Evidence map›Paper›PMID 33079129›Full record

ArticleThe Biochemical journal2020

Functional analysis of a species-specific inhibitor selective for human Na+-coupled citrate transporter (NaCT/SLC13A5/mINDY).

Kei Higuchi, Jonathan J Kopel, Sathish Sivaprakasam, Valeria Jaramillo-Martinez, R Bryan Sutton, Ina L Urbatsch, Vadivel Ganapathy

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 24 citations in OpenAlex.

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  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Kei HiguchiDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock 79430, Texas, U.S.A.
Jonathan J KopelDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock 79430, Texas, U.S.A.
Sathish SivaprakasamDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock 79430, Texas, U.S.A.
Valeria Jaramillo-MartinezDepartment of Pharmacology and Neuroscience, Texas Tech University Health Sciences Center, Lubbock 79430, Texas, U.S.A.
R Bryan SuttonDepartment of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock 79430, Texas, U.S.A.
Ina L UrbatschDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock 79430, Texas, U.S.A.
Vadivel GanapathyDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock 79430, Texas, U.S.A.
Texas Tech University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Na+-coupled citrate transporter (NaCT/SLC13A5/mINDY) in the liver delivers citrate from the blood into hepatocytes. As citrate is a key metabolite and regulator of multiple biochemical pathways, deletion of Slc13a5 in mice protects against diet-induced obesity, diabetes, and metabolic syndrome. Silencing the transporter suppresses hepatocellular carcinoma. Therefore, selective blockers of NaCT hold the potential to treat various diseases. Here we report on the characteristics of one such inhibitor, BI01383298. It is known that BI01383298 is a high-affinity inhibitor selective for human NaCT with no effect on mouse NaCT. Here we show that this compound is an irreversible and non-competitive inhibitor of human NaCT, thus describing the first irreversible inhibitor for this transporter. The mouse NaCT is not affected by this compound. The inhibition of human NaCT by BI01383298 is evident for the constitutively expressed transporter in HepG2 cells and for the ectopically expressed human NaCT in HEK293 cells. The IC50 is ∼100 nM, representing the highest potency among the NaCT inhibitors known to date. Exposure of HepG2 cells to this inhibitor results in decreased cell proliferation. We performed molecular modeling of the 3D-structures of human and mouse NaCTs using the crystal structure of a humanized variant of VcINDY as the template, and docking studies to identify the amino acid residues involved in the binding of citrate and BI01383298. These studies provide insight into the probable bases for the differential effects of the inhibitor on human NaCT versus mouse NaCT as well as for the marked species-specific difference in citrate affinity.

Indexed as

AnimalsCitric AcidEnzyme InhibitorsHEK293 CellsHep G2 CellsHumansInhibitory Concentration 50MiceModels, MolecularProtein BindingSpecies SpecificitySymportersCitric AcidEnzyme InhibitorsSLC13A5 protein, humanSymportersBI01383298cell growth arrestirreversible inhibitionmolecular modelingNACT/SLC13a5/mINDYspecies-specificity

Identifiers

PMID33079129
PMCPMC7657661
OpenAlexW3093428977

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.