Search PubMed⌕ Search

Biomedical subjects

S Seth

Publications and source records attributed to S Seth.

At least 19 recordsLinked to original sources

Outcome after intra- and extra-corporeal laparoscopic appendectomy techniques.

BACKGROUND: This study aimed to assess the outcome after intracorporeal (IC) and extracorporeal (EC) laparoscopic appendectomy technique in a single institution over a 5-year period. METHODS: Records of all children ( n = 60) who underwent laparoscopic appendectomy at the Royal Aberdeen Children's Hospital between February 1997 and March 2002 were retrieved and evaluated. Observations were made regarding operative technique, anesthetic time, intra- and postoperative complications, postoperative analgesic requirement, and postoperative hospital stay. RESULTS: There were 30 children in each group who had a similar demographic profile. The magnitude of appendicitis severity in both groups was similar. The mean anesthetic time was 67.8 min for the IC group and 50.7 min for the EC group (p = 0.001). There were no recorded intraoperative complications, although a single case in the EC group required conversion to open procedure. The postoperative analgesic requirement in both groups was similar. The mean postoperative stay was 2.1 days in the IC group and 2.5 days in the EC group. Two postoperative complications were noted in the IC group; one intraperitoneal collection and one postoperative chest infection. Four complications occurred in the EC group; one intraperitoneal collection and three minor port-site wound infections. CONCLUSIONS: The authors' experience shows the EC technique to be significantly quicker, although with a slightly increased complication rate. Either technique can be applied safely for acute appendicitis.

Adolescent↗

Potentiality of a new compound for in vitro differentiation between halophilic and non-halophilic vibrios.

Sensitivity of 21 halophilic vibrios and 16 clinical isolates of non-halophilic vibrios was determined against a new possible antivibrio agent, a pyrimidine analogue, 4, 6-dimethylpyrimidine -2-thiol (4,6-DMPT). It appeared to be a vibriocidal agent, having a mean MIC and MBC of 32 microg/ml for halophilic strains and 64 microg/ml for non-halophilic strains and an LD50 of 300 mg/Kg body weight of mice. Thus, 4,6-DMPT may help an in vitro distinction between halophilic and non-halophilic vibrios. Sensitivity of these strains was also studied with respect to pteridine, crystal violet and Tween 80 hydrolysis as further markers distinguishing between these 2 groups which could also be differentiated by their growth on TCBS or/and CLED media.

Animals↗

The fusion protein of Peste des petits ruminants virus mediates biological fusion in the absence of hemagglutinin-neuraminidase protein.

To study the process of membrane fusion in Morbilliviruses, the fusion (F) glycoproteins of Peste des petits ruminants virus (PPRV) and Rinderpest virus (RPV) were expressed transiently in mammalian cells. The recombinant F proteins were found to be localized at the surface of transfected cells. The fusion activity, as evident from cell fusion assays and lysis of chicken erythrocytes, documented that transiently expressed PPRV F glycoprotein induces cell fusion in the absence of homotypic hemagglutinin-neuraminidase (HN) attachment glycoprotein. The coexpression of homotypic HN increased the extent of fusion by twofold, while the efficiency of fusion was found to be substantially enhanced. In contrast, in RPV F-expressing cells, fusion was detected only when homotypic hemagglutinin (H) or heterotypic HN protein was coexpressed. This differs from the strict type-specific requirement for the attachment protein as in the fusion process of most of the paramyxoviruses. Further, we demonstrate by fluorescence transfer experiments that while PPRV F brings about both hemifusion and complete fusion on its own, RPV F induces only hemifusion while it brings about complete fusion in the presence of homotypic or heterotypic attachment protein.

Animals↗

The hemagglutinin-neuraminidase protein of peste des petits ruminants virus is biologically active when transiently expressed in mammalian cells.

The genes coding for the surface glycoproteins hemagglutinin-neuraminidase (HN) of the peste des petits ruminants virus (PPRV) and hemagglutinin (H) of rinderpest virus (RPV) were cloned in a cytomagalovirus promoter driven expression vector and expressed transiently in mammalian cells. The protein expression was apparent 24 h after transfection and the expressed proteins were detected at the cell surface. The transiently expressed PPRV HN protein was found to be biologically active in possessing hemadsorption and neuraminidase activities. On the other hand, RPV H protein exhibited neuraminidase activity but was deficient in hemadsorption activity. The substrate specificity of the neuraminidase activity of these two proteins differed distinctly. The presence of neuraminidase activity in both PPRV HN and RPV H proteins is unusual among members of the morbillivirus genus.

Animals↗

Step-wise formation of helical structure and side-chain packing in a peptide from scorpion neurotoxin support hierarchic model of protein folding.

The mechanism of protein folding has been the subject of extensive investigation during the last decade, both because of its academic challenge and because of its relation to many diseases which are known to occur due to misfolding of proteins. In this context, we report here a systematic investigation on the step-wise formation of a helical structure by the addition of hexafluoroacetone, in a 14-residue peptide derived from a part of the scorpion neurotoxin protein. The NMR and circular dichroism results indicate that the peptide has an inherent propensity for helix formation and this is limited to the internal few residues in aqueous solution. With the addition of the fluorosolvent, the helical content progressively increases and spans the whole sequence. This is accompanied by concomitant packing of the side chains. These results provide support to the so-called hierarchic model of protein folding which dictates that the local sequence determines the secondary structures in the protein and the side chains play an important role in this process.

Acetone↗

Tissue eosinophilia correlates strongly with poor prognosis in nodular sclerosing Hodgkin's disease, allowing for known prognostic factors.

Although eosinophilic granulocytes are frequently observed in lymphatic tissue of Hodgkin's patients, no substantial data reveal the prognostic role, if any, of tissue eosinophilia. Thus, eosinophilia was analyzed histologically in 1511 diagnostic biopsy specimens of patients treated under protocol therapy of the German Hodgkin's Lymphoma Study Group between 1988 and 1994. Prominent eosinophilia was seen in 38% of cases, which differed among the histologic types of Hodgkin's disease (HD): none in lymphocyte predominant, 14% in lymphocyte rich classical, 40% in nodular sclerosis grade 1 (NS-1), 55% in nodular sclerosis grade 2, 43% in mixed cellularity (MC), and 54% in lymphocyte depleted. In a multivariate analysis, tissue eosinophilia proved to be the strongest prognostic factor for freedom from treatment failure (P <. 001) and overall survival (P <.001) in a stage-stratified model. Among NS-1 patients, the effect was highly significant. In MC, no significant effect of eosinophilia on survival could be demonstrated. Eosinophils secrete CD30 ligand that is capable of binding to CD30 positive HD cells. The activation of TRAF2, followed by NF-kappaB, which occurs on CD30L/CD30 binding, may explain the neoplastic proliferation and apoptosis protection of HD cells. TRAF2 is also activated by EBV-LMP expression, which is detectable in the majority of MC but not NS cases. In addition to the possibility that eosinophils are only passive indicators for other unknown prognostic determinants, it may be concluded that the positive clinical outcome of eosinophilia-negative NS cases could be due to lower NF-kappaB activity. (Blood. 2000;95:1207-1213)

Adolescent↗

A study of hypoglycaemic effects of Azadirachta indica (Neem) in normaland alloxan diabetic rabbits.

Hypoglycaemic effect was observed with Azadirachta indica when given as a leaf extract and seed oil, in normal as well as diabetic rabbits. The effect, however, was more pronounced in diabetic animals in which administration for 4 weeks after alloxan induced diabetes, significantly reduced blood glucose levels. Hypoglycaemic effect was comparable to that of glibenclamide. Pretreatment with A. indica leaf extract or seed oil administration, started 2 weeks prior to alloxan, partially prevented the rise in blood glucose levels as compared to control diabetic animals. The data suggests that A. indica could be of benefit in diabetes mellitus in controlling the blood sugar or may also be helpful in preventing or delaying the onset of the disease.

Animals↗

CD and NMR investigations on trifluoroethanol-induced step-wise folding of helical segment from scorpion neurotoxin.

A 14 amino acid residue peptide from the helical region of Scorpion neurotoxin has been structurally characterized using CD and NMR spectroscopy in different solvent conditions. 2,2,2-Trifluoroethanol (TFE) titration has been carried out in 11 steps from 0 to 90% TFE and the gradual stabilization of the conformation to form predominantly alpha-helix covering all of the 14 residues has been studied by 1H and 13C NMR spectroscopy. Detailed information such as coupling constants, chemical shift indices, NOESY peak intensities and amide proton temperature coefficients at each TFE concentration has been extracted and analysed to derive the step-wise preferential stabilization of the helical segments along the length of the peptide. It was found that there is a finite amount of the helical conformation in the middle residues 5-11 even at low TFE concentrations. It was also observed that > 75% TFE (v/v) is required for the propagation of the helix to the N and C termini and for correct packing of the side chains of all of the residues. These observations are significant to understanding the folding of this segment in the protein and may throw light on the inherent preferences and side chain interactions in the formation of the helix in the peptide.

Circular Dichroism↗

Characterization of a 22-residue peptide derived from a designed ion channel.

We have designed a four-helix protein that is expected to tetramerize in the membrane to form an ion channel with a structurally well-defined pore. This should serve as a model system to study the structural requirements of voltage-sensitive, ion-selective transmembrane channels. We have synthesized the peptide corresponding to the channel-lining helix. Circular dichroism (CD) spectroscopy shows that this peptide is helical in the membrane. Fluorescence resonance energy transfer (FRET) shows that this peptide, at low concentrations, forms aggregates in 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes and facilitates ion transport across liposomal membranes. Our data indicate that a component of the designed four-helix protein, i.e., the channel-lining helix, behaves as per design.

Alamethicin↗

The crystal and molecular structure of (HgL2)n (L = 4,6-dimethylpyrimidine-2-thiolate)--an unusual helical supramolecular assembly in solid phase: in search of a new antidote to mercury poisoning.

An X-ray crystallographic study reveals that in solid phase, 4,6-dimethylpyrimidine-2-thiol (4,6Me2 Pm2SH) forms a multinuclear complex with mercury, containing an open HgN3S2 core and exhibiting a helix-like polymerization through repetitive distant Hg(sp3d) ... N(sp2) interactions along the b axis of the lattice. The complex, therefore, exemplifies a supramolecular assembly, generated by successive vacant ligand site promoted self-associations. It crystallizes in the monoclinic space group P2(1)/c, a = 11.808(2), b = 9.198(2), and c = 14.702(3) A, beta = 112.19(3)0, Z = 4 (monomers). Such self-associative distant interactions are absent in solution phase, as observed from the 1H NMR spectrum (acetone-d6, TMS). A preliminary toxicological study of the pyrimidinethiol ligand reveals a high toxicity at substantially higher doses and appreciably low toxic effects at lower doses. The ligand is also highly potent in inhibiting all common gram negative bacteria (except the acid fast group, which was not tested) and this property may endow it with some side therapeutic uses when considered as an antidote to mercury poisoning following some functional modifications in order to reduce the toxic effects, even when administered at higher doses.

Animals↗

Protective actions of a thromboxane receptor antagonist, SQ 29548 on the ischemic myocardium: morphologic and hemodynamic effects.

The effects of thromboxane A2 (TXA2)/prostaglandin endoperoxide receptor blockade on myocardial infarct size and cardiac dynamics were determined in a canine model of 24 h acute myocardial infarction. Anesthetized open-chest dogs were subjected to left anterior descending (LAD) coronary artery occlusion. Twenty minutes post-occlusion the dogs were given i.v. saline (0.9% NaCl solution) (n = 12) or the TXA2 receptor antagonist SQ 29548 (0.2 mg/kg i.v. loading dose +0.2 mg/kg/h i.v. for 4 h) (n = 10). SQ 29548 treatment resulted in a significant (P < 0.01) reduction in infarct size. Heart rate (HR) and systolic blood pressure (SAP) were not markedly affected by the drug. The sharp rise in the left ventricular end diastolic pressure (LVEDP) in the saline-treated animals was significantly lowered by SQ 29548 treatment and the correction of this variable was maintained till 24 h post-occlusion. The lowered maximal rate of rise of left ventricular pressure (LVdP/dt max) in the saline-treated animals was corrected albeit non-significantly by the drug treatment. Thus, SQ 29548 treatment resulted in a significant salvage of myocardial tissue and marked alterations in left ventricular dynamics. The study suggests a deleterious role for thromboxane A2 in ischemia; indicating that TXA2 blockade may have potential as a mode of therapy for ischemic heart disease.

Animals↗

Biological activity of 4-(4-bromophenyl)-thiosemicarbazide.

The two molecules (A and B) in the asymmetric unit of the title compound, C7H8BrN3S, display different conformation. In both molecules, the S atom is trans to the NH2 group. The Br atoms of the two molecules approach each other at a distance of 3.573(2) A. The crystal structure of the bromine compound is isomorphous with that of its chlorine analogue. In the crystal structure, intramolecular N-H...N and intermolecular N-H...S hydrogen bonds help stabilize the molecular packing. The increased antibacterial activity of the title compound compared to that of its chlorine analogue may be attributed to the increase in electron density on the hydrazinic end of the thiosemicarbazide chain.

Anti-Bacterial Agents↗

Serial blood phosphine levels in acute aluminium phosphide poisoning.

Serial blood phosphine (PH3) levels were done in patients with severe (Group I, n = 30), mild (Group 2, n = 10) and minimal or nil toxicity due to aluminium phosphide compound. Blood phosphine levels were significantly higher (p < 0.001) in patients of Group I than other two groups. Phosphine was not detectable in Group 3 patients. Therefore, blood phosphine levels were positively correlated to clinical grades of toxicity and to dose of active pesticide consumed. Higher the blood phosphine, higher was the mortality. Patients having blood phosphine levels equal to or less than 1.067 +/- 0.16 mg% survived, hence, it appeared to be limit of phosphine toxicity.

Adult↗