The ghrelin receptor GHSR has two efficient agonists in the lobe-finned fish Latimeria chalumnae.
The ghrelin receptor GHSR has two efficient agonists in the lobe-finned fish Latimeria chalumnae.
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DOI：
10.1016/j.bbrc.2023.09.002
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发表时间：
2023-09
影响因子：
3.1
通讯作者：
Hao-Zheng Li;Yafang Wang;Yong-Shan Zheng;Ya‐Li Liu;Zeng-guang Xu;Zhan-Yun Guo
中科院分区：
文献类型：
--
作者：
Hao-Zheng Li;Yafang Wang;Yong-Shan Zheng;Ya‐Li Liu;Zeng-guang Xu;Zhan-Yun Guo
The peptide hormone ghrelin (an agonist) and LEAP2 (an antagonist) play important functions in energy metabolism via their receptor GHSR, an A-class G protein-coupled receptor. Ghrelin, LEAP2, and GHSR are widely present from fishes to mammals. However, our recent study suggested that fish GHSRs have different binding properties to ghrelin: a GHSR from the lobe-finned fish Latimeriachalumnae(coelacanth) is efficiently activated by ghrelin, but GHSRs from the ray-finned fishDanio rerio(zebrafish) and Larimichthys crocea (large yellow croaker) have lost binding to ghrelin. Do fish GHSRs use another peptide as their agonist? In the present study we tested to two fish motilins fromD. rerioandL.chalumnaebecause motilin is distantly related to ghrelin. In ligand binding and activation assays, the fish GHSRs fromD. rerioandL. croceadisplayed no detectable or very low binding to all tested motilins; however, the fish GHSR fromL. chalumnaebound to its motilin with high affinity and was efficiently activated by it. Therefore, it seemed that motilin is not a ligand for GHSR in the ray-finned fishD. rerioandL. crocea, but is an efficient agonist for GHSR in the lobe-finned fishL. chalumnae, one of the closest fish relatives of tetrapods. The results of present study suggested that GHSR might have two efficient agonists, ghrelin and motilin, in ancient fishes; however, this feature might be only preserved in some extant fishes with ancient evolutionary origins.
