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SCIE SCOPUS
Ligand Binding Properties of Muscarinic Acetylcholine Receptors in Caenorhabditis elegans
Suck Jong You , Jung Do Choi, Nam Jeong Cho
BMB Reports vol. 29 iss. 6 525-529(5pages)
UCI I410-ECN-0102-2008-470-002190174

Ligand binding properties of muscarinic acetylcholine receptors (mAChRs) in the nematode Caenorhabditis elegans (C. elegans) were characterized by using filtration binding assays. Scatchard analysis using [³H]N-methylscopolamine ([³H]NMS) showed that the dissociation constant (K_d) and the maximum binding value (B_(max)) were 3.3±0.8×1^(-10)M and 9.0±1.1 fmol/㎎ protein, respectively. Binding competition experiments indicated that the affinities of C. elegans mAChRs to atropine. scopolamine, and oxotremorine were similar to those of mammalian mAChRs. Pirenzepine binding experiments revealed that the binding pattern of mAChRs in C. elegans closely resembled that of mAChRs in rat brain, suggesting that the receptors consist primarily of M1 subtype. The affinity of mAChRs for oxotremorine was significantly affected by guanylylimidodiphosphate (Gpp(NH)p), a nonhydrolyzable GTP analog, suggesting that mAChRs in C. elegans might be coupled to G proteins. The data presented here indicate the possibility that C. elegans provides a living animal model to study the action mode of the muscarinic cholinergic system.

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