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GIORNALE ITALIANO DI DERMATOLOGIA E VENEREOLOGIA

A Journal on Dermatology and Sexually Transmitted Diseases


Official Journal of the Italian Society of Dermatology and Sexually Transmitted Diseases
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Giornale Italiano di Dermatologia e Venereologia 2004 October;139(5):377-87

Copyright © 2004 EDIZIONI MINERVA MEDICA

language: English

The human desmosomal cadherins: structure, function and role in disease

Whittock N. V. 1, Bower C. 2

1 Institute of Biomedical and Clinical Science Peninsula Medical School, Exeter, UK 2 Department of Dermatology Royal Devon and Exeter Hospital, Exeter, UK


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The desmogleins along with the desmocollins comprise the desmosomal cadherins and the extracellular domains of these proteins make up the extracellular core domain of the desmosome. There are currently 7 known human desmosomal cadherins, namely desmocollins 1-3 and desmogleins 1-4, that are expressed in a differentiation and tissue specific manner and provide the sticky adhesion of the desmosome required between adjacent cells. The desmosomal cadherin genes are located in a cluster on 18q12 and their transcripts encode precursor proteins that are cleaved to yield a mature protein. Within the desmosome the extracellular domain of the desmosomal cadherins is essential for calcium dependent heterophilic/homophilic binding to desmosomal cadherins on adjacent cells, whereas the intracellular domain is essential for binding to the proteins of the desmosomal plaque such as plakoglobin. The desmosomal cadherins have been implicated in several human diseases. Mutations in desmogleins 1 and 4 lead to autosomal dominant striate palmoplantar keratoderma, and localized autosomal recessive hypotrichosis, respectively, whereas autoantibodies and strains of Staphylococcus aureus target their extracellular domains in the aquired bullous disorders, pemphigus and staphylococcal scalded skin syndrome. Therefore, intact and functionally active desmosomal cadherins are essential to epidermal integrity. Here, we review the expression, cloning and genetics, protein structure, and molecular interactions of the human desmosomal cadherins and outline the role they play within the desmosome and how it becomes defective in human disease.

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