Abstract: |
Six cell surface glycoproteins defined by monoclonal antibodies were selected for study on human epidermal cells. In tests on tissue sections, three of the glycoproteins [ J143 (gp 140 30); T43 (gp 85 36); H99 (gp38)] were expressed in the basal cell layer of the epidermis, whereas the other three glycoproteins [T179 (gp 140 95); T16 (gp 40 50); BT15 (gp80)] were preferentially expressed in maturing keratinocytes above the basal layer. We compared synthesis of these glycoproteins in fresh epidermis and in primary epidermal short term cultures using [35S]methionine for metabolic labeling. Synthesis of J143 was 8- to 20-fold higher and synthesis of T43 was 4- to 10-fold lower in cultured cells compared with fresh epidermis. BT15, an antigen strongly expressed on terminally differentiating keratinocytes, was synthesized at 5- to 15-fold higher levels in fresh epidermis than in cultured cells. Biosynthesis levels of H99, T179, and T16 did not change in cultured epidermal cells. Based on our findings, we propose a model of surface antigenic changes that occur during keratinocyte differentiation in vivo. © 1987. |
Keywords: |
immunohistochemistry; adult; human cell; cytology; cells, cultured; epidermis; membrane proteins; cell differentiation; keratinocyte; monoclonal antibody; gene expression regulation; antibodies, monoclonal; glycoproteins; glycoprotein; normal human; human; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; support, u.s. gov't, non-p.h.s.
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