Laparoendoscopic pfannenstiel nephrectomy using conventional laparoscopic instruments - preliminary experience

PURPOSE: To confirm the feasibility of the laparoendoscopic Pfannenstiel nephrectomy using conventional laparoscopic instruments. MATERIALS AND METHODS: Since March 2009, laparoscopic nephrectomy through a Pfannenstiel incision has been performed in selected patients in our service. The Veress needle was placed through the umbilicus which allowed carbon dioxide inflow. One 5 mm (or 10 mm) trocar was placed at the umbilicus for the laparoscope, to guide the placement of three trocars over the Pfannenstiel incision. Additional trocars were placed as follows: a 10 mm in the midline, a 10 mm ipsilateral to the kidney to be removed (2 cm away from the middle one), and a 5 mm contralateral to the kidney to be removed (2 cm away from the middle one). The entire procedure was performed using conventional laparoscopic instruments. At the end of the surgery, trocars were removed and all three incisions were united into a single Pfannenstiel incision for specimen retrieval. RESULTS: Five nephrectomies were performed following this technique: one atrophic kidney, one kidney donation, two renal cancers and one bilateral renal atrophy. Median operative time was 100 minutes and median intraoperative blood loss was 100 cc. No intraoperative complications occurred and no patients required blood transfusion. Median length of hospital stay was 1 day (range 1 to 2 days). CONCLUSIONS: The use of the Pfannenstiel incision for laparoscopic nephrectomy seems to be feasible even when using conventional laparoscopic instruments, and can be considered a potential alternative for traditional laparoscopic nephrectomy

Structure and Membrane Interactions of the Antibiotic Peptide Dermadistinctin K by Multidimensional Solution and Oriented 15N and 31P Solid-State NMR Spectroscopy

DD K, a peptide first isolated from the skin secretion of the Phyllomedusa distincta frog, has been prepared by solid-phase chemical peptide synthesis and its conformation was studied in trifluoroethanol/water as well as in the presence of sodium dodecyl sulfate and dodecylphosphocholine micelles or small unilamellar vesicles. Multidimensional solution NMR spectroscopy indicates an α-helical conformation in membrane environments starting at residue 7 and extending to the C-terminal carboxyamide. Furthermore, DD K has been labeled with 15N at a single alanine position that is located within the helical core region of the sequence. When reconstituted into oriented phosphatidylcholine membranes the resulting 15N solid-state NMR spectrum shows a well-defined helix alignment parallel to the membrane surface in excellent agreement with the amphipathic character of DD K. Proton-decoupled 31P solid-state NMR spectroscopy indicates that the peptide creates a high level of disorder at the level of the phospholipid headgroup suggesting that DD K partitions into the bilayer where it severely disrupts membrane packing