{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSLC7A1, also known as cationic amino acid transporter‐1 (CAT1), is a crucial plasma membrane protein that mediates the uptake of positively charged amino acids—most notably L‐arginine, the essential substrate for nitric oxide (NO) synthesis. In vascular endothelial cells, efficient L‐arginine import by SLC7A1 is necessary to sustain NO production, help maintain vasodilatory function, and preserve normal endothelial activity. Regulation of SLC7A1 in these cells is modulated by hormones and intracellular signaling proteins; for example, insulin and 17β‐estradiol enhance SLC7A1 expression and activity via transcriptional mechanisms involving Sp1, while protein kinase C activation leads to transporter phosphorylation, ubiquitination, and clathrin‐dependent endocytosis. Moreover, genetic variants that affect SLC7A1 regulatory elements—such as polymorphisms impacting SP1 binding and microRNA interaction—may contribute to endothelial dysfunction and a predisposition to hypertension."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in endothelial L‐arginine delivery, SLC7A1 exhibits tightly controlled membrane trafficking and kinetic properties. Studies have demonstrated that upon protein kinase C activation, SLC7A1 undergoes ubiquitination and internalization via clathrin‐coated pits, thereby modulating its surface expression. In addition, SLC7A1 not only transports L‐arginine but also facilitates the uptake of related substrates such as asymmetric dimethylarginine (ADMA) and L‐homoarginine, with competitive interactions among these ligands influencing cellular substrate availability. Detailed analyses in polarized cells have further characterized its basolateral localization and gene structure, underscoring the complexity of its regulation and intracellular trafficking."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "12"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSLC7A1’s function extends into pathological contexts, particularly in cancer and cell growth. In breast and colorectal cancer cells, over‐expression of SLC7A1 contributes to the accumulation of L‐arginine, supporting enhanced nitric oxide production, cellular proliferation, and survival. In ovarian cancer, high SLC7A1 levels in cancer‐associated fibroblasts promote invasion and metastasis via MAPK/ERK and epithelial–mesenchymal transition signaling. Additionally, in KRAS‐mutant non‐small cell lung cancer, the suppression of urea cycle enzymes creates an arginine dependency that renders the tumor cells particularly reliant on extracellular arginine uptake through SLC7A1."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "17"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in vascular function and tumor progression, SLC7A1 participates in a variety of other physiological and disease‐related processes. In models of Duchenne muscular dystrophy, up‐regulation of SLC7A1 appears to serve as a compensatory mechanism to maintain NO signaling in cardiac muscle. In the skin, SLC7A1 supports L‐arginine transport necessary for both inducible nitric oxide synthase and arginase activities that govern keratinocyte proliferation and differentiation—a process that is altered in inflammatory conditions such as psoriasis. Preliminary observations in diabetic kidneys, heart failure, and gestational dyslipidemia further suggest that fluctuations in SLC7A1 expression modulate local NO metabolism and contribute to disease manifestations. Its widespread presence is also evident in the brain, where SLC7A1 is expressed by neurons and glial cells, and novel findings indicate that it may be exploited as a receptor‐mediated pathway for transcytosis across the blood–brain barrier. Finally, studies in erythroid cells have revealed that optimal SLC7A1 function is essential for erythropoiesis, highlighting its importance in systemic amino acid homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "29"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Zhiyong Yang, Kylie Venardos, Emma Jones, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of a novel polymorphism in the 3'UTR of the L-arginine transporter gene SLC7A1: contribution to hypertension and endothelial dysfunction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Circulation (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1161/CIRCULATIONAHA.106.665836"}], "href": "https://doi.org/10.1161/CIRCULATIONAHA.106.665836"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17325243"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17325243"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Zhiyong Yang, David M Kaye "}, {"type": "b", "children": [{"type": "t", "text": "Mechanistic insights into the link between a polymorphism of the 3'UTR of the SLC7A1 gene and hypertension."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mutat (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/humu.20891"}], "href": "https://doi.org/10.1002/humu.20891"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19067360"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19067360"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Marcelo González, Victoria Gallardo, Natalia Rodríguez, et al. 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