Human gingival fibroblast production of interferon

• Published in: Journal of dental research Vol. 63; no. 12; p. 1369
• Main Authors: Rose, G G, Pinero, G J, O'Neill, P A, Nikai, H, Mahan, C J
• Format: Journal Article
• Language: English
• Published: United States 01-12-1984
• Subjects: Adult; Carcinoma, Squamous Cell - pathology; Carcinoma, Squamous Cell - ultrastructure; Cell Division - drug effects; Cell Line; Culture Media; Cycloheximide - pharmacology; Cytoplasm - ultrastructure; Dactinomycin - pharmacology; Fibroblasts - cytology; Fibroblasts - metabolism; Gingiva - cytology; Humans; Interferon Inducers - pharmacology; Interferons - biosynthesis; Interferons - pharmacology; Mouth Neoplasms - pathology; Mouth Neoplasms - ultrastructure
• ISSN: 0022-0345
• DOI: 10.1177/00220345840630120601

Three human gingival fibroblast cell lines were used to determine whether they could be induced by a synthetic RNA and superinduced by metabolic inhibitors to produce interferon (IFN-beta). When established procedures were followed for human fetal or newborn skin fibroblast cell lines, the adult gingival fibroblasts produced comparable amounts of IFN-beta. It was shown that the superinducers alone would not cause an IFN-beta production response, and that the absence of serum in the production medium also inhibited the production of IFN-beta. The effect of IFN-beta on cell growth was carried out in T-flasks seeded with 10(5) HEp-2 cells. After one and two wk, the cells of triplicate control flasks and triplicate flasks containing various dilutions of the production media were enumerated to determine a cell multiplication inhibition (CMI) value. A correlation between the IFN-beta content and the CMI effect, however, was not obtained, and it was concluded that other CMI agents, possibly more potent than the IFN-beta, were being produced by the stimulated human gingival fibroblasts. Cell protein assays which gave a high ng/cell protein content correlated with TEM micrographs which showed clusters of complex lysosomes, primarily in cells cultured in the IFN-beta-containing nutrient. However, since commercial IFN-beta initiated no such lysosomal response, it was further concluded that the complex lysosomes were due to CMI agent(s) other than IFN-beta.