Keratinocytes synthesize basal-lamina proteins in culture.

On histologic vertical sections of skin, the epidermis is separated from the dermis by an amorphous thin membrane, the basal lamina. Ultrastructurally, the basal lamina is composed of four areas, including the basal-cell plasma membrane and hemidesmosomes, the lamina lucida, the lamina densa, and the sub-lamina densa fibrillar region. In culture, epidermal keratinocytes are able to produce hemidesmosomes, lamina lucida, and lamina densa. There is no evidence that cultured keratinocytes can produce sub-lamina densa fibrils. Biochemically, the lamina lucida contains two major glycoproteins. One, the bullous pemphigoid antigen, is synthesized by epidermal keratinocytes in vitro. These cells also synthesize laminin, the other glycoprotein of lamina lucida. At the interface between lamina lucida and lamina densa there is probably a heparan sulfate proteoglycan. Whether this proteoglycan is produced by keratinocytes in culture is not known, but the possibility can be considered. Lamina densa contains collagen IV, and this collagen is synthesized by keratinocytes in culture. However, cultured keratinocytes may also synthesize collagen types I, III, and V. Type V is associated with the basal lamina, but its exact location is unknown. Types I and III (if they are produced in vivo) would be situated in the sub-basal lamina region. The problem of fibronectin remains unsolved. There is "some" fibronectin in the lamina lucida, but its origin is not clear.