ペルオキシソーム増殖剤活性化受容体γ、ペルオキシソーム増殖因子活性化受容体γ、PPARγ、PPAR-γ

関: peroxisome proliferator-activated receptor gamma、PPARgamma

WordNet

a unit of magnetic field strength equal to one-hundred-thousandth of an oersted
the 3rd letter of the Greek alphabet
a herd of whales

PrepTutorEJDIC

ガンマ(ギリシア語アルファベットの第3字Γ,γ;英語のG,gに相当)
(特に女性の)魅力的な脚,すんなりした脚

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/11/01 22:18:51」(JST)

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[Wiki en表示]

Peroxisome proliferator-activated receptor gamma (PPAR-γ or PPARG), also known as the glitazone receptor, or NR1C3 (nuclear receptor subfamily 1, group C, member 3) is a type II nuclear receptor that in humans is encoded by the PPARG gene.^[5]^[6]^[7]

Tissue distribution

PPARG is mainly present in adipose tissue, colon and macrophages. Two isoforms of PPARG are detected in the human and in the mouse: PPAR-γ1 (found in nearly all tissues except muscle) and PPAR-γ2 (mostly found in adipose tissue and the intestine).^[8] ^[9]

Function

PPARG regulates fatty acid storage and glucose metabolism. The genes activated by PPARG stimulate lipid uptake and adipogenesis by fat cells. PPARG knockout mice fail to generate adipose tissue when fed a high-fat diet.^[10]

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. Four subtypes of PPARs are known: PPAR-alpha, PPAR-delta, PPAR-beta and PPAR-gamma. The protein encoded by this gene is PPAR-gamma and is a regulator of adipocyte differentiation. Alternatively spliced transcript variants that encode different isoforms have been described.^[11]

Many naturally occurring agents directly bind with and activate PPAR gamma. These agents include various polyunsaturated fatty acids like arachidonic acid and arachidonic acid metabolites such as certain members of the 5-Hydroxyicosatetraenoic acid and 5-oxo-eicosatetraenoic acid family, e.g. 5-oxo-15(S)-HETE and 5-oxo-ETE or 15-Hydroxyicosatetraenoic acid family including 15(S)-HETE, 15(R)-HETE, and 15(S)-HpETE.^[12]^[13]^[14] The activation of PPAR gamma by these and other ligands may be responsible for inhibiting the growth of cultured human breast, gastric, lung, prostate and other cancer cell lines.^[15]

Interactions

Peroxisome proliferator-activated receptor gamma has been shown to interact with:

EDF1^[16]^[17]^[18]
EP300^[19]^[20]
HDAC3^[19]^[21]
MED1^[20]
NCOA3^[20]
NCOA4^[22]
NCOA2^[20]
NR0B2^[23]
PPARGC1A^[24]^[25]
RB1.^[19]

Clinical relevance

PPAR-gamma has been implicated in the pathology of numerous diseases including obesity, diabetes, atherosclerosis, and cancer. PPAR-gamma agonists have been used in the treatment of hyperlipidaemia and hyperglycemia.^[26] PPAR-gamma decreases the inflammatory response of many cardiovascular cells, particularly endothelial cells.^[27] PPAR-gamma activates the PON1 gene, increasing synthesis and release of paraoxonase 1 from the liver, reducing atherosclerosis.^[28]

Many insulin sensitizing drugs (namely, the thiazolidinediones) used in the treatment of diabetes activate PPARG as a means to lower serum glucose without increasing pancreatic insulin secretion. Different classes of compounds which activate PPARgamma weaker than thiazolidinediones (the so-called “partial agonists of PPARgamma”) are currently studied with the hope that such compounds would be still effective hypoglycaemic agents but with fewer side effects.^[29]^[30] The medium-chain triglyceride decanoic acid has been shown to be a partially-activating PPAR-gamma ligand that does not increase adipogenesis.^[31]

A fusion protein of PPAR-γ1 and the thyroid transcription factor PAX8 is present in approximately one-third of follicular thyroid carcinomas, to be specific those cancers with a chromosomal translocation of t(2;3)(q13;p25), which permits juxtaposition of portions of both genes.^[32]^[33]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000132170 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000000440 - Ensembl, May 2017
^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Greene ME, Blumberg B, McBride OW, Yi HF, Kronquist K, Kwan K, Hsieh L, Greene G, Nimer SD (1995). "Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping". Gene Expr. 4 (4–5): 281–99. PMID 7787419.
^ Elbrecht A, Chen Y, Cullinan CA, Hayes N, Leibowitz MD, Moller DE, Berger J (July 1996). "Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2". Biochem. Biophys. Res. Commun. 224 (2): 431–7. PMID 8702406. doi:10.1006/bbrc.1996.1044.
^ Michalik L, Auwerx J, Berger JP, Chatterjee VK, Glass CK, Gonzalez FJ, Grimaldi PA, Kadowaki T, Lazar MA, O'Rahilly S, Palmer CN, Plutzky J, Reddy JK, Spiegelman BM, Staels B, Wahli W (December 2006). "International Union of Pharmacology. LXI. Peroxisome proliferator-activated receptors". Pharmacol. Rev. 58 (4): 726–41. PMID 17132851. doi:10.1124/pr.58.4.5.
^ Fajas L, Auboeuf D, Raspé E, Schoonjans K, Lefebvre AM, Saladin R, Najib J, Laville M, Fruchart JC, Deeb S, Vidal-Puig A, Flier J, Briggs MR, Staels B, Vidal H, Auwerx J (July 1997). "The organization, promoter analysis, and expression of the human PPARgamma gene". J. Biol. Chem. 272 (30): 18779–89. PMID 9228052. doi:10.1074/jbc.272.30.18779.
^ Park YK, Wang L, Giampietro A, Lai B, Lee JE, Ge K (January 2017). "Distinct Roles of Transcription Factors KLF4, Krox20, and Peroxisome Proliferator-Activated Receptor γ in Adipogenesis". Mol Cell Biol. 37 (2): 18779–89. PMID 27777310. doi:10.1128/MCB.00554-16.
^ Jones JR, Barrick C, Kim KA, Lindner J, Blondeau B, Fujimoto Y, Shiota M, Kesterson RA, Kahn BB, Magnuson MA (April 2005). "Deletion of PPARγ in adipose tissues of mice protects against high fat diet-induced obesity and insulin resistance". Proc. Natl. Acad. Sci. U.S.A. 102 (17): 6207–12. Bibcode:2005PNAS..102.6207J. PMC 556131 . PMID 15833818. doi:10.1073/pnas.0306743102.
^ "Entrez Gene: PPARG peroxisome proliferator-activated receptor gamma".
^ Dreyer C, Keller H, Mahfoudi A, Laudet V, Krey G, Wahli W (1993). "Positive regulation of the peroxisomal beta-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR)". Biol. Cell. 77 (1): 67–76. PMID 8390886. doi:10.1016/s0248-4900(05)80176-5.
^ O'Flaherty JT, Rogers LC, Paumi CM, Hantgan RR, Thomas LR, Clay CE, High K, Chen YQ, Willingham MC, Smitherman PK, Kute TE, Rao A, Cramer SD, Morrow CS (2005). "5-Oxo-ETE analogs and the proliferation of cancer cells". Biochim. Biophys. Acta. 1736 (3): 228–36. PMID 16154383. doi:10.1016/j.bbalip.2005.08.009.
^ Naruhn S, Meissner W, Adhikary T, Kaddatz K, Klein T, Watzer B, Müller-Brüsselbach S, Müller R (2010). "15-hydroxyeicosatetraenoic acid is a preferential peroxisome proliferator-activated receptor beta/delta agonist". Mol. Pharmacol. 77 (2): 171–84. PMID 19903832. doi:10.1124/mol.109.060541.
^ Krishnan A, Nair SA, Pillai MR (2007). "Biology of PPAR gamma in cancer: a critical review on existing lacunae". Curr. Mol. Med. 7 (6): 532–40. PMID 17896990. doi:10.2174/156652407781695765.
^ Brendel C, Gelman L, Auwerx J (June 2002). "Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism". Mol. Endocrinol. 16 (6): 1367–77. PMID 12040021. doi:10.1210/mend.16.6.0843.
^ Berger J, Patel HV, Woods J, Hayes NS, Parent SA, Clemas J, Leibowitz MD, Elbrecht A, Rachubinski RA, Capone JP, Moller DE (April 2000). "A PPARgamma mutant serves as a dominant negative inhibitor of PPAR signaling and is localized in the nucleus". Mol. Cell. Endocrinol. 162 (1–2): 57–67. PMID 10854698. doi:10.1016/S0303-7207(00)00211-2.
^ Gampe RT, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE (March 2000). "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors". Mol. Cell. 5 (3): 545–55. PMID 10882139. doi:10.1016/S1097-2765(00)80448-7.
^ ^a ^b ^c Fajas L, Egler V, Reiter R, Hansen J, Kristiansen K, Debril MB, Miard S, Auwerx J (December 2002). "The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation". Dev. Cell. 3 (6): 903–10. PMID 12479814. doi:10.1016/S1534-5807(02)00360-X.
^ ^a ^b ^c ^d Kodera Y, Takeyama K, Murayama A, Suzawa M, Masuhiro Y, Kato S (October 2000). "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators". J. Biol. Chem. 275 (43): 33201–4. PMID 10944516. doi:10.1074/jbc.C000517200.
^ Franco PJ, Li G, Wei LN (August 2003). "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Mol. Cell. Endocrinol. 206 (1–2): 1–12. PMID 12943985. doi:10.1016/S0303-7207(03)00254-5.
^ Heinlein CA, Ting HJ, Yeh S, Chang C (June 1999). "Identification of ARA70 as a ligand-enhanced coactivator for the peroxisome proliferator-activated receptor gamma". J. Biol. Chem. 274 (23): 16147–52. PMID 10347167. doi:10.1074/jbc.274.23.16147.
^ Nishizawa H, Yamagata K, Shimomura I, Takahashi M, Kuriyama H, Kishida K, Hotta K, Nagaretani H, Maeda N, Matsuda M, Kihara S, Nakamura T, Nishigori H, Tomura H, Moore DD, Takeda J, Funahashi T, Matsuzawa Y (January 2002). "Small heterodimer partner, an orphan nuclear receptor, augments peroxisome proliferator-activated receptor gamma transactivation". J. Biol. Chem. 277 (2): 1586–92. PMID 11696534. doi:10.1074/jbc.M104301200.
^ Wallberg AE, Yamamura S, Malik S, Spiegelman BM, Roeder RG (November 2003). "Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha". Mol. Cell. 12 (5): 1137–49. PMID 14636573. doi:10.1016/S1097-2765(03)00391-5.
^ Puigserver P, Adelmant G, Wu Z, Fan M, Xu J, O'Malley B, Spiegelman BM (November 1999). "Activation of PPARgamma coactivator-1 through transcription factor docking". Science. 286 (5443): 1368–71. PMID 10558993. doi:10.1126/science.286.5443.1368.
^ Li Y, Qi Y, Huang TH, Yamahara J, Roufogalis BD (January 2008). "Pomegranate flower: a unique traditional antidiabetic medicine with dual PPAR-alpha/-gamma activator properties". Diabetes Obes Metab. 10 (1): 10–7. PMID 18095947. doi:10.1111/j.1463-1326.2007.00708.x.
^ Hamblin M, Chang L, Fan Y, Zhang J, Chen YE (June 2009). "PPARs and the Cardiovascular System". Antioxid. Redox Signal. 11 (6): 1415–52. PMC 2737093 . PMID 19061437. doi:10.1089/ARS.2008.2280.
^ Khateeb J, Gantman A, Kreitenberg AJ, Aviram M, Fuhrman B (January 2010). "Paraoxonase 1 (PON1) expression in hepatocytes is upregulated by pomegranate polyphenols: a role for PPAR-gamma pathway". Atherosclerosis. 208 (1): 119–25. PMID 19783251. doi:10.1016/j.atherosclerosis.2009.08.051.
^ Atanasov AG, Wang JN, Gu SP, Bu J, Kramer MP, Baumgartner L, Fakhrudin N, Ladurner A, Malainer C, Vuorinen A, Noha SM, Schwaiger S, Rollinger JM, Schuster D, Stuppner H, Dirsch VM, Heiss EH (2013). "Honokiol: a non-adipogenic PPARγ agonist from nature". Biochim. Biophys. Acta. 1830 (10): 4813–9. PMC 3790966 . PMID 23811337. doi:10.1016/j.bbagen.2013.06.021.
^ Atanasov AG, Blunder M, Fakhrudin N, Liu X, Noha SM, Malainer C, Kramer MP, Cocic A, Kunert O, Schinkovitz A, Heiss EH, Schuster D, Dirsch VM, Bauer R (2013). "Polyacetylenes from Notopterygium incisum--new selective partial agonists of peroxisome proliferator-activated receptor-gamma". PLoS ONE. 8 (4): e61755. Bibcode:2013PLoSO...861755A. PMC 3632601 . PMID 23630612. doi:10.1371/journal.pone.0061755.
^ Malapaka RR, Khoo S, Zhang J, Choi JH, Zhou XE, Xu Y, Gong Y, Li J, Yong EL, Chalmers MJ, Chang L, Resau JH, Griffin PR, Chen YE, Xu HE (2012). "Identification and mechanism of 10-carbon fatty acid as modulating ligand of peroxisome proliferator-activated receptors". Journal of Biological Chemistry. 287 (1): 183–195. PMC 3249069 . PMID 22039047. doi:10.1074/jbc.M111.294785.
^ Kroll TG, Sarraf P, Pecciarini L, Chen CJ, Mueller E, Spiegelman BM, Fletcher JA (August 2000). "PAX8-PPARgamma1 fusion oncogene in human thyroid carcinoma [corrected]". Science. 289 (5483): 1357–60. Bibcode:2000Sci...289.1357K. PMID 10958784. doi:10.1126/science.289.5483.1357.
^ Mitchell RS, Kumar V, Abbas AK, Fausto N (2007). "20". Robbins Basic Pathology (8th ed.). Philadelphia: Saunders/Elsevier. ISBN 1-4160-2973-7.

UpToDate Contents

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1. 糖尿病の治療におけるチアゾリジン thiazolidinediones in the treatment of diabetes mellitus
2. 糖尿病性腎症の治療 treatment of diabetic nephropathy
3. 濾胞性甲状腺癌の概要 overview of follicular thyroid cancer
4. 甲状腺結節および非髄様甲状腺癌におけるオンコジーンおよび腫瘍抑制遺伝子 oncogenes and tumor suppressor genes in thyroid nodules and nonmedullary thyroid cancer
5. 糖尿病における心不全 heart failure in diabetes mellitus

English Journal

Effects of canola proteins and hydrolysates on adipogenic differentiation of C3H10T/2 mesenchymal stem cells.

Alashi AM1, Blanchard CL2, Mailer RJ3, Agboola SO4, Mawson AJ4, Aluko RE5, Strappe P2.
Food chemistry.Food Chem.2015 Oct 15;185:226-32. doi: 10.1016/j.foodchem.2015.03.054. Epub 2015 Mar 27.
This study assessed the ability of canola protein isolate (CPI) and enzymatic hydrolysates (CPHs) to inhibit adipogenic differentiation of C3H10T1/2 murine mesenchymal stem cells in vitro. Cell viability was maintained at concentrations of 60μg/ml of sample. Cells treated with Alcalase hydrolysate
PMID 25952862

Peroxisome proliferator-activated receptor γ enhances adiponectin secretion via up-regulating DsbA-L expression.

Jin D1, Sun J1, Huang J1, Yu X1, Yu A1, He Y1, Li Q1, Yang Z2.
Molecular and cellular endocrinology.Mol Cell Endocrinol.2015 Aug 15;411:97-104. doi: 10.1016/j.mce.2015.04.015. Epub 2015 Apr 24.
Disulfide-bond A oxidoreductase like-protein (DsbA-L) was identified as a molecular chaperone facilitating the assembly and secretion of adiponectin, an adipokine with multiple beneficial effects. In obesity the level of DsbA-L is reduced with a concomitant decrease of the circulating adiponectin le
PMID 25917454

Phytomolecule icaritin incorporated PLGA/TCP scaffold for steroid-associated osteonecrosis: Proof-of-concept for prevention of hip joint collapse in bipedal emus and mechanistic study in quadrupedal rabbits.

Qin L1, Yao D2, Zheng L2, Liu WC2, Liu Z2, Lei M3, Huang L2, Xie X2, Wang X4, Chen Y5, Yao X6, Peng J7, Gong H8, Griffith JF9, Huang Y10, Zheng Y10, Feng JQ11, Liu Y11, Chen S2, Xiao D3, Wang D5, Xiong J5, Pei D12, Zhang P13, Pan X14, Wang X15, Lee KM16, Cheng CY2.
Biomaterials.Biomaterials.2015 Aug;59:125-43. doi: 10.1016/j.biomaterials.2015.04.038. Epub 2015 May 15.
Steroid-associated osteonecrosis (SAON) may lead to joint collapse and subsequent joint replacement. Poly lactic-co-glycolic acid/tricalcium phosphate (P/T) scaffold providing sustained release of icaritin (a metabolite of Epimedium-derived flavonoids) was investigated as a bone defect filler after
PMID 25968462

Japanese Journal

The E3 ubiquitin ligase TRIM23 regulates adipocyte differentiation via stabilization of the adipogenic activator PPARγ

Watanabe Masashi,Takahashi Hidehisa,Saeki Yasushi,Ozaki Takashi,Itoh Shihori,Suzuki Masanobu,Mizushima Wataru,Tanaka Keiji,Hatakeyama Shigetsugu
Elife 4, e05615, 2015-04-23
… PPAR gamma is one of the late adipogenic activators and is known as a master regulator of adipogenesis. … However, the factors that regulate PPAR gamma expression remain to be elucidated. … Here, we show that a novel ubiquitin E3 ligase, tripartite motif protein 23 (TRIM23), stabilizes PPAR gamma protein and mediates atypical polyubiquitin conjugation. …
NAID 120005617283

Suppressive Effects of Irbesartan on Inflammation and Apoptosis in Atherosclerotic Plaques of apoE(-/-) Mice: Molecular Imaging with C-14-FDG and Tc-99m-Annexin A5

Zhao Yan,Watanabe Ayahisa,Zhao Songji,Kobayashi Tatsuo,Fukao Keita,Tanaka Yoshikazu,Nakano Toru,Yoshida Tetsuya,Takemoto Hiroshi,Tamaki Nagara,Kuge Yuji
Plos one 9(2), e89338, 2014-02-19
… Background: Irbesartan has a peroxisome proliferator-activated receptor gamma (PPAR gamma) activation property in addition to its ability to block the AT1 receptor. … PPAR gamma activation was observed in cells treated with irbesartan (134% +/- 36% at 3 mu M to 3329% +/- 218% at 81 mu M) by a PPAR gamma reporter assay system. …
NAID 120005427743

Reduction of PP2A C alpha stimulates adipogenesis by regulating the Wnt/GSK-3 beta/beta-catenin pathway and PPAR gamma expression

Okamura H,Yang D,Yoshida K,Teramachi J,Haneji T
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH 1843(11), 2376-2384, 2014
NAID 120005597290

「PPARγ」

PPARG
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1FM6, 1FM9, 1I7I, 1K74, 1KNU, 1NYX, 1PRG, 1RDT, 1WM0, 1ZEO, 1ZGY, 2ATH, 2F4B, 2FVJ, 2G0G, 2G0H, 2GTK, 2HFP, 2HWQ, 2HWR, 2I4J, 2I4P, 2I4Z, 2OM9, 2P4Y, 2POB, 2PRG, 2Q59, 2Q5P, 2Q5S, 2Q61, 2Q6R, 2Q6S, 2Q8S, 2QMV, 2VSR, 2VST, 2VV0, 2VV1, 2VV2, 2VV3, 2VV4, 2XKW, 2YFE, 2ZK0, 2ZK1, 2ZK2, 2ZK3, 2ZK4, 2ZK5, 2ZK6, 2ZNO, 2ZVT, 3ADS, 3ADT, 3ADU, 3ADV, 3ADW, 3ADX, 3AN3, 3AN4, 3B0Q, 3B0R, 3B1M, 3B3K, 3BC5, 3CDP, 3CDS, 3CS8, 3CWD, 3D6D, 3DZU, 3DZY, 3E00, 3ET0, 3ET3, 3FEJ, 3FUR, 3G9E, 3GBK, 3H0A, 3HO0, 3HOD, 3IA6, 3K8S, 3KMG, 3LMP, 3NOA, 3OSI, 3OSW, 3PBA, 3PO9, 3PRG, 3QT0, 3R5N, 3R8A, 3R8I, 3S9S, 3SZ1, 3T03, 3TY0, 3U9Q, 3V9T, 3V9V, 3V9Y, 3VJH, 3VJI, 3VN2, 3VSO, 3VSP, 3WJ4, 3WJ5, 3WMH, 3X1H, 3X1I, 4A4V, 4A4W, 4CI5, 4E4K, 4E4Q, 4EM9, 4EMA, 4F9M, 4FGY, 4HEE, 4JAZ, 4JL4, 4L96, 4L98, 4O8F, 4OJ4, 4PRG, 4PVU, 4PWL, 4R2U, 4R6S, 4XLD, 4R06, 4Y29, 4XTA, 4XUM, 4YT1, 4XUH, 5F9B, 5AZV
Identifiers
Aliases	PPARG, CIMT1, GLM1, NR1C3, PPARG1, PPARG2, PPARgamma, peroxisome proliferator activated receptor gamma
External IDs	MGI: 97747 HomoloGene: 7899 GeneCards: PPARG
Gene location (Human)
Chr.	Chromosome 3 (human)
End	12,434,356 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	115,490,399 bp
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• protein binding; • drug binding; • alpha-actinin binding; • activating transcription factor binding; • chromatin binding; • prostaglandin receptor activity; • core promoter sequence-specific DNA binding; • enzyme binding; • protein phosphatase binding; • metal ion binding; • arachidonic acid binding; • ligand-dependent nuclear receptor transcription coactivator activity; • steroid hormone receptor activity; • sequence-specific DNA binding; • identical protein binding; • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; • estrogen receptor binding; • transcription factor activity, sequence-specific DNA binding; • transcription regulatory region DNA binding; • DNA binding; • transcription factor binding; • double-stranded DNA binding; • protein C-terminus binding; • zinc ion binding; • peptide binding; • protein self-association; • retinoid X receptor binding; • protein heterodimerization activity; • DBD domain binding; • LBD domain binding;
Cellular component	• cytosol; • RNA polymerase II transcription factor complex; • perinuclear region of cytoplasm; • cytoplasm; • nucleus; • intracellular membrane-bounded organelle; • nucleoplasm; • protein complex;
Biological process	• negative regulation of cell proliferation; • epithelial cell differentiation; • negative regulation of smooth muscle cell proliferation; • positive regulation of oligodendrocyte differentiation; • transcription, DNA-templated; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • response to lipid; • negative regulation of receptor biosynthetic process; • placenta development; • cellular response to vitamin E; • negative regulation of interferon-gamma-mediated signaling pathway; • negative regulation of sequestering of triglyceride; • regulation of fat cell differentiation; • cellular response to retinoic acid; • glucose homeostasis; • negative regulation of collagen biosynthetic process; • cellular response to hyperoxia; • response to estrogen; • regulation of cholesterol transporter activity; • regulation of circadian rhythm; • negative regulation of telomerase activity; • signal transduction; • cellular response to insulin stimulus; • monocyte differentiation; • regulation of transcription from RNA polymerase II promoter; • regulation of blood pressure; • positive regulation of apoptotic process; • low-density lipoprotein particle receptor biosynthetic process; • positive regulation of fat cell differentiation; • negative regulation of cholesterol storage; • regulation of transcription, DNA-templated; • negative regulation of cell growth; • response to drug; • negative regulation of transcription, DNA-templated; • cellular response to prostaglandin stimulus; • animal organ regeneration; • positive regulation of sequence-specific DNA binding transcription factor activity; • lipoprotein transport; • response to metformin; • heart development; • response to cold; • negative regulation of acute inflammatory response; • fatty acid oxidation; • lipid homeostasis; • transcription initiation from RNA polymerase II promoter; • response to vitamin A; • innate immune response; • response to retinoic acid; • cell maturation; • cell fate commitment; • peroxisome proliferator activated receptor signaling pathway; • rhythmic process; • response to mechanical stimulus; • long-chain fatty acid transport; • lipid metabolic process; • response to low-density lipoprotein particle stimulus; • response to caffeine; • positive regulation of fatty acid oxidation; • response to immobilization stress; • positive regulation of phagocytosis, engulfment; • negative regulation of pancreatic stellate cell proliferation; • response to starvation; • response to organic cyclic compound; • regulation of transcription involved in cell fate commitment; • regulation of lipid metabolic process; • steroid hormone mediated signaling pathway; • response to organic substance; • response to nutrient; • cellular response to prostaglandin E stimulus; • negative regulation of transcription from RNA polymerase II promoter; • white fat cell differentiation; • negative regulation of macrophage derived foam cell differentiation; • positive regulation of transcription from RNA polymerase II promoter; • G-protein coupled receptor signaling pathway; • macrophage derived foam cell differentiation; • positive regulation of DNA binding; • positive regulation of transcription, DNA-templated; • intracellular receptor signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	5468
	19016
	ENSG00000132170
	ENSMUSG00000000440
	P37231
	P37238
NM_005037; NM_015869; NM_138711; NM_138712; NM_001330615;
	NM_001354666; NM_001354667; NM_001354668; NM_001354669; NM_001354670
	NM_001127330; NM_011146; NM_001308352; NM_001308354
NP_001317544; NP_005028; NP_056953; NP_619725; NP_619726;
	NP_001341595; NP_001341596; NP_001341597; NP_001341598; NP_001341599
	NP_001120802; NP_001295281; NP_001295283; NP_035276
	Wikidata
View/Edit Human	View/Edit Mouse

　　[★]

英: PPARgamma、PPAR-gamma
関: ペルオキシソーム増殖剤活性化受容体γ、ペルオキシソーム増殖因子活性化受容体γ、PPAR-γ

「PPAR-γ」

　　[★]

英

(n

PPAR-gamma

関: ペルオキシソーム増殖剤活性化受容体γ、ペルオキシソーム増殖因子活性化受容体γ、PPARγ

「ペルオキシソーム増殖剤活性化受容体γ」

　　[★]

英: peroxisome proliferator-activated receptor gamma、PPAR-gamma
関: ペルオキシソーム増殖因子活性化受容体γ、PPARγ、PPAR-γ

「ペルオキシソーム増殖因子活性化受容体γ」

　　[★]

英: PPAR-gamma
関: ペルオキシソーム増殖剤活性化受容体γ、PPARγ、PPAR-γ

「peroxisome proliferator-activated receptor gamma」

　　[★]

ペルオキシソーム増殖剤活性化受容体γ

関: PPAR-gamma、PPARgamma

「PPAR」

　　[★]

英: peroxisome proliferator-activated receptor
関: peroxisome proliferator activated receptor-7

転写因子。核内受容体。

PPARα

肝臓に多く発現して、脂肪酸の分解に関わる

PPARγ

脂肪細胞の分化を抑制し、脂肪貯蔵に関わる

「PP」

　　[★]

「PPA」

　　[★]

原発性進行性失語

関: primary progressive aphasia

同: pure pulmonary atresia

同: pure pulmonary atresia

「gamma」

　　[★] γ ガンマ　　　

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000132170 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000000440 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid7787419-5] Greene ME, Blumberg B, McBride OW, Yi HF, Kronquist K, Kwan K, Hsieh L, Greene G, Nimer SD (1995). "Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping". Gene Expr. 4 (4–5): 281–99. PMID 7787419.

[pmid8702406-6] Elbrecht A, Chen Y, Cullinan CA, Hayes N, Leibowitz MD, Moller DE, Berger J (July 1996). "Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2". Biochem. Biophys. Res. Commun. 224 (2): 431–7. PMID 8702406. doi:10.1006/bbrc.1996.1044.

[pmid17132851-7] Michalik L, Auwerx J, Berger JP, Chatterjee VK, Glass CK, Gonzalez FJ, Grimaldi PA, Kadowaki T, Lazar MA, O'Rahilly S, Palmer CN, Plutzky J, Reddy JK, Spiegelman BM, Staels B, Wahli W (December 2006). "International Union of Pharmacology. LXI. Peroxisome proliferator-activated receptors". Pharmacol. Rev. 58 (4): 726–41. PMID 17132851. doi:10.1124/pr.58.4.5.

[pmid9228052-8] Fajas L, Auboeuf D, Raspé E, Schoonjans K, Lefebvre AM, Saladin R, Najib J, Laville M, Fruchart JC, Deeb S, Vidal-Puig A, Flier J, Briggs MR, Staels B, Vidal H, Auwerx J (July 1997). "The organization, promoter analysis, and expression of the human PPARgamma gene". J. Biol. Chem. 272 (30): 18779–89. PMID 9228052. doi:10.1074/jbc.272.30.18779.

[pmid27777310-9] Park YK, Wang L, Giampietro A, Lai B, Lee JE, Ge K (January 2017). "Distinct Roles of Transcription Factors KLF4, Krox20, and Peroxisome Proliferator-Activated Receptor γ in Adipogenesis". Mol Cell Biol. 37 (2): 18779–89. PMID 27777310. doi:10.1128/MCB.00554-16.

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[entrez-11] "Entrez Gene: PPARG peroxisome proliferator-activated receptor gamma".

[pmid8390886-12] Dreyer C, Keller H, Mahfoudi A, Laudet V, Krey G, Wahli W (1993). "Positive regulation of the peroxisomal beta-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR)". Biol. Cell. 77 (1): 67–76. PMID 8390886. doi:10.1016/s0248-4900(05)80176-5.

[pmid16154383-13] O'Flaherty JT, Rogers LC, Paumi CM, Hantgan RR, Thomas LR, Clay CE, High K, Chen YQ, Willingham MC, Smitherman PK, Kute TE, Rao A, Cramer SD, Morrow CS (2005). "5-Oxo-ETE analogs and the proliferation of cancer cells". Biochim. Biophys. Acta. 1736 (3): 228–36. PMID 16154383. doi:10.1016/j.bbalip.2005.08.009.

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[pmid17896990-15] Krishnan A, Nair SA, Pillai MR (2007). "Biology of PPAR gamma in cancer: a critical review on existing lacunae". Curr. Mol. Med. 7 (6): 532–40. PMID 17896990. doi:10.2174/156652407781695765.

[pmid12040021-16] Brendel C, Gelman L, Auwerx J (June 2002). "Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism". Mol. Endocrinol. 16 (6): 1367–77. PMID 12040021. doi:10.1210/mend.16.6.0843.

[pmid10854698-17] Berger J, Patel HV, Woods J, Hayes NS, Parent SA, Clemas J, Leibowitz MD, Elbrecht A, Rachubinski RA, Capone JP, Moller DE (April 2000). "A PPARgamma mutant serves as a dominant negative inhibitor of PPAR signaling and is localized in the nucleus". Mol. Cell. Endocrinol. 162 (1–2): 57–67. PMID 10854698. doi:10.1016/S0303-7207(00)00211-2.

[pmid10882139-18] Gampe RT, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE (March 2000). "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors". Mol. Cell. 5 (3): 545–55. PMID 10882139. doi:10.1016/S1097-2765(00)80448-7.

[pmid12479814-19] Fajas L, Egler V, Reiter R, Hansen J, Kristiansen K, Debril MB, Miard S, Auwerx J (December 2002). "The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation". Dev. Cell. 3 (6): 903–10. PMID 12479814. doi:10.1016/S1534-5807(02)00360-X.

[pmid10944516-20] Kodera Y, Takeyama K, Murayama A, Suzawa M, Masuhiro Y, Kato S (October 2000). "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators". J. Biol. Chem. 275 (43): 33201–4. PMID 10944516. doi:10.1074/jbc.C000517200.

[pmid12943985-21] Franco PJ, Li G, Wei LN (August 2003). "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Mol. Cell. Endocrinol. 206 (1–2): 1–12. PMID 12943985. doi:10.1016/S0303-7207(03)00254-5.

[pmid10347167-22] Heinlein CA, Ting HJ, Yeh S, Chang C (June 1999). "Identification of ARA70 as a ligand-enhanced coactivator for the peroxisome proliferator-activated receptor gamma". J. Biol. Chem. 274 (23): 16147–52. PMID 10347167. doi:10.1074/jbc.274.23.16147.

[pmid11696534-23] Nishizawa H, Yamagata K, Shimomura I, Takahashi M, Kuriyama H, Kishida K, Hotta K, Nagaretani H, Maeda N, Matsuda M, Kihara S, Nakamura T, Nishigori H, Tomura H, Moore DD, Takeda J, Funahashi T, Matsuzawa Y (January 2002). "Small heterodimer partner, an orphan nuclear receptor, augments peroxisome proliferator-activated receptor gamma transactivation". J. Biol. Chem. 277 (2): 1586–92. PMID 11696534. doi:10.1074/jbc.M104301200.

[pmid14636573-24] Wallberg AE, Yamamura S, Malik S, Spiegelman BM, Roeder RG (November 2003). "Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha". Mol. Cell. 12 (5): 1137–49. PMID 14636573. doi:10.1016/S1097-2765(03)00391-5.

[pmid10558993-25] Puigserver P, Adelmant G, Wu Z, Fan M, Xu J, O'Malley B, Spiegelman BM (November 1999). "Activation of PPARgamma coactivator-1 through transcription factor docking". Science. 286 (5443): 1368–71. PMID 10558993. doi:10.1126/science.286.5443.1368.

[pmid18095947-26] Li Y, Qi Y, Huang TH, Yamahara J, Roufogalis BD (January 2008). "Pomegranate flower: a unique traditional antidiabetic medicine with dual PPAR-alpha/-gamma activator properties". Diabetes Obes Metab. 10 (1): 10–7. PMID 18095947. doi:10.1111/j.1463-1326.2007.00708.x.

[pmid19061437-27] Hamblin M, Chang L, Fan Y, Zhang J, Chen YE (June 2009). "PPARs and the Cardiovascular System". Antioxid. Redox Signal. 11 (6): 1415–52. PMC 2737093 . PMID 19061437. doi:10.1089/ARS.2008.2280.

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[pmid23811337-29] Atanasov AG, Wang JN, Gu SP, Bu J, Kramer MP, Baumgartner L, Fakhrudin N, Ladurner A, Malainer C, Vuorinen A, Noha SM, Schwaiger S, Rollinger JM, Schuster D, Stuppner H, Dirsch VM, Heiss EH (2013). "Honokiol: a non-adipogenic PPARγ agonist from nature". Biochim. Biophys. Acta. 1830 (10): 4813–9. PMC 3790966 . PMID 23811337. doi:10.1016/j.bbagen.2013.06.021.

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[pmid22039047-31] Malapaka RR, Khoo S, Zhang J, Choi JH, Zhou XE, Xu Y, Gong Y, Li J, Yong EL, Chalmers MJ, Chang L, Resau JH, Griffin PR, Chen YE, Xu HE (2012). "Identification and mechanism of 10-carbon fatty acid as modulating ligand of peroxisome proliferator-activated receptors". Journal of Biological Chemistry. 287 (1): 183–195. PMC 3249069 . PMID 22039047. doi:10.1074/jbc.M111.294785.

[pmid10958784-32] Kroll TG, Sarraf P, Pecciarini L, Chen CJ, Mueller E, Spiegelman BM, Fletcher JA (August 2000). "PAX8-PPARgamma1 fusion oncogene in human thyroid carcinoma [corrected]". Science. 289 (5483): 1357–60. Bibcode:2000Sci...289.1357K. PMID 10958784. doi:10.1126/science.289.5483.1357.

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v t e PPAR modulators
PPARα	Agonists: 15-HETE 15-HpETE Aleglitazar Aluminium clofibrate Arachidonic acid Bezafibrate Clofibrate CP-775146 Daidzein DHEA (prasterone) (in rodents) Elafibranor Etomoxir Fenofibrate Genistein Gemfibrozil GW-7647 Leukotriene B₄ LG-101506 LG-100754 Lobeglitazone Muraglitazar Oleylethanolamide Palmitoylethanolamide Pemafibrate Perfluorononanoic acid Perfluorooctanoic acid Pioglitazone Saroglitazar Sodelglitazar Tesaglitazar Tetradecylthioacetic acid Troglitazone WY-14643 Antagonists: GW-6471 MK-886
PPARδ	Agonists: 15-HETE 15-HpETE Arachidonic acid Bezafibrate Daidzein Elafibranor Fonadelpar Genistein GW-0742 GW-501516 L-165,041 LG-101506 MBX-8025 Sodelglitazar Tetradecylthioacetic acid Antagonists: FH-535 GSK-0660 GSK-3787
PPARγ	Agonists: 5-Oxo-ETE 5-Oxo-15-hydroxy-ETE 15-Deoxy-Δ^12,14-prostaglandin J₂ 15-HETE 15-HpETE Aleglitazar Arachidonic acid Balaglitazone Berberine Bezafibrate Cevoglitazar Ciglitazone Daidzein Darglitazone Edaglitazone Efatutazone Englitazone Etalocib Farglitazar Genistein GW-1929 Ibuprofen Imiglitazar Indeglitazar LG-100268 LG-100754 LG-101506 Lobeglitazone Muraglitazar (muroglitazar) nTZDpa Naveglitazar Netoglitazone Oxeglitazar Peliglitazar Pemaglitazar Perfluorononanoic acid Pioglitazone Prostaglandin J₂ Ragaglitazar Reglitazar Rivoglitazone Rosiglitazone RS5444 Saroglitazar Sipoglitazar Sodelglitazar Telmisartan Tesaglitazar Troglitazone SPPARMs: BADGE EPI-001 INT-131 MK-0533 S26948 Antagonists: FH-535 GW-9662 SR-202 T-0070907 Unknown: SR-1664
Non-selective	Agonists: Ciprofibrate Clinofibrate Clofibride Englitazone Etofibrate Farglitazar Netoglitazone Ronifibrate Rivoglitazone Simfibrate
Unsorted	Agonists: Lanifibranor Seladelpar
See also Receptor/signaling modulators Nuclear receptor modulators

リンク元	「PPARγ」「PPAR-γ」「ペルオキシソーム増殖剤活性化受容体γ」「ペルオキシソーム増殖因子活性化受容体γ」「peroxisome proliferator-activated receptor gamma」
関連記事	「PPAR」「PP」「PPA」「gamma」

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PPAR-gamma