Peroxisome proliferator-activated receptor gamma

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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

Symbols

PPARG; NR1C3; PPARG1; PPARG2

External IDs

OMIM: 601487 MGI: 97747 HomoloGene: 7899

Gene ontology
Molecular function:	• transcription factor activity • steroid hormone receptor activity • protein binding • zinc ion binding • transcription activator activity • transcription repressor activity • sequence-specific DNA binding • metal ion binding
Cellular component:	• nucleus • cytosol
Biological process:	• negative regulation of transcription from RNA polymerase II promoter • generation of precursor metabolites and energy • transcription • regulation of transcription, DNA-dependent • lipid metabolic process • signal transduction • response to nutrient • epithelial cell differentiation • cell fate commitment • regulation of fat cell differentiation • positive regulation of transcription • positive regulation of transcription from RNA polymerase II promoter • white fat cell differentiation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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]

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.

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]

References

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

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.

This article on a gene on chromosome 3 is a stub. You can help Wikipedia by expanding it.

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	AP-4 • MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.4) NF-1	NFIC

(1.5) RF-X	NFX1

(1.6) Basic helix-span-helix (bHSH)	AP-2 (α, β, γ, δ, ε)

(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 (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ)) 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) • TRPS1

(2.3) Cys₂His₂	General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2)) ATBF1 • BCL (6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • GFI1 • GLI-Krüppel family (1, 2, 3, S2, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 17 ) • MTF1 • MYT1 • OSR1 • SP (1, 2, 4, 7) • Zbtb7 (7A, 7B) • ZBTB (16, 17, 20, 32, 33, 40) • 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, 423, 451, 452, 471, 593, 638, 649, 655)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix domains

(3.1) Homeo domain	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, 2-2, 2-3, 2-5, 3-1, 3-2) • PBX (1, 2, 3) • PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) • PITX (1, 2, 3) • POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2, SPIB) • 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	p53 • TBX (1, 2, 3, 5, 19, 21, 22)

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.6) TATA binding proteins	TBP • TBPL1

(4.7) High mobility group	HMGB (1, 2, 3) • HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21) • SRY • SSRP1 • TOX (1, 2, 3, 4)

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	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

Wikipedia content modification information:

This page was last modified on 15 July 2008, at 16:14.

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