Low molecular weight proteins secreted by peritoneal macrophages obtained from 2,3,7,8-tetrabromodibenzo-p-dioxin-treated NMRI mice.

The protein secretion patterns in a macrophage-like cell line (CBrD), established from the peritoneal cells of NMRI mice treated with the dioxin analog 2,3,7,8-tetrabromodibenzo-p-dioxin (TBrDD), were analyzed by high resolution two-dimensional gel electrophoresis (2-D PAGE), and compared to the pattern of proteins secreted by control macrophages which were intraperitoneally activated by bacterial lipopolysaccharide. The most striking alterations were observed in the low molecular range. The transformed cells encode a number of low molecular mass proteins (10-20 kDa) which were not detected in control cells under identical experimental conditions. The protein pattern with respect to isoelectric point, molecular weight, optical density (OD) and area of the spot (in mm2) has been depicted by computer analysis in relation to a standardized spot outline and the spot's background (in OD). It is concluded that the transformation of murine peritoneal macrophages by TBrDD leads to an upregulation of proteins, in particular of low-molecular-weight proteins.