関: PPAR-gamma、PPARgamma

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aerate (sewage) so as to favor the growth of organisms that decompose organic matter (同)aerate
make (substances) radioactive
make active or more active; "activate an old file"
make more adsorptive; "activate a metal"
rendered active; e.g. rendered radioactive or luminescent or photosensitive or conductive
(of e.g. a molecule) made reactive or more reactive (同)excited
(military) set up and placed on active assignment; "a newly activated unit"
(of sewage) treated with aeration and bacteria to aid decomposition
a unit of magnetic field strength equal to one-hundred-thousandth of an oersted
the 3rd letter of the Greek alphabet
a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response
a herd of whales

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…'を'活動的にする / …‘に'放射能を与える / 〈物質〉'を'活性化する
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)
=sense organ / 受信装置
(特に女性の)魅力的な脚,すんなりした脚

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/01 07:44:30」(JST)

wiki en

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.^[2]^[3]^[4]

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).^[5]

Function[edit]

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.^[6]

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. Alternatively spliced transcript variants that encode different isoforms have been described.^[7]

Interactions[edit]

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

EDF1^[8]^[9]^[10]
EP300^[11]^[12]
HDAC3^[11]^[13]
MED1^[12]
NCOA3^[12]
NCOA4^[14]
NCOA2^[12]
NR0B2^[15]
PPARGC1A^[16]^[17]
RB1.^[11]

Clinical relevance[edit]

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.^[18] PPAR-gamma decreases the inflammatory response of many cardiovascular cells, particularly endothelial cells.^[19] PPAR-gamma activates the PON1 gene, increasing synthesis and release of paraoxonase 1 from the liver, reducing atherosclerosis.^[20]

Many insulin sensitizing drugs (namely, the thiazolidinediones) used in the treatment of diabetes target 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.^[21]^[22]

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.^[23] ^[24]

Recently pioglitazone, a PPAR-γ agonist has been shown to be effective in reducing inflammation in Parkinson's Disease models. Levels of MMPs and microglia (and therefore TNF-α and other cytokine levels) were found to be reduced. Thus it has been shown to be neuroprotective in MPTP mouse models.

References[edit]

^ Chandra, V.; Huang, P.; Hamuro, Y.; Raghuram, S.; Wang, Y.; Burris, T. P.; Rastinejad, F. (2008). "Structure of the intact PPAR-γ–RXR-α nuclear receptor complex on DNA". Nature 456 (7220): 350–356. doi:10.1038/nature07413. PMC 2743566. PMID 19043829. edit
^ 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 M, 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. doi:10.1006/bbrc.1996.1044. PMID 8702406. Cite uses deprecated parameters (help)
^ 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. doi:10.1124/pr.58.4.5. PMID 17132851. Cite uses deprecated parameters (help)
^ 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. doi:10.1074/jbc.272.30.18779. PMID 9228052. Cite uses deprecated parameters (help)
^ 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. doi:10.1073/pnas.0306743102. PMC 556131. PMID 15833818. Cite uses deprecated parameters (help)
^ "Entrez Gene: PPARG peroxisome proliferator-activated receptor gamma".
^ 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. doi:10.1210/me.16.6.1367. PMID 12040021. Cite uses deprecated parameters (help)
^ 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. doi:10.1016/S0303-7207(00)00211-2. PMID 10854698. Cite uses deprecated parameters (help)
^ 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. doi:10.1016/S1097-2765(00)80448-7. PMID 10882139. Cite uses deprecated parameters (help)
^ ^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. doi:10.1016/S1534-5807(02)00360-X. PMID 12479814. Cite uses deprecated parameters (help)
^ ^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. doi:10.1074/jbc.C000517200. PMID 10944516. Cite uses deprecated parameters (help)
^ 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. doi:10.1016/S0303-7207(03)00254-5. PMID 12943985. Cite uses deprecated parameters (help)
^ 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. doi:10.1074/jbc.274.23.16147. PMID 10347167. Cite uses deprecated parameters (help)
^ 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. doi:10.1074/jbc.M104301200. PMID 11696534. Cite uses deprecated parameters (help)
^ 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. doi:10.1016/S1097-2765(03)00391-5. PMID 14636573. Cite uses deprecated parameters (help)
^ 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. doi:10.1126/science.286.5443.1368. PMID 10558993. Cite uses deprecated parameters (help)
^ 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. doi:10.1111/j.1463-1326.2007.00708.x. PMID 18095947. Cite uses deprecated parameters (help)
^ Hamblin M, Chang L, Fan Y, Zhang J, Chen YE (June 2009). "PPARs and the Cardiovascular System". Antioxid. Redox Signal. 11 (6): 1415–52. doi:10.1089/ARS.2008.2280. PMC 2737093. PMID 19061437. Cite uses deprecated parameters (help)
^ 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. doi:10.1016/j.atherosclerosis.2009.08.051. PMID 19783251. Cite uses deprecated parameters (help)
^ 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. Honokiol: A non-adipogenic PPARγ agonist from nature. Biochim Biophys Acta. 2013 Oct;1830(10):4813-9. doi:10.1016/j.bbagen.2013.06.021. Epub 2013 Jun 27. PubMed PMID 23811337. http://www.ncbi.nlm.nih.gov/pubmed/23811337
^ 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. Polyacetylenes from Notopterygium incisum - new selective partial agonists of peroxisome proliferator-activated receptor-gamma. PLoS One. 2013 Apr22;8(4):e61755. doi: 10.1371/journal.pone.0061755. Print 2013. PubMed PMID 23630612; PubMed Central PMCID: PMC3632601. http://www.ncbi.nlm.nih.gov/pubmed/23630612
^ Kroll, TG; et al. (25 August 2000). "PAX8-PPARγ1 Fusion in Oncogene Human Thyroid Carcinoma". Science 28 (5483): 1357–1360. doi:10.1126/science.289.5483.1357. Retrieved 8 December 2010. Cite uses deprecated parameters (help)
^ Chapter 20 in: Mitchell, Richard Sheppard; Kumar, Vinay; Abbas, Abul K.; Fausto, Nelson. Robbins Basic Pathology. Philadelphia: Saunders. ISBN 1-4160-2973-7. 8th edition.

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. 濾胞性甲状腺癌の概要 overview of follicular thyroid cancer
3. 糖尿病性腎症の治療 treatment of diabetic nephropathy
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

Broiler chicken adipose tissue dynamics during the first two weeks post-hatch.

Bai S1, Wang G2, Zhang W2, Zhang S2, Rice BB2, Cline MA2, Gilbert ER3.
Comparative biochemistry and physiology. Part A, Molecular & integrative physiology.Comp Biochem Physiol A Mol Integr Physiol.2015 Nov;189:115-23. doi: 10.1016/j.cbpa.2015.08.002. Epub 2015 Aug 8.
Selection of broiler chickens for growth has led to increased adipose tissue accretion. To investigate the post-hatch development of adipose tissue, the abdominal, clavicular, and subcutaneous adipose tissue depots were collected from broiler chicks at 4 and 14days post-hatch. As a percent of body w
PMID 26263851

Tectorigenin regulates adipogenic differentiation and adipocytokines secretion via PPARγ and IKK/NF-κB signaling.

Li QY1, Chen L, Yan MM, Shi XJ, Zhong MK.
Pharmaceutical biology.Pharm Biol.2015 Nov;53(11):1567-75. doi: 10.3109/13880209.2014.993038. Epub 2015 Apr 9.
CONTEXT: Obesity is associated with a number of diseases with metabolic abnormalities such as type 2 diabetes (T2D).OBJECTIVE: We investigate the effects of tectorigenin on 3T3-L1 preadipocyte differentiation and adipocytokines secretion.MATERIALS AND METHODS: The effects of tectorigenin on adipocyt
PMID 25856699

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 60 μg/ml of sample. Cells treated with Alcalase hydrolysate
PMID 25952862

Japanese Journal

The Effect of Sex Hormones on Peroxisome Proliferator-Activated Receptor Gamma Expression and Activity in Mature Adipocytes

Sato Hiromi,Sugai Hana,Kurosaki Hiroshi [他]
Biological & pharmaceutical bulletin 36(4), 564-573, 2013-04
NAID 40019621272

Effects of Structural and Electronic Characteristics of Chalcones on the Activation of Peroxisome Proliferator-Activated Receptor Gamma

Schott Jason Taylor,Mordaunt Charles Edward,Vargas Anthony Joseph [他]
Chemical and pharmaceutical bulletin 61(2), 229-236, 2013-02
NAID 40019558736

Mechanisms of lifespan extension and preventive effects of calorie restriction on tumor development: Possible link between central neuroendocrine system and peripheral metabolic adaptation

Chiba Takuya,Dong Kesu,Nishizono Shoko,Shimokawa Isao
The Journal of Physical Fitness and Sports Medicine 2(3), 259-266, 2013
… On the other hand, possible peripheral regulators of the beneficial effects of CR involve a transcriptional regulator complex, the hepatocyte nuclear factor 4α/peroxisome proliferator-activated receptor gamma coactivator 1-α (HNF-4α/PGC-1α) complex. …
NAID 130003379966

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★リンクテーブル★

リンク元	「PPAR-gamma」「ペルオキシソーム増殖剤活性化受容体γ」
関連記事	「activated」「activate」「peroxisome proliferator」「proliferator」「gamma」

「PPAR-gamma」

Peroxisome proliferator-activated receptor gamma
	; PPAR-G dimer bound to DNA. PDB rendering based on 3e00.
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, 4A4V, 4A4W, 4E4K, 4E4Q, 4EM9, 4EMA, 4F9M, 4FGY, 4HEE, 4PRG
Identifiers
Symbols	PPARG; CIMT1; GLM1; NR1C3; PPARG1; PPARG2; PPARgamma
External IDs	OMIM: 601487 MGI: 97747 HomoloGene: 7899 IUPHAR: NR1C3 ChEMBL: 235 GeneCards: PPARG Gene
Gene Ontology
Molecular function	• RNA polymerase II regulatory region DNA binding; • DNA binding; • chromatin binding; • sequence-specific DNA binding transcription factor activity; • steroid hormone receptor activity; • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity; • prostaglandin receptor activity; • protein binding; • drug binding; • zinc ion binding; • enzyme binding; • ligand-dependent nuclear receptor transcription coactivator activity; • activating transcription factor binding; • sequence-specific DNA binding; • transcription regulatory region DNA binding; • retinoid X receptor binding; • arachidonic acid binding;
Cellular component	• nucleus; • nucleoplasm; • cytosol;
Biological process	• negative regulation of transcription from RNA polymerase II promoter; • placenta development; • negative regulation of acute inflammatory response; • transcription initiation from RNA polymerase II promoter; • lipid metabolic process; • induction of apoptosis; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • signal transduction; • heart development; • response to nutrient; • regulation of blood pressure; • response to cold; • gene expression; • negative regulation of macrophage derived foam cell differentiation; • negative regulation of receptor biosynthetic process; • negative regulation of cholesterol storage; • negative regulation of sequestering of triglyceride; • long-chain fatty acid transport; • fatty acid oxidation; • monocyte differentiation; • negative regulation of cell growth; • epithelial cell differentiation; • response to caffeine; • organ regeneration; • response to retinoic acid; • cellular response to insulin stimulus; • response to vitamin A; • response to lipid; • peroxisome proliferator activated receptor signaling pathway; • response to drug; • glucose homeostasis; • lipoprotein transport; • response to estrogen stimulus; • innate immune response; • cell fate commitment; • positive regulation of fat cell differentiation; • low-density lipoprotein particle receptor biosynthetic process; • negative regulation of transcription, DNA-dependent; • positive regulation of transcription, DNA-dependent; • positive regulation of transcription from RNA polymerase II promoter; • positive regulation of fatty acid oxidation; • cell maturation; • negative regulation of smooth muscle cell proliferation; • positive regulation of oligodendrocyte differentiation; • white fat cell differentiation; • brown fat cell differentiation; • positive regulation of sequence-specific DNA binding transcription factor activity; • negative regulation of telomerase activity; • lipid homeostasis; • response to low-density lipoprotein particle stimulus; • negative regulation of interferon-gamma-mediated signaling pathway; • regulation of cholesterol transporter activity; • cellular response to lithium ion;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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