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Contains fulltext : 292432.pdf (Publisher’s version ) (Open Access) BACKGROUND: The population-based colorectal cancer (CRC) screening program in individuals aged 55 to 75 years in the Netherlands uses fecal immunochemical testing (FIT), to detect hemoglobin in feces, followed by colonoscopy in individuals with a positive FIT. OBJECTIVES: The objectives of this study are to assess the false-positive rate, detection rate, and positive predictive value of FIT for CRC and advanced adenoma (AA) in patients with Von Willebrand disease (VWD) or hemophilia. METHODS: We performed a multicenter, nationwide cross-sectional study embedded in 2 nationwide studies on VWD and hemophilia in the Netherlands. RESULTS: In total, 493 patients with hemophilia (n = 329) or VWD (n = 164) were included, of whom 351 patients participated in the CRC screening program (71.2%). FIT positivity and false-positive rate in patients with hemophilia and VWD were significantly higher than those in the general population (14.8% vs. 4.3%, p < .001 and 10.3% vs. 2.3%, p

Additional file 1: Figure S1. Detailed description of the position of the samples in the phatom in the different batches scanned. Percentages correspond to the blood percentage in the sample. a) First batch scanned at all field strenghts. b) Second batch scanned at all field strengths. c) Third batch scanned at 3T. Figure S2. (A) Signal intensity in the ROI vs IR delays for the 0% blood tube at 3T: the experimental data are indicated with blue ��� and the fitting with a red line. (B) Analysis of the residuals: each ��� represents the residual of each experimental data point from the one predicted with the fitting. The mean of the residual is also reported as dotted line. Figure S3. T2 mapping at 1.5T with different echo spacing on dependence on the blood concentration. Figure S4. T2 mapping at 1.5T (A) and 3 T (B) with a multi-slice accelerated scans and single slice non accelerated scans.

Fibrinogen has a principal role in blood clot formation. It is a soluble protein that is converted to fibrin and polymerizes into insoluble fibrin fibres forming a clot-stabilizing network. This is further strengthened by activated factor XIII (FXIIIa) via cross-linking and incorporation of α2-antiplasmin and thrombin activatable fibrinolysis inhibitor (TAFI). Fibrinogen is synthesized in hepatocytes and composed of three pairs of different polypeptide chains (Aα, Bβ, γ), interconnected via disulphide bridges. Each chain is encoded by a single gene (FGA, FGB and FGG). In congenital dysfibrinogenaemia, a qualitative defect is caused by mutations within any of these genes. According to the online database of dysfibrinogenaemias, 1,215 cases are reported at present: 626 with a defect in the Aα chain, 154 in the Bβ chain, and 435 in the γ chain.[1] The clinical spectrum of this disorder is heterogeneous: 26% of the patients have a bleeding tendency, 21% of the patients have a thrombotic tendency, and 53% of the patients are asymptomatic.[2] [3] [4] Dysfibrinogenaemia can thus lead to both bleeding and thrombosis, illustrating the versatile functions of fibrinogen in coagulation. Furthermore, fibrinogen is important for wound healing. The fibrin network serves as a provisional scaffold at the site of injury and supports cell proliferation and migration.[5] This role of fibri(noge)n in tissue repair is illustrated by the use of fibrin sealants to promote wound healing,[6] although this fibrin concentration is much higher than in physiological conditions. Delayed wound healing and/or wound dehiscence is a clinical feature in FXIII deficiency due to decreased cross-linking of fibrin and decreased linking to other proteins.[7] Surprisingly, impaired wound healing is not a well-known feature in congenital dysfibrinogenaemia. We here report a case of severely impaired wound healing in a man with dysfibrinogenemia due to fibrinogen Longmont, a heterozygous dysfibrinogenaemia causing impaired polymerization.