The interaction of cells with extracellular matrix components plays a significant role in the regulation of cell biology. Laminin is a large glycoprotein involved in fundamental interactions between cells and the basement membrane. Several cell surface receptors are responsible for cell-matrix interactions. The 67 kDa high affinity laminin receptor, 67LR, is involved in the adhesion of normal cells to the laminin network and is also associated with the metastatic phenotype of some tumoral cells. We have investigated the expression of laminin and of the 67LR in normal human skin using immunoperoxidase staining. Twenty samples of skin were analyzed. Antibody against laminin reacted in a continuous linear band at the dermal-epidermal junction, as well as basement membranes of hair follicles, sebaceous and eccrine sweat glands, and dermal blood vessels. The epidermis and the follicular epithelium were negative for laminin. The 67LR seemed not to be expressed on the basal surface of basal keratinocytes. The major expression of this receptor may be detected in the upper half of the spinous layer and in the granular layer. The cells of the outer root sheath in hair follicle showed the same immunohistochemical pattern described for epidermis. In sebaceous glands and in eccrine sweat glands the secreting epithelium was positive. Endothelial cells of dermal blood vessels were routinely positive for 67LR. We observed that the expression of the 67LR in normal human skin is mostly located in epidermal areas in which the keratinizing process was particularly advanced.The interaction of cells with extracellular matrix components plays a significant role in the regulation of cell morphology, growth and differentiation and contributes to the pathogenesis of cancer (1). Extracellular matrix organization is particularly complex at the interface between histologically dissimilar tissues that originate from different primary germ layers. In this area the so-called basement membrane is formed (2).The skin basement membrane zone is among the most complex basement membranes of the human body (3). Several macromolecules have been identified within the basement membrane zone. Among these laminin is a ubiquitous, large glycoprotein with a molecular weight of approximately 900 kDa. It is composed of three genetically different subunits, named A, B I and B2 in the classical form, which assemble into a cruciform structure with one long arm and three short arms (4-5).Laminin is thought to form a major basement membrane network located in the lamina lucida (6) and to be involved in important interactions between cells and basement membrane (7). Epidermal cells and extracellular matrix proteins interact through specific receptors of the cellular surface. To date, severallaminin binding proteins have been identified (8). The high affinity laminin receptor, molecular weight 67 kDa, was the first laminin receptor to be identified in 1983 (9-11).This receptor is physiologically expressed by a large variety of cells and seems to be involved in the a...