Fig 1: mRNA of SERPINC1 potentially generated by the gross deletion of exon 4 (A) and the 193 bp duplication involving exon 6 (B) with potential alternative splicing, two of them rendering normal RNA. Bold text is used to indicate each exon
Fig 2: Thrombophilic families carrying new SERPINC1 variants affecting N-glycosylation of Asn224. Clinical information, including type and age of the first thrombotic event (between brackets) and recurrence, functional values (anti-FXa activity), antigen levels, and molecular data (including the electropherogram of exon 4 in a symptomatic patient and a healthy control patient) are shown. Symbols half filled with red represent heterozygous subjects, and a red border indicates a patient who had a thrombotic event. The proband is pointed by an arrow. (A) p.Glu227Lys. Pedigree tree of the index French thrombophilic family. Thrombin generation data in available subjects are also shown. The c.679G>A (p.Glu227Lys) mutation is pointed by a red arrow. (B) p.Asn224His. Pedigree 3 of 2 unrelated Norwegian families. The c.670A>C (p.Asn224His) mutation is pointed by a red arrow. DVT, deep venous thrombosis; PVT, portal venous thrombosis; PE, pulmonary embolism; ND, not determined; AT Ag, antithrombin antigen; ETP, endogenous thrombin potential; OC, oral contraceptives; R, recurrence; F1, family 1; F2, family 2.
Fig 3: Comparative analysis of in silico predictions and molecular dynamics simulation for p.Arg445Serfs*17 variant versus WT AT.(A) Chromatograph (reverse sequence) detecting the gene variant in exon 7 of SERPINC1. The small deletion c.1332-1336delAAGAG is highlighted (arrow). (B) Nucleotide and primary sequence of p.Arg445Serfs*17 and WT AT. The nucleotide deletion and the aberrant C-terminal sequence are highlighted in red and yellow, respectively. Conserved Pro and Cys C-terminal residues are highlighted in red. (C and D) Graphic comparison of structures of p.Arg445Serfs*17 and WT AT through Swiss-Model and AlphaFold, visualized with UCSF Chimera (C), and molecular dynamics simulation (D). Note the similarities in C-terminal s4B-s5B segments, hydrogen-bond and disulfide-bond formation. Molecular dynamics simulation maximum time setup was 680 ns. C-term, C-terminus; MUT-AT, mutant antithrombin.
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