Acknowledgments
We would like to thank all patients and families for their willingness to take part in this study. We would like to thank Ms. Ghazale Mahjoub for her help in current paper and performing some relevant bioinformatics analysis.
Figure Legends
Figure 1: Family I. A) Patient I, pseudosyndactyly is clear in the photo B) Wound on elbow of the patient I which leads to squamous cell carcinoma. C) pedigree and sequence chromatograms. Both parents are heterozygous and the affected twin are homozygous for the identified glycine substitution mutation. D) Comparative amino acid alignment shows the conservation of amino acid glycine 1673 across distinct animal kingdoms. Symbols: (*) identical amino acids; (:) just similar amino acids.
Figure 2: Family II, A) patient III, Hand and neck wounds are clear in the picture. B) Pedigree and sequence chromatograms. Both parents are heterozygous for identified mutation. The mutation was confirmed in the proband as homozygous. The first pregnancy was homozygous and affected and the second one was carrier heterozygous and healthy. C) Comparative amino acid alignment shows the conservation of amino acid lysine 142 across distinct animal kingdoms. Symbols: (*) identical amino acids; (:) just similar amino acids.
Figure 3: A) Family III Pedigree and sequence chromatograms. The proband was homozygous for identified mutation and her parents and sister were carrier heterozygous of this mutation in COL7A1 gene. B) Family IV pedigree and sequence chromatograms. Both parents are heterozygous for splice site mutation in COL7A1 gene.
Figure 4: Family V, A) Pedigree and sequence chromatograms. Both parents didn’t reveal the mutation, while it was heterozygous in proband, which indicates the autosomal dominant inheritance. B) Comparative amino acid alignment shows the conservation of amino acid glycine 2034 across distinct animal kingdoms during evolution. Symbols: (*) identical amino acids; (:) just similar amino acids.