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.