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The location of binding sites of pemphigus vulgaris and pemphigus foliaceus autoantibodies: a post‐embedding immunoelectron microscopic study
Author(s) -
ZHOU S.,
FERGUSON D.J.P.,
ALLEN J.,
WOJNAROWSKA F.
Publication year - 1997
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 - 10.1046/j.1365-2133.1997.01823.x
Subject(s) - pemphigus foliaceus , pemphigus vulgaris , immunoelectron microscopy , pemphigus , autoantibody , dermatology , medicine , pathology , immunology , immunohistochemistry , antibody
Summary Pemphigus is a life‐threatening autommune blistering discase of skin and mucous membranes that has two major subtypes based on clinical and histolgical features, pemphigus vulgaris (PV) and pemphigus foliaceus (PF). Autoantibodies against the PV antigen (desmoglein 3) and the PF antigen (desmoglein 1) are involved in the pathogenesis of blister formation. In the present study, the location of epitopes recognized by autoantibodies of patients with PV and PF was studied by postembedding immunogold electron microscopy. PV and PF autoantibodies were observed bound predominantly to the intercellular domains of desmosomes, but not to the non‐desmosomal keratinocyte cell surface. The relationship between the location of PF antigen and other constitutive desmosomal proteins. desmocollin, desmoplakin and plakoglobin, in normal human skin was investigated using a double immunogold labelling techinique. It was observed that PF antigen and desmocollin co‐localize within the intercellular domain of the desmosomes. In contrast, the antibodies against desmoplakin and plakoglobin bound predominantly to the intracellular desmosomal attachment plaque with the binding site of the antibody against plakoglobin closer to the desmosomal cell membrane than that of the antibody to desmoplakin. We show that the LR White postembedded immunogold electronmicroscopy technique is convenient and easily applied to studied to studies of autoimmune bullous skin diseases. We have used it to demonstrated the precise localization of the binding sites of PV and PF autoantibodies and their reltionship with other constitutive desmosomal proteins.