Abstract
The aim of this study is to localize the α 2 laminin chain in normal human skin. The methods used were immuno-gold cytochemistry on cryo-ultramicrotomy sections and thin-section-fracture-label, together with electron microscopy observation. Results were compared with light microscopy peroxidase immuno-staining. Both normal skin samples and skin biopsies from laminin α 2 chain deficient congenital muscular dystrophy affected patients were studied. The results show that, in normal skin, the laminin α 2 chain is spread throughout the cytoplasm of basal keratinocytes, while it appears associated with desmosomal tonofilaments in the spinous and granular epidermal layers; in skin samples from dystrophic patients the laminin α 2 chain was not detectable. These data suggest that the function of the laminin α 2 chain is different in that epidermis as compared to that in muscle and peripheral nerve, where it is localized in the basement membrane.
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