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Laparoscopic appendectomy for the children with perforated appendicitis in this study was associated with a significant decrease in the rate of wound infection. Furthermore, on the average, the children who underwent laparoscopic appendectomy tolerated enteral feedings and were discharged from the hospital approximately 24 h earlier than those who had open appendectomy.

The study aims to evaluate the effectiveness and safety of endoscopic balloon dilatation (EBD) in childhood benign esophageal strictures. The medical records of 38 patients who underwent EBD from 1999 to 2013 were retrospectively reviewed. Demographic features, diagnoses, features of strictures, frequency and number of EBD, complications, outcome, and recurrence data were recorded. Median age was 1.5 years (0-14), and female/male ratio was 17/21 (n = 38). Primary diagnoses were corrosive esophageal stricture (n = 19) and esophageal atresia (n = 19). The length of strictures were less than 5 cm in 78.9% (n = 30). No complication was seen in 86.8% (n = 33). Perforation was seen in 10.5% (n = 4), and recurrent fistula was seen in 2.7% (n = 1). Total treatment lasted for 1 year (1-11). Dysphagia was relieved in 60.5% (n = 23). Recurrence was seen in 31.6% (n = 12). Treatment effectiveness was higher, and complication rates were lower in strictures shorter than 5 cm compared with longer ones (70% vs. 25%, P < 0.05, and 3.4% vs. 37.5%, P < 0.05). Although there was no statistical difference, treatment effectiveness rates were lower and complication and recurrence rates were higher in corrosive strictures compared with anastomotic ones (P > 0.05). EBD is a safe and efficient treatment choice in esophageal strictures, especially in strictures shorter than 5 cm and anastomotic strictures.

Agouti-related protein (AGRP) is an endogenous antagonist of the melanocortin-4 receptor (MC4R) that functions in the hypothalamic control of feeding behavior. Our previous studies have suggested that in addition to exoloops 2 and 3, several transmembrane domains of MC4R may be important for AGRP binding. However, the detailed molecular basis of MC4R domains in AGRP binding is presently unclear. The present studies were designed to determine the specific contribution of MC4R exoloops and transmembrane domains to AGRP binding by using chimeric receptor constructs of the human melanocortin-1 receptor (hMC1R), a receptor that is not inhibited by AGRP, and the human MC4R (hMC4R), a receptor that is potently inhibited by AGRP. Our results indicate that substitutions of the second and third extracellular loops of the MC4R with homologous domains of the MC1R dramatically decreased AGRP 87-132 binding affinity, but did not affect AGRP 110 -117 binding affinity. In contrast, cassette substitutions of the third or fourth transmembrane domain of the MC4R with the homologous domain of the MC1R resulted in a substantial decrease of AGRP 87-132 binding affinity and loss of AGRP 110 -117 binding affinity. These data suggest that the AGRP fragment 110 -117 has no binding sites at exoloops of hMC4R and that transmembrane domains of MC4R may play an important role in AGRP 110 -117 binding and function, whereas the exoloops do not. The second and third extracellular loops of MC4R are important for AGRP 87-132 N-terminal binding, whereas the third and fourth transmembrane domains of hMC4R are crucial for AGRP 110 -117 binding.