{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRecent investigations into the atypical functions of angiotensin‐converting enzyme (ACE) have revealed its ability to interact with membrane‐bound proteins such as carboxypeptidase M (CPM) via glycosylphosphatidylinositol (GPI)‐anchored mechanisms. Although TTTY22 is not directly examined in these studies, its genomic proximity to the CPM locus raises the possibility that this transcript, like other non‐protein coding RNAs, might modulate or influence the local microenvironment that supports ACE–CPM interactions and the ensuing release of CPM. This notion is supported by findings demonstrating that ACE, independent of its dipeptidase activity, can evoke the release of CPM in cellular models."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn broader genomic analyses aimed at refining our understanding of gene architecture, the region encompassing the CPM locus has been shown to harbor multiple transcripts beyond traditional protein coding sequences. Among these, TTTY22 emerges as a candidate non‐coding RNA whose expression may be intricately linked with the regulation of CPM gene structure and function. The study highlights how transcriptome data have unveiled layers of complexity, suggesting that TTTY22 could play a role in gene regulatory networks operating in this critical region."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn summary, while the precise function of TTTY22 remains to be fully elucidated, insights derived from the interplay between ACE and CPM, along with comprehensive transcriptomic evaluations, imply that TTTY22 may contribute to the regulation of membrane protein functions and proteolytic activity at the CPM locus. Ongoing and future studies are essential to further define its role within these regulatory circuits."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Xiaoou Sun, Burkhard Wiesner, Dorothea Lorenz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interaction of angiotensin-converting enzyme (ACE) with membrane-bound carboxypeptidase M (CPM) - a new function of ACE."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1515/BC.2008.168"}], "href": "https://doi.org/10.1515/BC.2008.168"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18844448"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18844448"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Alessander O Guimarães, Fabiana L Motta, Viviane S Alves, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Multiple RNAs from the mouse carboxypeptidase M locus: functional RNAs or transcription noise?"}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Mol Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1471-2199-10-7"}], "href": "https://doi.org/10.1186/1471-2199-10-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19200403"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19200403"}]}]}]}