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Abstract  Laparoscopy-assisted gastrectomy with extraperigastric lymph node dissection for gastric cancer is a complicated procedure that generally requires advanced laparoscopic surgical skill. We devised a simplified but effective laparoscopic procedure that provides a better visual field to perform safe lymph node dissection more quickly. First, a mini-laparotomy is done and a clear visual field is created by pulling a mini-retractor to the right or left. The laparoscopic procedure is made easier and safer by taping the stomach body, and by using the fringe of an abdominal wall sealing device (Lapdisk) placed behind the stomach, and a scope holder for the snake-retractor. The lymph nodes along the common hepatic vessels, left gastric vessels, and celiac artery (extraperigastric lymph nodes) are then dissected laparoscopically. The suprapyloric and infrapyloric lymph nodes are dissected through the mini-laparotomy incision and gastroduodenostomy is done using an anastomotic device. We performed laparoscopy-assisted distal gastrectomy (LADG) in 70 patients with gastric carcinomas located in the distal stomach (mean body mass index: 24.3). The mean operating time was 170 min and blood loss was minimal. All patients recovered well with minimal pain and good postoperative quality of life. We conclude that our simple and practical procedure for LADG with extraperigastric lymph node dissection can be performed safely and easily. [ABSTRACT FROM AUTHOR]

Endpolygalacturonase I from Stereum purpureum has been identified as a causative substance for the silver-leaf disease in apples. It possesses a unique pro-sequence in the C-terminal region that lacks endpolygalacturonases from any other origin. In this study, we analyzed and compared enzymatic characteristics between pro-form (pro-endoPG I) and mature form processed by V8 protease (endoPG I) and described the suppression activity of the pro-sequence. Of note, the optimal pH for pro-endoPG I activity shifted to pH 4.0 from pH 4.5-5.0 of endoPG I. The kinetic parameters indicated that the activity inhibition resulted from a pH-independent decrease of substrate affinity and pH-dependent deterioration of velocity by the pro-sequence. Analysis of site-directed mutations within pro-endoPG I showed that its α-helical structure includes two glutamates (E364 and E366) and alanine (A365), and its orientation by prolines (especially P348) in the pro-sequence played a significant role in its suppression activity. As for mutations in the mature domain, a marked reduction of suppression was observed for enzymes with mutations in H150, R220 and K253, indicating that the pro-sequence interacts with the active cleft by a few ionic bonds. [ABSTRACT FROM AUTHOR]