The alanine at position 8, the residue immediately adjacent to the DPP-4 cleavage bond, is replaced by alpha-aminoisobutyric acid (Aib), a non-canonical, doubly methylated amino acid whose steric bulk blocks protease access [1]
Sep 2015;1(3):119-122
Glutathione peroxidase 4 (GPX4), a key inhibitor of ferroptosis, uses glutathione (GSH) as a cofactor to reduce phospholipid hydroperoxides to their corresponding alcohols, thereby protecting cells and membranes from oxidative damage
The title for Figure 4 should be reconsidered as the term "mutually opposite signal modulation" is unclear and/or does not reflect the description to follow. Response: We have replaced the term mutually opposite signal modulation with: amplification of MC3R signaling and attenuation of GHSR1a signaling For Figure 5, the figure legend should clarified if 5-HT2c-GHSR1a dimerization produces reduced Ca++ accumulation with (as appears to be implied by the figure) or without ligand for each receptor. Response: To make it clearer that the 5-HT2C ligand is not required, while the ghrelin ligand is, we have changed the description to read: When dimerized with 5-HT2C, GHSR1a displays a 65% reduction in ghrelin-induced Ca2+ accumulation, with this effect not requiring the presence of a 5-HT2C ligand. Reviewer #2: The review includes an excellent explanation of GSHR1a dimerization with other receptors at the cellular and molecular level and also does a good job of explaining technical aspects of this type of work
David Amron
Dysbiosis of Gut Microbiota (DOGMA)a novel theory for the development of Polycystic Ovarian Syndrome
