Binding of 125I-gamma interferon to cultured human keratinocytes.
Gamma interferon (IFN-gamma), a product of activated lymphocytes, influences keratinocyte proliferation and differentiation. Recombinant gamma interferon (r-IFN-gamma) was radioiodinated using the Bolton-Hunter reagent and retained 90% of its biologic activity as determined by induction of HLA-DR expression. The biochemical ligand-binding properties of iodinated IFN-gamma to cultured human keratinocytes revealed a plateau of binding at 150 min at 4 degrees C, and a single class of specific high affinity receptors (kD = 1.3 X 10(-10) M; 2200 sites/cell). The binding of human IFN-gamma, to keratinocytes was inhibited by human r-IFN-gamma, but not by either murine recombinant gamma interferon or human recombinant beta interferon (r-IFN-beta). The presence of high affinity receptor sites on human keratinocytes assures the reception of appropriate immunologic signals in lymphocyte-keratinocyte interactions.
D002478:Cells, Cultured; D000078404:Epidermal Cells; D004817:Epidermis / Q000276:immunology*; D006684:HLA-DR Antigens / Q000032:analysis; D006801:Humans; D007371:Interferon-gamma / Q000378:metabolism*; D007633:Keratins; D007700:Kinetics; D008970:Molecular Weight; D011869:Radioligand Assay; D011971:Receptors, Immunologic / Q000378:metabolism*; D017471:Receptors, Interferon; D011994:Recombinant Proteins / Q000378:metabolism
D006684:HLA-DR Antigens; D011971:Receptors, Immunologic; D017471:Receptors, Interferon; D011994:Recombinant Proteins; D007633:Keratins; D007371:Interferon-gamma