Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 521, Issue 1, Pages 227-231Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.10.111
Keywords
Calcium-sensing receptor; Agonist; Class C GPCR; Lysozyme; Thaumatin; Sweet protein
Categories
Funding
- KAKENHI from the Japan Society for the Promotion of Science [18K19753, 18H03195, 19K15792]
- Kieikai Research Foundation
- Fuji Foundation for Protein Research
- Grants-in-Aid for Scientific Research [19K15792, 18H03195, 18K19753] Funding Source: KAKEN
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In addition to the maintenance of Ca2+ homeostasis, the calcium-sensing receptor (CaSR) is involved in many diverse physiological functions in the mammalian body. The receptor works as a kokumi taste receptor in taste buds and as a nutrient sensor in the gut, where it regulates the secretion of glycemic response and appetite-related hormones. To identify novel human CaSR (hCaSR) activators from food ingredients, we conducted a screening using a cell-based hCaSR assay. Hen egg-white lysozyme, which is a sweet protein, was found to be a novel orthosteric agonist of hCaSR with an EC50 value of 592 mu M. Lysozyme hydrolysate was not able to activate hCaSR, thus suggesting that the protein structure of lysozyme is necessary for hCaSR activation. Thaumatin, which is another sweet protein, also activated hCaSR with an EC50 value of 71 mu M. This is the first report that shows hCaSR activation by proteins with molecular weights exceeding 10,000 Da. These results provide a new avenue for the development of hCaSR activators, which could be applicable in food or drugs that modulate taste perception, appetite, or glucose tolerance, in addition to Ca2+ homeostasis. (C) 2019 Elsevier Inc. All rights reserved.
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