Abstract
We present herein the cloning of the human nicotinic acetylcholine receptor α9-ortholog and the identification of a new α-like subunit (α10) that shares 58% identity with α9. Whereas α10 fails to produce functional receptors alone, it promoted robust acetylcholine-evoked currents when coinjected with α9. The presence of α10 modifies the physiological and pharmacological properties of the α9 receptor indicating that the two subunits coassemble in a single functional receptor. Fusing the N-terminal domain of α9 with the rest of the α10-cDNA yielded a functional α9:α10-chimera that displays the acetylcholine binding properties of α9 and ionic pore characteristics of α10-containing receptors. In addition, α9- and α10-subunit mRNAs show limited similar tissue distribution patterns and are expressed in cochlea, pituitary gland, and keratinocytes. These data suggest that, in vivo, α9-containing receptors coassemble with α10-subunit.
- The American Society for Pharmacology and Experimental Therapeutics
MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|