Peroxisome proliferator-activated receptor gamma

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Peroxisome proliferator-activated receptor gamma (PPAR-gamma), also known as NR1C3 (nuclear receptor subfamily 1, group C, member 3) is a nuclear receptor encoded by the PPARG gene.

Peroxisome proliferator-activated receptor gamma
PDB rendering based on 1fm6.
Available structures: 1fm6, 1fm9, 1i7i, 1k74, 1knu, 1nyx, 1prg, 1rdt, 1wm0, 1zeo, 1zgy, 2ath, 2f4b, 2fvj, 2g0g, 2g0h, 2gtk, 2hfp, 2i4j, 2i4p, 2i4z, 2om9, 2prg, 3prg, 4prg
Identifiers
Symbol(s) PPARG; NR1C3; PPARG1; PPARG2
External IDs OMIM: 601487 MGI: 97747 HomoloGene: 7899
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5468 19016
Ensembl ENSG00000132170 ENSMUSG00000000440
Uniprot P37231 A0N0C8
Refseq NM_005037 (mRNA)
NP_005028 (protein)		 NM_011146 (mRNA)
NP_035276 (protein)
Location Chr 3: 12.3 - 12.45 Mb Chr 6: 115.39 - 115.46 Mb
Pubmed search [1] [2]

This gene encodes a member of the peroxisome proliferator-activated receptor (PPAR) subfamily of nuclear receptors. PPARs form heterodimers with retinoid X receptors (RXRs) and these heterodimers regulate transcription of various genes. Three subtypes of PPARs are known: PPAR-alpha, PPAR-delta, and PPAR-gamma. The protein encoded by this gene is PPAR-gamma and is a regulator of adipocyte differentiation. Additionally, PPAR-gamma has been implicated in the pathology of numerous diseases including obesity, diabetes, atherosclerosis and cancer. Alternatively spliced transcript variants that encode different isoforms have been described.[1]


[edit] References

  1. ^ Entrez Gene: PPARG peroxisome proliferator-activated receptor gamma.

[edit] Further reading

  • Qi C, Zhu Y, Reddy JK (2001). "Peroxisome proliferator-activated receptors, coactivators, and downstream targets.". Cell Biochem. Biophys. 32 Spring: 187–204. PMID 11330046. 
  • Kadowaki T, Hara K, Kubota N, et al. (2002). "The role of PPARgamma in high-fat diet-induced obesity and insulin resistance.". J. Diabetes Complicat. 16 (1): 41–5. PMID 11872365. 
  • Wakino S, Law RE, Hsueh WA (2002). "Vascular protective effects by activation of nuclear receptor PPARgamma.". J. Diabetes Complicat. 16 (1): 46–9. PMID 11872366. 
  • Takano H, Komuro I (2002). "Roles of peroxisome proliferator-activated receptor gamma in cardiovascular disease.". J. Diabetes Complicat. 16 (1): 108–14. PMID 11872377. 
  • Stumvoll M, Häring H (2002). "The peroxisome proliferator-activated receptor-gamma2 Pro12Ala polymorphism.". Diabetes 51 (8): 2341–7. PMID 12145143. 
  • Koeffler HP (2003). "Peroxisome proliferator-activated receptor gamma and cancers.". Clin. Cancer Res. 9 (1): 1–9. PMID 12538445. 
  • Puigserver P, Spiegelman BM (2003). "Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator.". Endocr. Rev. 24 (1): 78–90. PMID 12588810. 
  • Takano H, Hasegawa H, Nagai T, Komuro I (2003). "The role of PPARgamma-dependent pathway in the development of cardiac hypertrophy.". Drugs Today 39 (5): 347–57. PMID 12861348. 
  • Rangwala SM, Lazar MA (2004). "Peroxisome proliferator-activated receptor gamma in diabetes and metabolism.". Trends Pharmacol. Sci. 25 (6): 331–6. doi:10.1016/j.tips.2004.03.012. PMID 15165749. 
  • Cuzzocrea S (2005). "Peroxisome proliferator-activated receptors gamma ligands and ischemia and reperfusion injury.". Vascul. Pharmacol. 41 (6): 187–95. doi:10.1016/j.vph.2004.10.004. PMID 15653094. 
  • Savage DB (2007). "PPAR gamma as a metabolic regulator: insights from genomics and pharmacology.". Expert reviews in molecular medicine 7 (1): 1–16. doi:10.1017/S1462399405008793. PMID 15673477. 
  • Pégorier JP (2005). "[PPAR receptors and insulin sensitivity: new agonists in development]". Ann. Endocrinol. (Paris) 66 (2 Pt 2): 1S10–7. PMID 15959400. 
  • Tsai YS, Maeda N (2005). "PPARgamma: a critical determinant of body fat distribution in humans and mice.". Trends Cardiovasc. Med. 15 (3): 81–5. doi:10.1016/j.tcm.2005.04.002. PMID 16039966. 
  • Gurnell M (2006). "Peroxisome proliferator-activated receptor gamma and the regulation of adipocyte function: lessons from human genetic studies.". Best Pract. Res. Clin. Endocrinol. Metab. 19 (4): 501–23. doi:10.1016/j.beem.2005.10.001. PMID 16311214. 
  • Cecil JE, Watt P, Palmer CN, Hetherington M (2006). "Energy balance and food intake: the role of PPARgamma gene polymorphisms.". Physiol. Behav. 88 (3): 227–33. doi:10.1016/j.physbeh.2006.05.028. PMID 16777151. 
  • Rousseaux C, Desreumaux P (2007). "[The peroxisome-proliferator-activated gamma receptor and chronic inflammatory bowel disease (PPARgamma and IBD)]". J. Soc. Biol. 200 (2): 121–31. PMID 17151549. 
  • Eriksson JG (2007). "Gene polymorphisms, size at birth, and the development of hypertension and type 2 diabetes.". J. Nutr. 137 (4): 1063–5. PMID 17374678. 
  • Tönjes A, Stumvoll M (2007). "The role of the Pro12Ala polymorphism in peroxisome proliferator-activated receptor gamma in diabetes risk.". Current opinion in clinical nutrition and metabolic care 10 (4): 410–4. doi:10.1097/MCO.0b013e3281e389d9. PMID 17563457. 
  • Burgermeister E, Seger R (2007). "MAPK kinases as nucleo-cytoplasmic shuttles for PPARgamma.". Cell Cycle 6 (13): 1539–48. PMID 17611413. 
  • Papageorgiou E, Pitulis N, Msaouel P, et al. (2007). "The non-genomic crosstalk between PPAR-gamma ligands and ERK1/2 in cancer cell lines.". Expert Opin. Ther. Targets 11 (8): 1071–85. doi:10.1517/14728222.11.8.1071. PMID 17665979. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH)
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1
(1.3) bHLH-ZIP
MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4
GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)
(2.3) Cys2His2
ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6
(2.5) Alternating composition
AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B
(3) Helix-turn-helix
domains
ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1
(3.2) Paired box
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)
HSF (1, 2, 4)
(3.5) Tryptophan clusters
ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2
(3.6) TEA domain
transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)
(4.2) STAT
STAT (1, 2, 3, 4, 5, 6)
(4.3) p53
(4.4) MADS box
Mef2 (A, B, C, D) • SRF
HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1
(4.10) Cold-shock domain
(4.11) Runt
(0) Other
transcription factors
(0.2) HMGI(Y)
HMGA (1, 2) • HBP1
Rb • RBL1 • RBL2
(0.5) AP-2/EREBP-related factors
Apetala 2 • EREBP • B3
(0.6) Miscellaneous
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD