Experiments were designed to clarify the role of several proteins, junB, retinoblastoma protein (RB), and the transforming growth factor- (TGF-) receptors that are potential intermediates in TGF- activation of the 2(I) collagen promoter. Treatment of NIH-3T3 cells with TGF- increased the activity of a transiently transfected murine 2(I) collagen promoter (nucleotides -350 to +54) fused to a luciferase reporter gene 9-fold. Co-transfection of a junB stimulated the basal activity of the 2(I) collagen promoter 93-fold, respectively. Expression of antisense junB RNA attenuated the effect of TGF-. Simian virus 40 large T antigen, an inhibitor RB function, did not prevent TGF- effects on the 2(I) collagen promoter. A chimeric receptor containing the extracellular domain of the colony-stimulating factor-1 receptor and the intracellular domain of the type I TGF- receptor enhanced 2(I) collagen promoter activity 4.8-fold, whereas a similar chimera containing the type II receptor intracellular domain had much weaker effects. Similar results were obtained with a plasminogen activator inhibitor-1 promoter, previously shown to be activated by TGF- through AP-1 elements. We conclude that TGF- activates the 2(I) collagen and plasminogen activator inhibitor-1 promoters in NIH-3T3 cells through junB and the type I TGF- receptor kinase domain.

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