The role of preoperative optimization of the nutritional status on the improvement of short-term outcomes after liver transplantation? - A review of the literature and expert panel recommendations

Background: Malnutrition is a known risk factor for postoperative morbidity and mortality in patients awaiting liver transplantation (LT). Malnutrition is a potentially reversible risk factor, though there are no clear guidelines on the best mechanism for an improvement. It also remains unclear if preoperative nutritional interventions have benefits to post-transplant outcomes for transplant recipients. Objectives: Primary objective: To identify if preoperative optimization of nutritional status is associated with improved short-term outcomes after LT. Secondary objectives: To determine if preoperative improvement of malnutrition improves short-term outcomes after LT, as well as, if weight loss in obese patients affects short-term outcomes after LT. Data sources: Ovid MEDLINE, Embase, Scopus, Google Scholar, and Cochrane Central. Methods: Systematic review following PRISMA guidelines and recommendations using the GRADE approach derived from an international expert panel. POSPERO Protocol ID: CRD42021237450 RESULTS: 3851 records were identified in searching the databases, 3843 records were excluded by not fulfilling eligibility criteria. Seven full-text articles were included for the final analysis of which three were randomized controlled trials, one was prospective observational studies, and three were retrospective observational studies. No appreciable difference in mortality, post-transplant complication rate was noted across the studies. Length of stay (LOS) was noted to be shorter in two observational studies of Vitamin D deficiency in liver transplant patients. Conclusions: We have made a weak recommendation supporting pre-transplant nutritional supplementation due to possible benefit in reducing LOS as well as the lack of harms (Quality of Evidence low | Grade of Recommendation; Weak). No effective conclusions were reached for the secondary objectives due to the conflicting evidence. This article is protected by copyright. All rights reserved

Correlating structure with non-linear optical properties in xAs₄₀Se₆₀·(1 - X)As₄₀S₆₀ glasses

A series of xAs40Se60·(100 − x)As40S60 glasses, where x = 0, 25, 33, 50, 67, 75 and 100 mol% As40Se60, has been studied using neutron and X-ray total scattering, Raman spectroscopy and 77Se MAS-NMR. The results are presented with measurements of non-linear refractive indices, n2, and densities. There is no evidence for the formation of homopolar bonds in these glasses, but neutron correlation functions suggest that there is a non-random distribution of sulfur and selenium atoms in sulfur-rich glasses. The average number of sulfur atoms at a distance of 3–4 Å from a selenium atom, nSeS, deviates from a linear variation with x in glasses containin

The 52 000 MW Ro/SS-A autoantigen in Sjögren's syndrome/systemic lupus erythematosus (Ro52) is an interferon-γ inducible tripartite motif protein associated with membrane proximal structures

The 52 000 MW Ro/SS-A (Ro52) protein is a major target of autoantibodies in autoimmune conditions such as systemic lupus erythematosus and Sjögren's syndrome. Recent genomic and bioinformatic studies have shown that Ro52 belongs to a large family of related RING/Bbox/coiled-coil (RBCC) tripartite motif proteins sharing overall domain structure and 40–50% identity at the amino acid level. Ro52 also has a B30.2 domain at the C-terminus. Using the human genome draft sequence, the genomic organization of the Ro52 gene on human chromosome 11p15.5 has been deduced and related to the protein domain structure. We show that the steady-state levels of Ro52 mRNA are normally very low but are induced by cell activation with interferon-γ. In transient transfection of HeLa cells, epitope-tagged Ro52 protein was localized to unidentified membrane proximal rod-like structures. Using in vitro coupled transcription/translation followed by immunoprecipitation, the autoimmune response to Ro52 protein was investigated and two distinct interactions were resolved. The Ro52 C-terminal B30.2 domain interacts with human immunoglobulin independently of antibody specificities. Sera derived from patients with Sjögren's syndrome and systemic lupus erythematosus, in addition, contained specific autoantibodies directed towards the rest of the Ro52 molecule. The majority of these autoimmune sera also immunoprecipitated the Ro52-related molecule RNF15. A possible role for Ro52 protein in alterations of plasma membranes during cellular activation or apoptosis is discussed