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Alterations of epidermal lectin binding sites in acute contact dermatitis *
Author(s) -
Wollina Uwe,
Fünfstück Veronika,
Hipler Christina,
Knopf Burkhard
Publication year - 1988
Publication title -
contact dermatitis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.524
H-Index - 96
eISSN - 1600-0536
pISSN - 0105-1873
DOI - 10.1111/j.1600-0536.1988.tb05506.x
Subject(s) - bullous pemphigoid , contact dermatitis , chemistry , lectin , pemphigus vulgaris , antigen , allergic contact dermatitis , epidermis (zoology) , immunology , dermatology , irritant contact dermatitis , pemphigus , pemphigoid , sialic acid , antibody , allergy , medicine , biochemistry , anatomy
We investigated alterations of epidermal lectin binding sues, as well as of pemphigus and bullous pemphigoid antigen in 28 human patch test reactions, both allergic (nickel, formaldehyde, N.N′‐1.3‐dimethylbutyl‐N′‐phenylenediamine) and irritant (sodium lauryl sulfate). The epidermal reactivity to a panel of lectins and human antisera to pemphigus vulgaris and bullous pemphigoid antigens was compared with samples obtained from normal skin and from skin under tape occlusion. We observed selective perturbations of lectin and antibody binding in acute contact dermatitis, whether allergic or irritant. The main findings were a loss of terminal sialic acids and longer bi‐ and triantennary mannosyl residues as well as a loss of pemphigus vulgaris antigen. The only difference between allergic and irritant patch test reactions was in topography of loss of WGA binding sites: in the former, it was most pronounced in the lower and middle epidermis, whereas in the latter it was seen in the uppermost subeorneal layers. Our findings support a common pathway of cell membrane alterations, of keratinocytes in acute contact dermatitis.