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. 2018 Jun 25;115(28):E6428–E6436. doi: 10.1073/pnas.1802977115

Fig. 1.

Fig. 1.

Identification of hereditary amyloidosis in proband II-4, which is linked to a TTR variant, Glu51_Ser52dup. (A) Family pedigree. Squares, males; circles, females; diagonal line, deceased members; black triangle, the proband. (B) Histological analyses. (Left) Congo red-positive amyloid deposits viewed by light microscopy in fat tissue. (Right) Polarized light view demonstrating apple-green birefringence of Congo red-positive amyloid deposits. (Magnification: Left and Right, 400×.) (C) Serum isoelectric focusing. Screening of serum from the proband (II-4) showed the presence of both WT and Glu51_Ser52dup variant proteins. Normal serum (Control) contained only the WT. (D) Genetic analyses. Partial sequence chromatograms of exon 3 of the TTR (Top), the subcloned WT allele (Middle), and the subcloned mutant allele (Bottom) are shown. A heterozygous duplication, c.212_217dupAGTCTG (red box), resulted in Glu51_Ser52dup protein variant. (E) Gene sequence alignment of the WT (wt; black) and mutant (red) TTR. The c.212_217dupAGTCTG duplication is underlined.