Melanocytes freshly isolated from normal human skin express the cell membrane receptor for the adhesive glycoprotein thrombospondin.

Thrombospondin (TSP) is an adhesive protein with multiple binding sites, which is able to mediate several cell-to-cell and cell-to-matrix interactions, particularly through its cell membrane receptor (TSP-R). Because human keratinocytes are able to synthesize and express TSP, and as TSP is also localized at the dermal-epidermal junction in normal human skin, we questioned whether epidermal cells are able to bind available TSP, that is, to express TSP-R. To investigate this, we employed gold immunoelectron microscopy on epidermal cells freshly isolated from normal human skin; the TSP-R was detected by OKM5 monoclonal antibody. Epidermal cells showing ultrastructural characteristics of melanocytes were gold-stained on their plasma membrane, whereas keratinocytes, Langerhans cells and lymphocytes were unstained. Although functional studies are clearly necessary to clarify the role(s) played by the TSP-R on the cell surface of melanocytes, it is tempting to speculate that the TSP-R may be important for melanocyte adhesion to the dermal-epidermal junction and to keratinocytes. Such adhesion may not only subserve the steric localization of melanocytes, but also have important implications for those functional activities of melanocytes which have been shown to require close contact between these cells and adjacent keratinocytes and/or basement membrane components.