Kidney and vascular function in adult patients with hereditary fructose intolerance.

Objective: Previous studies have shown that patients with hereditary fructose intolerance (HFI) are characterized by a greater intrahepatic triglyceride content, despite a fructose-restricted diet. The present study aimed to examine the long-term consequences of HFI on other aldolase-B-expressing organs, i.e. the kidney and vascular endothelium. Methods: Fifteen adult HFI patients were compared to healthy control individuals matched for age, sex and body mass index. Aortic stiffness was assessed by carotid-femoral pulse wave velocity (cf-PWV) and endothelial function by peripheral arterial tonometry, skin laser doppler flowmetry and the endothelial function biomarkers soluble E-selectin [sE-selectin] and von Willebrand factor. Serum creatinine and cystatin C were measured to estimate the glomerular filtration rate (eGFR). Urinary glucose and amino acid excretion and the ratio of tubular maximum reabsorption of phosphate to GFR (TmP/GFR) were determined as measures of proximal tubular function. Results: Median systolic blood pressure was significantly higher in HFI patients (127 versus 122 mmHg, p = .045). Pulse pressure and cf-PWV did not differ between the groups (p = .37 and p = .49, respectively). Of all endothelial function markers, only sE-selectin was significantly higher in HFI patients (p = .004). eGFR was significantly higher in HFI patients than healthy controls (119 versus 104 ml/min/1.73m2, p = .001, respectively). All measurements of proximal tubular function did not differ significantly between the groups. Conclusions: Adult HFI patients treated with a fructose-restricted diet are characterized by a higher sE-selectin level and slightly higher systolic blood pressure, which in time could contribute to a greater cardiovascular risk. The exact cause and, hence, clinical consequences of the higher eGFR in HFI patients, deserves further study.

Facile synthesis of copper(II)-decorated functional mesoporous material for specific adsorption of histidine-rich proteins.

The Cu2+-decorated functional mesoporous material was fabricated by thermally initiated free-radical polymerization of octavinyl polyhedral oligomeric silsesquioxane. It was used as adsorbent for highly specific separation of histidine (His)-rich proteins in blood and cell lysate based on immobilized metal affinity chromatography. The functional mesoporous material (named as PPOSS-IDA-Cu2+) was characterized in detail and its selectivity and binding capacity were evaluated using a His-rich protein (bovine hemoglobin, BHb) and other proteins (bovine serum albumin, myoglobin, lysozyme and horseradish peroxidase) containing fewer surface-exposed His residues as model proteins. The results indicated that PPOSS-IDA-Cu2+ exhibited large specific surface area and good selective adsorption ability and the maximum adsorption capacity for BHb was 3150mgg-1. Moreover, PPOSS-IDA-Cu2+ had excellent recyclability and the adsorption capacity of the reused material for BHb remained almost unchanged after six cycles. In addition, PPOSS-IDA-Cu2+ not only showed excellent performance for the removal of highly abundant hemoglobin in human blood, but also can be a good adsorbent for the enrichment of proteins in cell lysate. It was the first time to explore the application of Cu2+-decorated functional material as an adsorbant for the separation of proteins in cell lysate. This approach can be combined with other techniques which can remove or deplete highly abundant proteins from real biological samples to obtain more comprehensive data about low abundant His-rich proteins in proteomic analysis.

Know your fish: A novel compound-specific isotope approach for tracing wild and farmed salmon.

The rapid expansion of the aquaculture industry with carnivorous fish such as salmon has been accompanied by an equally rapid development in alternative feed ingredients. This has outpaced the ability of prevailing authentication method to trace the diet and origins of salmon products at the retail end. To close this gap, we developed a new profiling tool based on amino acid δ13C fingerprints. With this tool, we discriminated with high-accuracy among wild-caught, organically, and conventionally farmed salmon groups, as well as salmon fed alternative diets such as insects and macroalgae. Substitution of fishmeal with macroalgae was detected at 5% difference level. The δ13C fingerprints of essential amino acids appear particularly well suited for tracing protein sources, and the non-essentials for tracing lipid origins (terrestrial vs. aquatic). In an industry constantly developing new feed proteins and functional additives, our method is a promising tool for tracing salmon and other seafood products.