Peroxisome proliferator-activated receptor alpha


Peroxisome proliferator-activated receptor alpha
Peroxisome proliferator-activated receptor alpha

PDB rendering based on 1i7g.
Identifiers
Symbols PPARA; MGC2237; MGC2452; NR1C1; PPAR; PPARalpha; hPPAR
External IDs OMIM170998 MGI104740 HomoloGene21047 IUPHAR: NR1C1 GeneCards: PPARA Gene
RNA expression pattern
PBB GE PPARA 206870 at tn.png
PBB GE PPARA gnf1h00859 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5465 19013
Ensembl ENSG00000186951 ENSMUSG00000022383
UniProt Q07869 Q542P9
RefSeq (mRNA) NM_001001928.2 NM_011144
RefSeq (protein) NP_001001928.1 NP_035274
Location (UCSC) Chr 22:
46.55 – 46.64 Mb
Chr 15:
85.57 – 85.63 Mb
PubMed search [1] [2]

Peroxisome proliferator-activated receptor alpha (PPAR-alpha), also known as NR1C1 (nuclear receptor subfamily 1, group C, member 1), is a nuclear receptor protein that in humans is encoded by the PPARA gene.[1]

Contents

Function

PPAR-alpha is a transcription factor and a major regulator of lipid metabolism in the liver. PPAR-alpha is activated under nutrient-deficient conditions and is necessary for the process of ketogenesis, a key adaptive response to prolonged fasting [2]. Activation of PPAR-alpha promotes uptake, utilization, and catabolism of fatty acids by upregulation of genes involved in fatty acid transport and peroxisomal and mitochondrial fatty acid β-oxidation. PPAR-alpha is primarily activated through ligand binding. Synthetic ligands include the fibrate drugs, which are used to treat hyperlipidemia. An endogenous ligand has been identified as the phosphatidylcholine species 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine [3]. Endogenous activation of PPAR-alpha is dependent on the presence of fatty acid synthase.

Interactions

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

See also

References

  1. ^ Sher T, Yi HF, McBride OW, Gonzalez FJ (June 1993). "cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor". Biochemistry 32 (21): 5598–604. doi:10.1021/bi00072a015. PMID 7684926. 
  2. ^ Kersten S, Seydoux J, Peters JM, Gonzalez FJ, Desvergne B, Wahli W. (June 1999). "Peroxisome proliferator-activated receptor alpha mediates the adaptive response to fasting.". J Clin Invest. 103 (11): 1489–98. doi:10.1172/JCI6223. PMC 408372. PMID 10359558. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=408372. 
  3. ^ Chakravarthy MV, Lodhi IJ, Yin L, Malapaka RR, Xu HE, Turk J, Semenkovich CF. (August 2009). "Identification of a physiologically relevant endogenous ligand for PPARalpha in liver.". Cell. 138 (3): 476–88. doi:10.1016/j.cell.2009.05.036. PMC 2725194. PMID 19646743. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2725194. 
  4. ^ a b Sumanasekera WK, Tien ES, Turpey R, Vanden Heuvel JP, Perdew GH (February 2003). "Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2". J. Biol. Chem. 278 (7): 4467–73. doi:10.1074/jbc.M211261200. PMID 12482853. 
  5. ^ a b Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (December 1997). "p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha". J. Biol. Chem. 272 (52): 33435–43. doi:10.1074/jbc.272.52.33435. PMID 9407140. 
  6. ^ a b Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (May 1999). "Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein". J. Biol. Chem. 274 (22): 15901–7. doi:10.1074/jbc.274.22.15901. PMID 10336495. 
  7. ^ Treuter E, Albrektsen T, Johansson L, Leers J, Gustafsson JA (June 1998). "A regulatory role for RIP140 in nuclear receptor activation". Mol. Endocrinol. 12 (6): 864–81. doi:10.1210/me.12.6.864. PMID 9626662. 

Further reading

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


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