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Article
September 1997

Immunohistochemical, Ultrastructural, and Molecular Features of Kindler Syndrome Distinguish It From Dystrophic Epidermolysis Bullosa

Author Affiliations

From the Departments of Dermatology, Keio University School of Medicine, Tokyo, Japan (Drs Shimizu, Sato, and Nishikawa), Gifu University School of Medicine, Gifu, Japan (Drs Ban and Kitajima), Tokyo Women's Medical College, Daini Hospital, Tokyo, Japan (Drs Ishizaki and Harada), University of Münster, Münster, Germany (Dr Bruckner-Tuderman), University of North Carolina School of Medicine, Chapel Hill (Dr Fine), and the Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown (Dr Burgeson), the Department of Dermatology and Cutaneous Biology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pa (Drs Kon, Christiano, and Uitto), and St John's Institute of Dermatology, St Thomas' Hospital, London, England (Dr McGrath).

Arch Dermatol. 1997;133(9):1111-1117. doi:10.1001/archderm.1997.03890450057007
Abstract

Background:  Kindler syndrome is a rare, inherited skin disease characterized by acral bullae formation, fusion of fingers and toes, and generalized progressive poikiloderma. The purpose of this study was to clarify the nature of the bullous component of Kindler syndrome and to determine whether this inherited skin disorder represents a variant of dystrophic epidermolysis bullosa or a unique independent clinical entity.

Observations:  Two unrelated patients with Kindler syndrome were studied. Electron microscopy demonstrated marked duplication of the lamina densa, and clefts were observed in areas where the lamina densa was destroyed or obscured. Hemidesmosomes and anchoring fibrils showed normal features. Indirect immunofluorescence revealed normal linear labeling with antibodies against hemidesmosomal components (α6 and β4 integrins, BPAG1, and BPAG2) and against anchoring filament components such as uncein, as detected by the 19-DEJ-1 monoclonal antibody. However, antibodies against the 3 respective laminin 5 chains, type IV collagen, and various type VII collagen epitopes (the aminoterminal NCI domain, the central triple helical collagenous domain, and the carboxyterminal end of the triple helical collagenous domain) revealed a broad reticular staining pattern. Molecular screening of the type VII collagen gene (COL7A1) in the patients and their parents by heteroduplex analysis failed to detect any bandshifts indicative of pathologic mutations.

Conclusions:  These results suggest that the bullous component of Kindler syndrome is distinct from dystrophic epidermolysis bullosa caused by mutations in the type VII collagen gene. Additionally, the differential distribution patterns of uncein and laminin 5 in the patients' skin samples support the hypothesis that uncein and laminin 5 are different molecules.Arch Dermatol. 1997;133:1111-1117

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