Macrophge에서 IL-1과 heat shock protein의 상관관계 = Interaction of IL-1 and heat shock proteins on macrophage

다국어 초록 (Multilingual Abstract)

The macrophage plays an important role in lipopolysaccharide (LPS)-induced fever. Fever formation is attributed to macrophage activity. The purpose of this study is to examine whether induced fever has the charateristics of self-restriction during the process of a fever response. The result of methy-[^(3)H]-thymidine incorporation in RAW 246.7 cells showed that the proliferation of the macrohage was suppressed by a heat load of 39℃ for 2 hr. Enzyme-linked immunosorbent assay (ELISA) showed that the activity of IL-1 secretion induced by LPS was also suppressed by heat load. Suppression of activities of the macrophage including proliferation and secretion suggest that negative feedback loops exist where the end product, heat, may act back on the macrophage and finally result in the subsiding of a fever. The induction of heat shock protein (hsp70) by heat shock in the macrophage was detected by Western blot and Northern blot analysis. In U-937 cells, the increase of hsp70 band appears to be related to the extent of inhibition of IL-1 secretion. It is assumed that IL-1 secretion from the macrophage which effects the induction of fever, has a close relationship to the induction of hsp70.