Preoperative progressive pneumoperitoneum in patients with abdominal-wall hernias.

Induction of preoperative progressive pneumoperitoneum is an elective procedure in patients with hernias with loss of domain. A prospective study was carried out from June 2003 to May 2005 at the Hospital de Especialidades, Instituto Mexicano del Seguro Social, Leon, Mexico. Preoperative progressive pneumoperitoneum was induced using a double-lumen intraabdominal catheter inserted through a Veress needle and daily insufflation of ambient air. Variables analyzed were age, sex, body mass index, type, location and size of defective hernia, number of previous repairs, number of days pneumoperitoneum was maintained, type of hernioplasty, and incidence of complications. Of 12 patients, 2 were excluded because it was technically impossible to induce pneumoperitoneum. Of the remaining 10 patients, 60% were female and 40% were male. The patients' average age was 51.5 years, average body mass index was 34.7, and evolution time of their hernias ranged from 8 months to 23 years. Nine patients had ventral hernias and one had an inguinal hernia. Pneumoperitoneum was maintained for an average of 9.3 days and there were no serious complications relating to the puncture or the maintenance of the pneumoperitoneum. One patient who previously had undergone a mastectomy experienced minor complications. We were able to perform hernioplasty on all patients, eight with the Rives technique, one with supra-aponeurotic mesh, and one using the Lichtenstein method for inguinal hernia repair. One patient's wound became infected postoperatively. Preoperative progressive pneumoperitoneum is a safe procedure that is easy to perform and that facilitates surgical hernia repair in patients with hernia with loss of domain. Complications are infrequent, patient tolerability is adequate, and the proposed modification to the puncture technique makes the procedure even safer.

Comparison of soluble and membrane-bound pyroglutamyl peptidase I activities in rat brain tissues in the presence of detergents.

Pyroglutamyl peptidase I activity from soluble and membrane-bound fractions of rat brain homogenates is inhibited by the presence of sodium deoxycholate but not by triton X-100. Biobeads SM2, a polystyrene adsorbent reported to be useful in removing detergents from aqueous solutions, inhibits enzymatic activity in both fractions regardless of the presence of these detergents, probably because of partial adsorption of the enzyme by the polymeric microspheres. These effects seem to be enzyme-specific since other aminopeptidase activities are not affected by detergents or biobeads. The results suggest that soluble and membrane-bound forms of the enzyme represent the same protein in two different cell compartments.

Properties of rat brain dipeptidyl aminopeptidases in the presence of detergents.

Rat brain dipeptidyl aminopeptidases I to IV were assayed in the soluble and membrane-bound fractions of rat brain, and the effects of the detergents Triton X-100 and sodium deoxycholate on their activities were studied. Dipeptidyl aminopeptidases I and II were significantly inhibited in the presence of sodium deoxycholate, but were not affected by the presence of Triton X-100. However, dipeptidyl aminopeptidase III was not influenced by either detergent, whereas the activity of dipeptidyl aminopeptidase IV was stimulated in the presence of Triton X-100, but remained unaffected by deoxycholate. These effects were partially or totally reversed after detergents were removed from the medium with adsorbent polymeric beads. Although detergents may have different effects on each DAP activity, the behavior of each enzyme activity in the presence of these substances was similar regardless of their subcellular location. These findings suggest that, as with other aminopeptidases, each of these proteins corresponds to the same molecular species in two different cell compartments.

Effect of lindane on galactose and leucine transport in chicken enterocytes.

Lindane (gamma-hexachlorocyclohexane) influence on the in vitro intestinal transport of D-galactose and L-leucine has been studied in isolated chicken enterocytes. Animals were injected i.p. with 30 mg/kg b.w. of the pesticide over 7 days. Total uptake of D-galactose and L-leucine was significantly decreased by lindane action. There was no alteration in the non-mediated component, but the mediated transport was markedly inhibited in both cases. Furthermore, the exit of D-galactose across the basolateral membrane, as well as (Na(+)-K+)-ATPase activity, was significantly decreased in pesticide-treated chickens.

Regional distribution of soluble and membrane-bound aminopeptidase activities in rat brain.

Soluble and membrane-bound aminopeptidase activities in 11 regions of the rat brain were assayed using L-Leucine-2-naphthylamide as a substrate. In addition, two metabolic enzymatic activities were compared: lactate dehydrogenase and aspartate aminotransferase. All enzymatic activities showed significant regional differences when the data were analyzed statistically. Soluble aminopeptidase and aspartate aminotransferase activities were significantly lower in cortical than in subcortical areas. Membrane-bound aminopeptidase activity levels were higher in cortical areas. Lactate dehydrogenase activities did not differ between cortical areas and the rest of the zones studied. However, although no wide regional differences were found for the other enzymatic activities, membrane-bound aminopeptidase varied markedly across brain regions: a fivefold difference was observed between zones such as parietotemporal cortex and medulla. The differential distribution of this enzymatic activity is consistent with the hypothesis that it could be responsible for the enzymatic inactivation of some neuroactive peptides.

[Regional distribution of brain aminopeptidases in the rat]. / Distribución regional de aminopeptidasas cerebrales en rata.

Soluble and membrane-bound aminopeptidase activities in eleven regions of the rat brain were assayed using L-leucine-2-naphthylamide as a substrate. In addition, two metabolic enzymatic activities were compared: lactate dehydrogenase and aspartate aminotransferase. All enzymatic activities showed significant regional differences when the data were analyzed statistically. Soluble aminopeptidase and aspartate aminotransferase activities were significantly lower in cortical than in subcortical areas. Membrane-bound aminopeptidase activity levels were higher in cortical areas. Lactate dehydrogenase activities did no differ between cortical areas and the rest of the zones studied. However, while no wide regional differences were found for the other enzymatic activities, membrane-bound aminopeptidase varied markedly across brain regions: a 5-fold difference was observed between zones. The differential distribution of this enzymatic activity is consistent with the hypothesis that it is responsible for the enzymatic inactivation of some neuroactive peptides.