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Gene Review:

Hcar2 - hydroxycarboxylic acid receptor 2

Mus musculus

Synonyms: G-protein coupled receptor 109, G-protein coupled receptor 109A, G-protein coupled receptor HM74, Gpr109, Gpr109a, ...

Taggart, A.K. et al., Tunaru, S. et al., Benyó, Z. et al., Schaub, A. et al., Lorenzen, A. et al., et al.

Lorenzen, Stannek, Burmeister, Kalvinsh, Schwabe, Taggart, Kero, Gan, Cai, Cheng, Ippolito, Ren, Kaplan, Wu, Wu, Jin, Liaw, Chen, Richman, Connolly, Offermanns, Wright, Waters,

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Disease relevance of Gpr109a

The identification of the nicotinic acid receptor may be useful in the development of new drugs to treat dyslipidemia [1].
In vivo PUMA-G was up-regulated in mice suffering from microbial sepsis or from Listeria monocytogenes infection [2].

High impact information on Gpr109a

Binding of nicotinic acid to PUMA-G or HM74 results in a G(i)-mediated decrease in cAMP levels [1].
In mice lacking PUMA-G, the nicotinic acid-induced decrease in free fatty acid (FFA) and triglyceride plasma levels was abrogated, indicating that PUMA-G mediates the anti-lipolytic and lipid-lowering effects of nicotinic acid in vivo [1].
The mouse orthologue of GPR109A, PUMA-G, is highly expressed in macrophages and other immune cells, and transplantation of wild-type bone marrow into irradiated PUMA-G-deficient mice restored the nicotinic acid-induced flushing response [3].
In mice, nicotinic acid inhibits lipolysis via PUMA-G, a Gi/o-coupled seven-transmembrane receptor expressed in adipocytes and activated macrophages (Tunaru, S., Kero, J., Schaub, A., Wufka, C., Blaukat, A., Pfeffer, K., and Offermanns, S. (2003) Nat. Med. 9, 352-355) [4].
(D)-beta-Hydroxybutyrate inhibits adipocyte lipolysis via the nicotinic acid receptor PUMA-G [4].

Biological context of Gpr109a

PUMA-G maps to mouse chromosome 5F [2].
Characterization of the genomic locus revealed an intronless PUMA-G open reading frame [2].

Anatomical context of Gpr109a

The rank orders of potency in macrophage membranes were identical for inhibition of [(3)H]nicotinic acid binding and G protein activation, and were pharmacologically indistinguishable from that of the G protein-coupled nicotinic acid receptor in spleen membranes [5].
Our results provided direct evidence indicating that HM74A, but not HM74, was sufficient to mediate anti-lipolytic effect of niacin in adipose tissue [6].

Associations of Gpr109a with chemical compounds

Here we show that the fatty acid-derived ketone body (D)-beta-hydroxybutyrate ((D)-beta-OHB) specifically activates PUMA-G/HM74a at concentrations observed in serum during fasting [4].

Analytical, diagnostic and therapeutic context of Gpr109a

Genomic Southern blot analysis indicates that PUMA-G is a single-copy gene [2].

References

PUMA-G and HM74 are receptors for nicotinic acid and mediate its anti-lipolytic effect. Tunaru, S., Kero, J., Schaub, A., Wufka, C., Blaukat, A., Pfeffer, K., Offermanns, S. Nat. Med. (2003) [Pubmed]
PUMA-G, an IFN-gamma-inducible gene in macrophages is a novel member of the seven transmembrane spanning receptor superfamily. Schaub, A., Fütterer, A., Pfeffer, K. Eur. J. Immunol. (2001) [Pubmed]
GPR109A (PUMA-G/HM74A) mediates nicotinic acid-induced flushing. Benyó, Z., Gille, A., Kero, J., Csiky, M., Suchánková, M.C., Nüsing, R.M., Moers, A., Pfeffer, K., Offermanns, S. J. Clin. Invest. (2005) [Pubmed]
(D)-beta-Hydroxybutyrate inhibits adipocyte lipolysis via the nicotinic acid receptor PUMA-G. Taggart, A.K., Kero, J., Gan, X., Cai, T.Q., Cheng, K., Ippolito, M., Ren, N., Kaplan, R., Wu, K., Wu, T.J., Jin, L., Liaw, C., Chen, R., Richman, J., Connolly, D., Offermanns, S., Wright, S.D., Waters, M.G. J. Biol. Chem. (2005) [Pubmed]
G protein-coupled receptor for nicotinic acid in mouse macrophages. Lorenzen, A., Stannek, C., Burmeister, A., Kalvinsh, I., Schwabe, U. Biochem. Pharmacol. (2002) [Pubmed]
Niacin mediates lipolysis in adipose tissue through its G-protein coupled receptor HM74A. Zhang, Y., Schmidt, R.J., Foxworthy, P., Emkey, R., Oler, J.K., Large, T.H., Wang, H., Su, E.W., Mosior, M.K., Eacho, P.I., Cao, G. Biochem. Biophys. Res. Commun. (2005) [Pubmed]

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HCAR2	Homo sapiens
HCAR2	Pan troglodytes
Niacr1	Rattus norvegicus

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