Communicated by Michael Dean
Variations in human HM74 (GPR109B) and HM74A (GPR109A) niacin receptors†
Article first published online: 3 DEC 2004
© 2004 Wiley-Liss, Inc.
Volume 25, Issue 1, pages 18–21, January 2005
How to Cite
Zellner, C., Pullinger, C. R., Aouizerat, B. E., Frost, P. H., Kwok, P.-Y., Malloy, M. J. and Kane, J. P. (2005), Variations in human HM74 (GPR109B) and HM74A (GPR109A) niacin receptors. Hum. Mutat., 25: 18–21. doi: 10.1002/humu.20121
- Issue published online: 3 DEC 2004
- Article first published online: 3 DEC 2004
- Manuscript Accepted: 11 AUG 2004
- Manuscript Received: 15 JUN 2004
- American Heart Association, Western Affiliate. Grant Number: Postdoctoral Fellowship Award 0225004Y
- haplotype analysis;
HM74 (GPR109B) and the highly homologous gene, HM74A (GPR109A) code for Gi-G protein-coupled orphan receptors that recently have been discovered to be involved in the metabolic effects of niacin. The B vitamin niacin is an important agent used in the treatment of dyslipidemias, but its use is limited by side effects. The novel role of the adjacent HM74 and HM74A genes in the metabolism of niacin may provide new targets for drug development. Human genetic variations in HM74 and HM74A have been reported but have not been studied in detail. These variations may play a role in the response to agents targeting receptors coded by these genes. Here we show that many of the nonsynonymous SNPs listed in public databases for HM74 and HM74A are artifacts resulting from extensive homology between these two genes. This may be representative of a neglected phenomenon in reporting sequences of highly homologous genes. We provide primer sequences that permit selective amplification of the complete coding regions of HM74 and HM74A. Using these primers, we show that subsequent sequencing of HM74 and HM74A reveals a novel and unique variation in the HM74A gene. Haplotype analysis suggests four SNPs can define the five major haplotypes that lie within a single haplotype block encompassing these two genes. Hum Mutat 25:18–21, 2005. © 2004 Wiley-Liss, Inc.