ArticleProceedings of the National Academy of Sciences of the United States of America2014
Transcriptional regulation of the sodium-coupled neutral amino acid transporter (SNAT2) by 17β-estradiol.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- SNAT2-mediated regulation of estrogen and progesterone in the proliferation of goat mammary epithelial cells.Amino acids · 2024Article
- Nutrient uptake and metabolism in osteoblasts.Current opinion in endocrine and metabolic research · 2023Article
- SLC38A2 provides proline and alanine to regulate postnatal bone mass accrual in mice.Frontiers in physiology · 2022Article
- Effects of a High-Grain Diet With a Buffering Agent on Milk Protein Synthesis in Lactating Goats.Frontiers in veterinary science · 2021Article
- Hypoxia-induced switch in SNAT2/SLC38A2 regulation generates endocrine resistance in breast cancer.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- CDK7 is a component of the integrated stress response regulating SNAT2 (SLC38A2)/System A adaptation in response to cellular amino acid deprivation.Biochimica et biophysica acta. Molecular cell research · 2019Article
- Article
- The Regulatory Role of MeAIB in Protein Metabolism and the mTOR Signaling Pathway in Porcine Enterocytes.International journal of molecular sciences · 2018Article
- Identification of estrogen-responsive genes based on the DNA binding properties of estrogen receptors using high-throughput sequencing technology.Acta pharmacologica Sinica · 2015Review
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Authors and funding
12 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sodium-coupled neutral amino acid transporter 2 (SNAT2) translocates small neutral amino acids into the mammary gland to promote cell proliferation during gestation. It is known that SNAT2 expression increases during pregnancy, and in vitro studies indicate that this transporter is induced by 17β-estradiol. In this study, we elucidated the mechanism by which 17β-estradiol regulates the transcription of SNAT2. In silico analysis revealed the presence of a potential estrogen response element (ERE) in the SNAT2 promoter. Reporter assays showed an increase in SNAT2 promoter activity when cotransfected with estrogen receptor alpha (ER-α) after 17β-estradiol stimulation. Deletion of the ERE reduced estradiol-induced promoter activity by 63%. Additionally, EMSAs and supershift assays showed that ER-α binds to the SNAT2 ERE and that this binding competes with the interaction of ER-α with its consensus ERE. An in vivo ChIP assay demonstrated that the binding of ER-α to the SNAT2 promoter gradually increased in the mammary gland during gestation and that maximal binding occurred at the highest 17β-estradiol serum concentration. Liquid chromatography-elevated energy mass spectrometry and Western blot analysis revealed that the SNAT2 ER-α-ERE complex contained poly(ADP-ribose) polymerase 1, Lupus Ku autoantigen protein p70, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) proteins and that the silencing of each of these proteins nearly abolished 17β-estradiol-stimulated SNAT2 promoter activity. Nuclear levels of GAPDH increased progressively during gestation in the mammary gland, and GAPDH binding was nucleotide-specific for the SNAT2 ERE. Thus, this study provides new insights into how the mammary epithelium adapts to control amino acid uptake through the transcriptional regulation of the SNAT2 transporter via 17β-estradiol.
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