scholarly journals Three dimensional printed models of the airway for preoperative planning of open Laryngotracheal surgery in children: Surgeon’s perception of utility

Author(s):  
Oshri Wasserzug ◽  
Gadi Fishman ◽  
Narin Carmel-Neiderman ◽  
Yael Oestreicher-Kedem ◽  
Maher Saada ◽  
...  

Abstract Background Preoperative planning of open laryngotracheal surgery is important for achieving good results. This study examines the surgeon’s perception of the importance of using life size 3D printed models of the pediatric airway on surgical decision making. Methods Life-size three-dimensional models of the upper airway were created based on CT images of children scheduled for laryngotracheal-reconstruction and cricotracheal resection with anastomosis. Five pediatric airway surgeons evaluated the three-dimensional models for determining the surgical approach, incision location and length, graft length, and need for single or double-stage surgery of seven children (median age 4.4 years, M:F ratio 4:3). They rated the importance of the three-dimensional model findings compared to the direct laryngoscopy videos and CT findings for each domain on a validated Likert scale of 1–5. Results The mean rating for all domains was 3.6 ± 0.63 (“moderately important” to “very important”), and the median rating was 4 (“very important”). There was full agreement between raters for length of incision and length of graft. The between-rater agreement was 0.608 (“good”) for surgical approach, 0.585 (“moderate”) for incision location, and 0.429 (“moderate”) for need for single- or two-stage surgery. Conclusion Patient-specific three-dimensional printed models of children’s upper airways were scored by pediatric airway surgeons as being moderately to very important for preoperative planning of open laryngotracheal surgery. Large–scale, objective outcome studies are warranted to establish the reliability and efficiency of these models. Graphical abstract

Surgery ◽  
2020 ◽  
Vol 167 (2) ◽  
pp. 259-263 ◽  
Author(s):  
Michael G. Bateman ◽  
William K. Durfee ◽  
Tinen L. Iles ◽  
Cindy M. Martin ◽  
Kenneth Liao ◽  
...  

1975 ◽  
Vol 39 (8) ◽  
pp. 544-546
Author(s):  
HL Wakkerman ◽  
GS The ◽  
AJ Spanauf

2020 ◽  
Vol 17 (4) ◽  
pp. 342-351
Author(s):  
Sergio A. Durán-Pérez ◽  
José G. Rendón-Maldonado ◽  
Lucio de Jesús Hernandez-Diaz ◽  
Annete I. Apodaca-Medina ◽  
Maribel Jiménez-Edeza ◽  
...  

Background: The protozoan Giardia duodenalis, which causes giardiasis, is an intestinal parasite that commonly affects humans, mainly pre-school children. Although there are asymptomatic cases, the main clinical features are chronic and acute diarrhea, nausea, abdominal pain, and malabsorption syndrome. Little is currently known about the virulence of the parasite, but some cases of chronic gastrointestinal alterations post-infection have been reported even when the infection was asymptomatic, suggesting that the cathepsin L proteases of the parasite may be involved in the damage at the level of the gastrointestinal mucosa. Objective: The aim of this study was the in silico identification and characterization of extracellular cathepsin L proteases in the proteome of G. duodenalis. Methods: The NP_001903 sequence of cathepsin L protease from Homo sapienswas searched against the Giardia duodenalisproteome. The subcellular localization of Giardia duodenaliscathepsin L proteases was performed in the DeepLoc-1.0 server. The construction of a phylogenetic tree of the extracellular proteins was carried out using the Molecular Evolutionary Genetics Analysis software (MEGA X). The Robetta server was used for the construction of the three-dimensional models. The search for possible inhibitors of the extracellular cathepsin L proteases of Giardia duodenaliswas performed by entering the three-dimensional structures in the FINDSITEcomb drug discovery tool. Results: Based on the amino acid sequence of cathepsin L from Homo sapiens, 8 protein sequences were identified that have in their modular structure the Pept_C1A domain characteristic of cathepsins and two of these proteins (XP_001704423 and XP_001704424) are located extracellularly. Threedimensional models were designed for both extracellular proteins and several inhibitory ligands with a score greater than 0.9 were identified. In vitrostudies are required to corroborate if these two extracellular proteins play a role in the virulence of Giardia duodenalisand to discover ligands that may be useful as therapeutic targets that interfere in the mechanism of pathogenesis generated by the parasite. Conclusion: In silicoanalysis identified two proteins in the Giardia duodenalisprotein repertoire whose characteristics allowed them to be classified as cathepsin L proteases, which may be secreted into the extracellular medium to act as virulence factors. Three-dimensional models of both proteins allowed the identification of inhibitory ligands with a high score. The results suggest that administration of those compounds might be used to block the endopeptidase activity of the extracellular cathepsin L proteases, interfering with the mechanisms of pathogenesis of the protozoan parasite Giardia duodenalis.


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