1. Trp-Trp acts as a multifunctional blocker for human bitter taste receptors, hTAS2R14, hTAS2R16, hTAS2R43, and hTAS2R46
Ichie Ojiro, Hiromi Nishio, Toyomi Yamazaki-Ito, Shogo Nakano, Sohei Ito, Yoshikazu Toyohara, Tadahiro Hiramoto, Yuko Terada, Keisuke Ito Biosci Biotechnol Biochem. 2021 May 25;85(6):1526-1529. doi: 10.1093/bbb/zbab061.
Many functional food ingredients activate human bitter taste receptors (hTAS2Rs). In this study, A novel inhibitor, Trp-Trp, for hTAS2R14 was identified by searching for the agonist peptide's analogs. Trp-Trp also inhibited hTAS2R16, hTAS2R43, and hTAS2R46, which share the same agonists with hTAS2R14. The multifunctional characteristic of Trp-Trp is advantageous for use as bitterness-masking agents in functional foods.
2. Transient receptor potential (TRP) channels, promising potential diagnostic and therapeutic tools for cancer
Jianpeng Chen, Yi Luan, Ruofei Yu, Zheng Zhang, Jinbiao Zhang, Weibo Wang Biosci Trends. 2014 Feb;8(1):1-10. doi: 10.5582/bst.8.1.
Despite the advances in detection of and therapies for various tumors, high rates of treatment failure and mortality still exist throughout the world. These high rates are mainly due to the powerful capability of tumor cells to proliferate and migrate. Recent studies regarding the transient receptor potential (TRP) have indicated that TRP channels are associated with tumors and that TRP channels might represent potential targets for cancer treatment. TRP channels are important calcium-selective ion channels in many different tissues and cell types in mammals and are crucial regulators of calcium and sodium. TRP were first discovered in the photoreceptors of Drosophila with gene defects or mutations. TRP channels can be divided into seven subfamilies: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPML (mucolipin), TRPP (polycystin), TRPA (ankyrin transmembrane protein), and TRPN (NomPC-like). TRPC proteins are conserved across organisms since they are most homologous to Drosophila TRP. TRP superfamilies have been linked to many physiological and pathological functions, including cell differentiation, proliferation, apoptosis, and ion homeostasis. This review focuses on the properties of TRP in oncogenesis, cancer proliferation, and cell migration.
3. The TRP superfamily of cation channels
Craig Montell Sci STKE. 2005 Feb 22;2005(272):re3. doi: 10.1126/stke.2722005re3.
The transient receptor potential (TRP) protein superfamily consists of a diverse group of cation channels that bear structural similarities to Drosophila TRP. TRP channels play important roles in nonexcitable cells; however, an emerging theme is that many TRP-related proteins are expressed predominantly in the nervous system and function in sensory physiology. The TRP superfamily is divided into seven subfamilies, the first of which is composed of the "classical" TRPs" (TRPC subfamily). Some TRPCs may be store-operated channels, whereas others appear to be activated by production of diacylglycerol or regulated through an exocytotic mechanism. Many members of a second subfamily (TRPV) function in sensory physiology and respond to heat, changes in osmolarity, odorants, and mechanical stimuli. Two members of the TRPM family function in sensory perception and three TRPM proteins are chanzymes, which contain C-terminal enzyme domains. The fourth and fifth subfamilies, TRPN and TRPA, include proteins with many ankyrin repeats. TRPN proteins function in mechanotransduction, whereas TRPA1 is activated by noxious cold and is also required for the auditory response. In addition to these five closely related TRP subfamilies, which comprise the Group 1 TRPs, members of the two Group 2 TRP subfamilies, TRPP and TRPML, are distantly related to the group 1 TRPs. Mutations in the founding members of these latter subfamilies are responsible for human diseases. Each of the TRP subfamilies are represented by members in worms and flies, providing the potential for using genetic approaches to characterize the normal functions and activation mechanisms of these channels.
