[Intraoperative fascial traction (IFT) for treatment of large ventral hernias : A retrospective analysis of 50 cases]. / Intraoperative Faszientraktion (IFT) zur Behandlung großer ventraler Hernien : Eine retrospektive Analyse von 50 Fällen.

OBJECTIVE: The aim was to evaluate the effectiveness, clinical practicability, and complication rate of the intraoperative fascial traction (IFT) procedure for the treatment of large ventral hernias. METHOD: This study evaluated 50 patients from 11 specialized centers with an intraoperatively measured fascial distance of more than 8 cm, who were treated by IFT (traction time 30-35 min) using the fasciotens® hernia traction procedure. RESULTS: Fascial gaps measured preoperatively ranged from 8 cm to 44 cm, with most patients (94%) having a fascial gap above 10 cm (W3 according to the European Hernia Society classification). The mean fascial distance was reduced from 16.1 ± 0.8 cm to 5.8 ± 0.7 cm (stretch gain 10.2 ± 0.7 cm, p < 0.0001, Wilcoxon matched-pairs signed-ranks test). A reduction in fascial distance of at least 50% was achieved in three quarters of the patients and in half of the treated patients the reduction in fascial distance amounted to even more than 70%. The closure rate achieved by IFT after a mean surgical duration of 207.3 ± 11.0 min was 90% (45/50). Hernia closure was performed in all cases with a mesh augmentation in a sublay position. Postoperative complications occurred in 6 patients (12%). A reoperation was required in 3 patients (6%). CONCLUSION: The described IFT method is a new procedure for abdominal wall closure in large ventral hernias. The presented results demonstrate a high effectiveness, a good clinical practicability and a low complication rate of IFT.

A cysteine near the C-terminus of UCH-L1 is dispensable for catalytic activity but is required to promote AKT phosphorylation, eIF4F assembly, and malignant B-cell survival.

The enzyme UCH-L1 is a neuro-endocrine and germinal center B-cell marker that contributes to the development and aggressive behavior of mature B-cell malignancies. While mutations in this enzyme have been associated with Parkinson's disease, relatively little is known about the molecular features associated with the biochemical activities of UCH-L1. Here we use a survival-based complementation assay and site-directed mutagenesis and identify a novel role for the C-terminus of UCH-L1 in supporting cell survival. The C220 residue is required for UCH-L1 to promote the assembly of mTOR complex 2 and phosphorylation of the pro-survival kinase AKT. While this residue was previously described as a potential farnesylation site, destruction of the putative CAAX motif by adding a C-terminal epitope tag did not interfere with cell survival, indicating an alternate mechanism. We used proximity-based proteomics comparing the proteomes of wild-type and C220S UCH-L1 and identified a selective loss of association with RNA-binding proteins including components of the translation initiation machinery. As a consequence, the C220S mutant did not promote the assembly of the eIF4F complex. These data identify a novel role for the C-terminus of UCH-L1 in supporting pro-survival and metabolic activities in malignant B-cells. This finding may lead to the development of therapeutics with selective activity towards malignancy that potentially avoid neuronal toxicities.