Peroxisome proliferator-activated receptors (PPARs): Novel therapeutic targets in renal disease  YouFei Guan, M.D., Ph.D., Matthew D. Breyer  Kidney International  Volume 60, Issue 1, Pages 14-30 (July 2001) DOI: 10.1046/j.1523-1755.2001.00766.x Copyright © 2001 International Society of Nephrology Terms and Conditions

Figure 1 (A) Structural and functional domains of the human peroxisome proliferator-activated receptors (PPARs). Domains are: A/B, N-terminal A/B domain containing a ligand-independent activation function (AF-1); C, DNA-binding domain (DBD); D, hinge region; and E/F, C-terminal ligand-binding domain (LBD) containing the ligand-dependent activation function (AF-2). Numbers inside the boxes represent the percentage (%) identity between the human PPAR isofoms. (B) The genomic organization of the human PPARγ gene. Alternative promoter usage and splicing of the three 5′ exons A1, A2, and B results in three different transcripts and two PPARγ protein products (PPARγ1 and PPARγ2). Note that transcription from the promoter γ1 and γ3 results in same protein of 477 amino acids (PPARγ1protein) and transcript using the promoter γ2 encoded a protein of 505 amino acids (PPARγ2 protein), which has additional 28 amino acids at the N-terminus compared with PPARγ1 protein. Kidney International 2001 60, 14-30DOI: (10.1046/j.1523-1755.2001.00766.x) Copyright © 2001 International Society of Nephrology Terms and Conditions

Figure 2 Model for gene activation and repression by PPARγ. Kidney International 2001 60, 14-30DOI: (10.1046/j.1523-1755.2001.00766.x) Copyright © 2001 International Society of Nephrology Terms and Conditions