Abstract
S100 protein, so called because of its solubility in 100% saturated ammonium sulphate1, is an acidic cytoplasmic protein specific for the nervous system2,3. It is localized primarily to glial elements of the brain, Schwann cells in the peripheral nervous system and satellite cells in sympathetic ganglia4,5. This brain-specific protein shows a close immunological relationship among a wide variety of vertebrates, as measured by a quantitative complement fixation technique6. Although strict serological conservation and tissue localization have been maintained among different species, no function for S100 protein has been determined. However, the appearance of S100 protein in brain is correlated with maturation of the nervous system in both rat and man7,8. Previous in vitro studies on the production and regulation of S100 protein in the C6 cell line derived from a rat astrocytoma indicated that cell contact and cessation of division induced S100 protein9. Neuroblastoma cell lines lack this protein10,11 although it is found in other astrocyte cell lines. We are unaware of any reports of cell lines, other than those of glial origin, which produce S100 protein. Melanocytes are derived from neuroectodermal elements, and this common origin of glial cells and melanocytes prompted us to study whether S100 protein might be present in cell lines from human malignant melanomas. We now report the presence of S100 protein in five of seven continuous cell lines of human malignant melanoma.
Published Version
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