ArticleJournal of physical organic chemistry2022
Alanine serine cysteine transporter (ASCT) substrate binding site properties probed with hydroxyhomoserine esters.
Article in Journal of physical organic chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 6 citations in OpenAlex.
- Exploring Amino Acid Transporters as Therapeutic Targets for Cancer: An Examination of Inhibitor Structures, Selectivity Issues, and Discovery Approaches.Pharmaceutics · 2024Review
- Investigations of potential non-amino acid SNAT2 inhibitors.Frontiers in pharmacology · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The glutamine transporter ASCT2 is highly overexpressed in cancer cells. Block of glutamine uptake by ASCT2 is a potential strategy to inhibit growth of cancer cells. However, pharmacology of the ASCT2 binding site is not well established. In this work, we report the computational docking to the binding site, and the synthesis of a new class of ASCT2 inhibitors based on the novel L-hydroxyhomoserine scaffold. While these compounds inhibit the ASCT2 leak anion conductance, as expected for competitive inhibitors, they did not block leak conductance in glutamate transporters (EAAT1-3 and EAAT5). They were also ineffective with respect to subtype ASCT1, which has >57% amino acid sequence similarity to ASCT2. Molecular docking studies agree very well with the experimental results and suggest specific polar interactions in the ASCT2 binding site. Our findings add to the repertoire of ASCT2 inhibitors and will aid in further studies of ASCT2 pharmacology.
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Registered trials
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