Minimizing Ports During Robotic Partial Nephrectomy

Methods:Data on 11 robot-assisted laparoscopic partial nephrectomies performed by using our technique from February 2015 through June 2015 were retrospectively analyzed. The robotic platform used was DaVinci Xi (Intuitive Surgical, Inc., Sunnyvale, California, USA) with a 3-arm setup. The AirSeal system (SurgiQuest, Milford, Connecticut, USA) was used as a port allowing simultaneous introduction of 2 instruments for the bedside surgeon, obviating the need for an additional (fourth) robotic arm. A long suction-and-irrigation device and atraumatic grasping forceps were used. Both instruments were introduced through the trocar of the AirSeal system, making simultaneous introduction and use possible. We preferred the long suction-and-irrigation device, because it minimizes collision of the instruments.Results:Mean age and BMI of the patients were 55 ±14.6 y and 29.18 ± 6.85, respectively. Seven tumors were on the right side and 4 were on the left. The mean size of the tumors was 32.45 mm (± 11.31). Surgical time was 132.2 minutes (±37.17), with an estimated blood loss and ischemia time of 103.63 mL (±65.92) and 16.72 minutes (±9.52), respectively. One patient had postoperative bleeding that was resolved without transfusion. The median hospitalization period was 3.9 d (±0.53). Loss of intra-abdominal pressure was not observed, and pressure was stable at 10 mm Hg.Conclusion:The AirSeal System and its valveless trocar eliminated the need for an additional port placement in our series. The technique is feasible, safe, and reproducible; therefore, it may be implemented in selected cases of robot-assisted partial nephrectomies.     

MBL,P2X7, and SLC11A1 gene polymorphisms in patients with oropharyngeal tularemia

Conclusion: A significant association was found of oropharyngeal tularemia with SLC11A1 allele polymorphism (INT4?G/C) and MBL2 C?+?4T (P/Q). These results indicate C allele and Q allele might be a risk factor for the development of oropharyngeal tularemia.

Aim: This study aimed to investigate the relationship of SLC11A1, MBL, and P2X₇ gene polymorphism with oropharyngeal tularemia.

Methods: The study included totally 120 patients who were diagnosed with oropharyngeal tularemia. Frequencies of polymorphisms in the following genes were analyzed both in the patient and control groups in the study: SLC11A1 (5’(GT)_n Allele 2/3, Int4?G/C, 3’ UTR, D543N G/A), MBL (MBL2 C?+?4T (P/Q), and P2X₇ (?762 C/T and 1513 A/C).

Results: Among all polymorphisms that were investigated in this study, SLC11A1 gene showed a significance in the distriburtion of polymorphism allelle frequency at the INT4 region. Frequency of C allele was 54 (28%) in patients with oropharyngeal tularemia, and 31 (13%) in the control group (p?=?0.006 and OR = 1.96 (1.21–3.20)). An association was detected between MBL2 C?+?4T (P/Q) gene polymorphism and oropharyngeal tularemia (p?7 (?762 C/T and 1513 A/C) gene polymorphism and oropharyngeal tularemia in this study (p?>?0.05).     

Ideal,catch, and slip bonds in cadherin adhesion

Classical cadherin cell-cell adhesion proteins play key morphogenetic roles during development and are essential for maintaining tissue integrity in multicellular organisms. Classical cadherins bind in two distinct conformations, X-dimer and strand-swap dimer; during cellular rearrangements, these adhesive states are exposed to mechanical stress. However, the molecular mechanisms by which cadherins resist tensile force and the pathway by which they convert between different conformations are unclear. Here, we use single molecule force measurements with an atomic force microscope (AFM) to show that E-cadherin, a prototypical classical cadherin, forms three types of adhesive bonds: catch bonds, which become longer lived in the presence of tensile force; slip bonds, which become shorter lived when pulled; and ideal bonds that are insensitive to mechanical stress. We show that X-dimers form catch bonds, whereas strand-swap dimers form slip bonds. Our data suggests that ideal bonds are formed as X-dimers convert to strand-swap binding. Catch, slip, and ideal bonds allow cadherins to withstand tensile force and tune the mechanical properties of adhesive junctions.