChE inhibitors, interacting with the enzyme as their primary target, are applied as relevant drugs and toxins. Many clinically established drugs are carbonic anhydrase inhibitors, and it is highly anticipated that many more will eventually find their way into the market. The novel synthesized compounds inhibited AChE and BChE with K-i values in the range of 0.64-1.47 nM and 9.11-48.12 nM, respectively. On the other hand, hCA I and II were effectively inhibited by these compounds, with K-i values between 63.27-132.34 and of 29.63-127.31 nM, respectively

Characterization and inhibition effects of some metal ions on carbonic anhydrase enzyme from Kangal Akkaraman sheep

In this work, the carbonic anhydrase (CA) enzyme was purified from Kangal Akkaraman sheep in Sivas, Turkey with specific activity value of 6681.57 EU/mg and yield of 14.90% with using affinity column chromatography. For designating the subunit molecular mass and enzyme purity. sodium dodecyl sulfate polyacrylamide gel electrophoresis method was used and single band for this procedure was obtained. The molecular mass of CA enzyme was found as 28.89 kDa. In this study, the optimum temperature and optimum pH were obtained from 30 and 7.5. V-max and K(m )values for p-nitrophenylacetate substrate of the CA were determined from Lineweaver-Burk graphs. Additionally, the inhibitory results of diverse heavy metal ions (He+, Fe2+, pb(2+), co(2+), A(g+), and Cu2+) on sheep were studied. Indeed, CA enzyme activities of Kangal sheep were investigated with using esterase procedure under in vitro conditions. The heavy metal concentrations inhibiting 50% of enzyme activity (IC50) and K-i values were obtained

The in vivo effects of cefazolin, cefuroxime, and cefoperazon on the carbonic anhydrase in different rat tissues

PubMed: 29457666In this paper, the in vivo effects of some antibiotics including cefazolin, cefuroxime, and cefoperazon, on the activity of the carbonic anhydrase enzyme (CA) in heart, brain, eye, liver, and kidney tissues of rats were evaluated. For this purpose, 16 different groups, which each containing six rats (n = 6), were formed (control group, cefazolin groups, cefuroxime groups, and cefoperazon groups). The rats were necropsied 60 min after the intraperitoneal injection of the chemicals into the rats. The CA activities were measured for each tissue using esterase activity methods. The activity values for each tissue obtained were statistically calculated. The CA activities in the liver tissue were assessed, and the activities of the cefoperazon groups were decreased compared to the sham groups from the third hour (p < 0.05). In the cefuroxime and cefoperazon groups, the CA activities in the eye tissue were decreased during the first 3 h and then increased (p < 0.05). © 2018 Wiley Periodicals, Inc