Patient and healthy subject characteristics.

<p>p-values, when shown in italics such as <i>p<0.01</i>, indicate that there are significant differences. Values are shown as mean ± SD (standard deviation). BMI; Body Mass Index, AST; Aspartate transaminase, ALT; Alanine transaminase, CHO; cholesterol, TG; triglyceride.</p

Scatter plots of serum total TG, VLDL-TG, non-VLDL-TG levels, and VLDL-TG/non-VLDL-TG ratios.

<p>P-values are indicated as the values between groups with bars. The mean value of each group is indicated at the bottom of each diagram. P-values, when indicated in bold with an asterisk (such as <b>0.025*)</b>, indicate significant differences. SD; standard deviation.</p

Kaplan–Meier survival curves of rats with tracheal stenosis.

<p>At the start of the study, 10 untreated rats and nine FIR-SeV/ΔF-treated rats were included. A survival analysis was performed using the log-rank test. The FIR-SeV/ΔF-treated animals (solid line) displayed a significantly higher survival rate than the untreated control animals (dotted line) five days following the scraping of the tracheal mucosa. *<i>P</i> < 0.05 using the log-rank test.</p

Additional file 1: Table S1. of A novel KCNQ1 nonsense variant in the isoform-specific first exon causes both jervell and Lange-Nielsen syndrome 1 and long QT syndrome 1: a case report

The proband’s (II-2 in Fig. 2) results of genetic screening of LQT causative genes (KCNQ1, KCNH2, SCN5A, KCNE1, KCNE2, KCNJ2, SCN4B, KCNJ5). Entire coding exons, including the intronic boundaries of the genes were analyzed. (XLSX 10 kb

Quantitative analysis of tracheal stenosis.

<p>The percentage of stenosis five days following tracheal scraping was calculated using the following formula: (1 − the area of the mucosal surface lumen (solid line)/the area of the tracheal cartilage lumen (dotted line)) × 100 (<b>a</b>). The animals in which FIR-SeV/ΔF was administered (black) displayed a significantly lower percentage of stenosis than the untreated controls (white) (<b>b</b>). The results are expressed as the mean + SEM (bars). *P < 0.05 using the Mann–Whitney U test.</p

Representative H&E-stained axial sections of the rat trachea five days following the scraping of the tracheal mucosa.

<p>The untreated controls (tracheal scraping only (n = 10)), (<b>a, c</b>) showed both hyperplasia of the airway epithelium and a thickened submucosal layer with extensive fibrosis, angiogenesis, and collagen deposition causing lumen stenosis. The FIR-SeV/ΔF-treated animals, in which FIR-SeV/ΔF was administered into the tracheal mucosa following tracheal scraping (n = 9), (<b>b, d</b>), showed a reduction in the extent of hyperplasia of the tracheal epithelium. The scale bar in (<b>a, b</b>) and (<b>c, d</b>) indicates 500 μm and 100 μm, respectively.</p

Serotyping in heterozygous combinations.

<p>Figure shows representative ion chromatograms of the wild-type (E3/E3) and all heterozygous combinations (E2/E3, E3/E4, E2/E4). Tryptic peptide polymorphisms correspond to each ApoE isoform. As described under “ApoE serotyping” in the <b>Materials and Methods</b>, the correlation between ApoE genotypes and isoforms enables determination of the genotype from the blood ApoE isoform combination.</p

Apolipoprotein E resequencing and its application to serotyping.

<p>(<b>A</b>) ApoE resequencing. Figure shows a representative result of wild-type ApoE amino acid sequence determination (sequence coverage = 93.6%, excluding the 18-residue signal peptide) using Orbitrap LC-MS/MS. Black highlighting denotes the determined sequence. Amino acid residues C112 and R158, which demonstrate polymorphism in ApoE2 (C158) and ApoE4 (R112), are circled. Amino acids are represented by their one-letter codes. (<b>B</b>) Tryptic peptide polymorphisms and ion chromatograms. Mutations in amino acid residues 112 and 158, which were covered by protein resequencing, cause peptide fragment polymorphisms. The R158C mutation (ApoE2) results in the cLAVYQAGAR peptide, where the C112R mutation (ApoE4) yields the LGADMEDVR peptide. Figure shows representative chromatograms for the doubly charged ions extracted from subjects with E2/E3 and E3/E4 heterozygous combinations. The calculated and observed monoisotopic masses for each peptide are indicated. (<b>C</b>) Corresponding MS/MS spectra for each peptide in (<b>B</b>). Polymorphic peptide sequences from subjects with heterozygous combinations were confirmed by MS/MS. The b- and y-ions are labeled. In (<b>B</b>) and (<b>C</b>), lower-case “c” represents alkylated cysteine residues. C. mass = calculated mass; O. mass = observed mass; Da = dalton.</p