Is rat LRRP Ba1-651 a Delta-1-pyrroline-5-carboxylate dehydrogenase activated by changes in the concentration of sweet molecules?

The ANF receptor domain of rat LRRP Ba1-651, which domain is part of the receptor family ligand binding region, shows a very high sequence homology (almost identity) to the extracellular amino-terminal domains of the mammalian sweet taste receptor T1R2. This receptor belongs to the type C family of G protein coupled receptors (GPCRs) and is characterized by the presence of large extracellular amino-terminal domains, a nine cysteine domain of family 3 GPCR and a 7tm_3 transmembrane type domain. We suggest that rat LRRP Ba1-651 protein is a liver P5CDh-ANF that is activated by changes in the concentration of sweet molecules. If the sugar concentration in the organ increases due to liver damage or the intake of carbohydrate-rich or protein-rich foods, the P5CDh-ANF enzyme is activated to help in P5C catabolism. The hormone insulin probably plays a key role in the regulation of this enzyme. In the model that we propose, the P5CDh-ANF enzyme is activated by a conformational change in protein structure in the P5C docking site due to sugars binding in the AFN receptor region of the LRRP Ba1-651 protein. Our research could be a further understanding of the biological significance of this P5CDh-ANF enzyme, with important potential applications in the treatment of HPII and liver diseases and in liver transplantation. Further studies of our P5CDh-ANF enzyme are needed to clarify its features and functions, and which substances are involved in its induction. These might use liver cell lines or purified LRRP Ba1-651 protein with sweet molecules in vitro. Other experiments may help to localize LRRP Bal-651 in the organ and to link its abnormal presence or absence to certain tumors like hepatocellular carcinoma.