Immunoelectron microscopic analysis of in vivo interaction of basement membrane components using human skin lacking laminin 5.

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The epidermal basement membrane, an important structure to adhere the epidermis to the dermis, is consisted of many molecules. To clarify the in vivo interaction between these components gives a clue to elucidating the pathophysiology of skin bullous diseases showing blister formation in the epidermal basement membrane zone. In the present study, we employed post-embedding immunoelectron microscopy using human skin lacking laminin 332 (former laminin 5) to clarify the ultrastructural distribution of basement membrane components, including type XVII collagen. As a result, ultrastructural distribution of C-terminus of type XVII collagen in human skin lacking laminin 332 was different from that in normal human skin, indicating in vivo interaction between laminin 332 and type XVII collagen.