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PPARG (Peroxisome proliferator-activated receptor gamma) is a protein that switches other genes on and off. The public catalogues list it as a drug target, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Colorectal cancer, Thyroid cancer and Endometrial cancer.
Ligand-activated transcription factor that forms obligate heterodimers with the retinoic acid receptor and acts as a key regulator of biological processes, such as adipocyte differentiation, lipid metabolism, glucose homeostasis and beta-oxidation of fatty acids. Activated by lipid ligands: binds peroxisome proliferators, such as hypolipidemic drugs, and fatty acids, such as prostaglandin J2 metabolites. Ligand-binding results in a conformational change in the receptor, promoting dissociation of repressors and recruitment of coactivators, and subsequent activation of target gene expression.
Open Targets scores its association with cancer at 0.79 (direct and indirect evidence; datatypes genetic literature 0.30, clinical 0.58, affected pathway 0.25, literature 1.00, genetic association 0.50, somatic mutation 0.93, animal model 0.38).
In plain words · PPARG (Peroxisome proliferator-activated receptor gamma) is a protein that switches other genes on and off. The public catalogues list it as a drug target, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Colorectal cancer, Thyroid cancer and Endometrial cancer.
PPARG (Peroxisome proliferator-activated receptor gamma) is a protein that switches other genes on and off. The public catalogues list it as a drug target, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Colorectal cancer, Thyroid cancer and Endometrial cancer.
Ligand-activated transcription factor that forms obligate heterodimers with the retinoic acid receptor and acts as a key regulator of biological processes, such as adipocyte differentiation, lipid metabolism, glucose homeostasis and beta-oxidation of fatty acids.
No product in this corpus aims at PPARG yet. Transcription factors have no pocket to plug, so drugs either degrade them or block the partner protein they need to dock on DNA.
Specificity not established: no corpus medicine is aimed at it and the catalogues give it only the role drug-target; HPA finds the RNA tissue enhanced, which says where the protein sits but not whether the tumour differs from normal tissue. HPA PPARG: RNA tissue enhanced (adipose tissue 153 nTPM, breast 84 nTPM); high antibody staining in 11 normal tissues; highest cancer staining head and neck cancer (2 of 4 high). Distribution: 3 cancer families in the corpus carry a prevalence row, label threshold or catalogue link for it (Colorectal cancer, Thyroid cancer, Endometrial cancer); Open Targets associates it with 1 specific cancer type at or above 0.5 (colon carcinoma). (No rule of scripts/fetch-target-specificity.ts fired.)
Sources: Human Protein Atlas PPARG tissue; Open Targets ENSG00000132170 associations
First described 1995. Earliest sequence paper UniProt cites for the protein: Greene M.E. et al, Gene Expr, 1995, "Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping". Source.
Sources: HGNC HGNC:9236 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P37231 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000132170 (association with cancer (MONDO_0004992) 0.79; per-cancer scores at or above 0.5: colorectal cancer 0.59, endometrial cancer 0.54, thyroid cancer 0.56 (GraphQL API, CC0))
Ligand-activated transcription factor that forms obligate heterodimers with the retinoic acid receptor and acts as a key regulator of biological processes, such as adipocyte differentiation, lipid metabolism, glucose homeostasis and beta-oxidation of fatty acids. Activated by lipid ligands: binds peroxisome proliferators, such as hypolipidemic drugs, and fatty acids, such as prostaglandin J2 metabolites. Ligand-binding results in a conformational change in the receptor, promoting dissociation of repressors and recruitment of coactivators, and subsequent activation of target gene expression. Specifically binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. Location: Nucleus; Cytoplasm (UniProt). Locus 3p25.2 (HGNC).
RNA: tissue enhanced (adipose tissue 153 nTPM, breast 84 nTPM), detected in many normal tissues.
Medium: Adrenal gland, Duodenum, Gallbladder, Hippocampus, Lung, Salivary gland, Skin, Small intestine.
RNA cancer enhanced: Bladder Urothelial Carcinoma 111 pTPM.
Medium only: breast cancer, liver cancer, lymphoma, ovarian cancer.
HPA PPARG tissue · HPA PPARG pathology · HPA protein class: FDA approved drug targets
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"PPARG" OR ABSTRACT:"PPARG" OR TITLE:"peroxisome proliferator activated receptor gamma" OR ABSTRACT:"peroxisome proliferator activated receptor gamma" OR TITLE:"Peroxisome proliferator-activated receptor gamma" OR ABSTRACT:"Peroxisome proliferator-activated receptor gamma" OR TITLE:"PPARG1" OR ABSTRACT:"PPARG1" OR TITLE:"PPARG2" OR ABSTRACT:"PPARG2" OR TITLE:"NR1C3" OR ABSTRACT:"NR1C3") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about PPARG, not a curated reading list.
Shares Thyroid cancer, Open Targets Platform.
Shares Thyroid cancer, Open Targets Platform.
Shares Thyroid cancer, Open Targets Platform.
Shares Thyroid cancer, Open Targets Platform.
Shares Thyroid cancer, Open Targets Platform.
Shares Thyroid cancer, Open Targets Platform.
Shares Thyroid cancer, Open Targets Platform.
Shares Thyroid cancer, Open Targets Platform.