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The distribution of α6β4 integrins in lesional and non‐lesional skin in bullous pemphigoid
Author(s) -
VENNING V.A.,
ALLEN J.,
APLIN J.D.,
KIRTSCHIG G.,
WOJNAROWSKA F.
Publication year - 1992
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/j.1365-2133.1992.tb08040.x
Subject(s) - hemidesmosome , bullous pemphigoid , integrin , laminin , basement membrane , blisters , type iv collagen , antigen , immunofluorescence , chemistry , pathology , beta (programming language) , keratinocyte , immunohistochemistry , antibody , medicine , microbiology and biotechnology , biology , immunology , extracellular matrix , receptor , biochemistry , in vitro , computer science , programming language
Summary The α6β4 integrin is associated ultrastructurally with the hemidesmosomes of the basal keratinocytes and with the bullous pemphigoid antigen (BPA), suggesting an important role in adhesion of epidermal cells to the basement membrane. Using an immunofluorescence technique with chainspecific monoclonal antibodies to the α and β subunits we have investigated the distribution of the α6β4 integrin in normal skin ( n =3) and in BP skin (uninvolved, perilesional and lesional) [ n =11]). The findings have been compared with other types of subepidermal blisters and with normal skin split by chemical means ( n =2) and by suction ( n =2). The distribution of α6β4 integrin was compared with that of bullous pemphigoid antigen (BPA) and with other basement membrane zone (BMZ) macromolecules, laminin, collagen type IV, collagen type VII and the BM600 antigen. In uninvolved, perilesional and early pre‐blistered lesional BP skin the distribution of both the α6 and β4 integrin subunits, BPA laminin, collagen types IV and VII and the BM600 antigen was identical to normal skin, i.e. a linear band in the BMZ. Within BP blisters, both α6 and β4 integrin subunits and BPA were absent, except in two blisters in which the integrin expression was retained in the blister roof, despite loss of BPA. The other BMZ components were expressed on the blister floor. These findings distinguished BP from linear IgA disease (patchy retention of α6β4 integrin expression along the blister roof and floor, with BPA expressed in the roof), and from blisters of the dermolytic type (recessive dystrophic epidermolysis bullosa and eosinophilic cellulites) in which all the BMZ components, including α6β4 integrin and BPA were expressed along the blister roof. In artificially split skin, α6β4 integrin and BPA were expressed along the roof of the split, whereas the other BMZ components were expressed along the floor. We conclude that although there is no widespread abnormality of α6β4 integrin expression in uninvolved BP skin, nor in early pre‐blistered lesions, loss of expression of both α6β4 integrin and BPA is a feature of most fully developed BP blisters, and is specific for BP compared with other types of subepidermal blisters. Disruption of the hemidesmosomerelated antigens appears be a prerequisite for blistering to occur in BP.