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Last update 08 May 2025

SLC7A9

Last update 08 May 2025

Basic Info

Synonyms

b(0,+)-type amino acid transporter 1, b(0,+)AT1, BAT1

+ [5]

Introduction

Associates with SLC3A1 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1 (PubMed:16825196, PubMed:32494597, PubMed:32817565, PubMed:8663357). Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids (PubMed:16825196, PubMed:32494597, PubMed:8663357). Substrate exchange is driven by high concentration of intracellular neutral amino acids and the intracellular reduction of L-cystine to L-cysteine (PubMed:8663357). Required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane in renal proximal tubules.

Drugs associated with SLC7A9

Cystinuria (BridgeBio Pharma)

Target

SLC3A1 x SLC7A9

Mechanism

SLC3A1 modulators [+1]

Active Org.-

Originator Org.

BridgeBio Pharma, Inc.

Active Indication-

Inactive Indication

Cystinuria

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SLC7A9

100 Translational Medicine associated with SLC7A9

0 Patents (Medical) associated with SLC7A9

282

Literatures (Medical) associated with SLC7A9

01 Jun 2025·Poultry Science

Transport and expression of transporters for 3-O-methyl-D-glucose and L-methionine along the intestine of broiler chickens receiving different methionine supplements

Article

Author: Schermuly, Isabel I ; Riedel, Julia ; Saliu, Eva-Maria ; Romanet, Stella ; Lemme, Andreas ; Zentek, Jürgen ; Aschenbach, Jörg R

The present study hypothesized that supplementation of different methionine (Met) sources might influence the intestinal absorption of l-Met and 3-O-methyl-d-glucose (3-OMG) in broilers. In a completely randomized study, a total of 53 Cobb500 broilers (30 males and 23 females) received a grower-finisher diet that was either not supplemented with Met (Met + Cys, 0.49 %; control) or supplemented with either 0.27 % l-Met, 0.27 % DL-Met or 0.47 % DL-2‑hydroxy-4-(methylthio) butanoic acid (HMTBA). After ≥10 days on the diets, uptakes of 3-OMG and l-Met were measured in duodenum, mid-jejunum and caecum at 50 µM and 5 mM concentrations in Ussing chambers, each in the presence and absence of Na⁺. We also investigated the mRNA expression of apical glucose and Met transporters. Dietary supplements had no effect on 3-OMG and l-Met uptakes (P > 0.05), except for male broilers receiving DL-Met or DL-HMTBA, that showed higher jejunal uptakes of l-Met than control at 5 mM (P < 0.001). Except for l-Met uptakes at 5 mM, tissue × sodium interactions (P ≤ 0.05) for 3-OMG and l-Met uptakes verified higher uptakes in jejunum compared to duodenum and caecum; with higher uptakes in the presence vs. absence of Na⁺ in jejunum only. In duodenum, uptakes of l-Met and 3-OMG at 50 µM concentration were higher in males vs. females. Expression of SGLT1, B⁰AT1, ATB^0,+ and rBAT, but not ASCT1, were lowest in caecum (P ≤ 0.05). Expression of B⁰AT1 was higher in males vs. females (P ≤ 0.05). Expression of ASCT1 was higher with DL-Met and DL-HMTBA supplements compared to l-Met and control (P ≤ 0.05). These findings indicate that jejunum is the main intestinal segment for Na⁺-dependent l-Met and 3-OMG absorption in broilers with minor effects of dietary Met source. A sexual dimorphism for duodenal nutrient uptake and mRNA abundance of B⁰AT1 was congruent with the more efficient growth performance of male chickens known from the literature.

01 Apr 2025·Naunyn-Schmiedeberg's Archives of Pharmacology

Differential uptake of arginine derivatives by the human heteromeric amino acid transporter b0,+AT-rBAT (SLC7A9-SLC3A1)

Article

Author: Maas, Renke ; Banjarnahor, Sofna ; König, Jörg ; Keller, Max ; Scherpinski, Lorenz A ; Scherpinski, Lorenz A.

AbstractL-arginine and its (patho-)physiologically active derivatives, L-homoarginine and asymmetric dimethylarginine (ADMA), show significant differences in their renal clearance. The underlying molecular mechanisms remain to be elucidated, but selective tubular transport protein-mediated mechanisms likely play a role. In the present study, we investigate the human heteromeric transporter b0,+AT-rBAT (encoded by the SLC7A9 and SLC3A1 genes) as a potential candidate because it is localized in the luminal membrane of human proximal tubule cells and capable of mediating the cellular uptake of amino acids, including L-arginine. Double-transfected Madin-Darby canine kidney (MDCK) cells stably expressing human b0,+AT-rBAT exhibited significant uptake of L-arginine and L-homoarginine, with apparent Km values of 512.6 and 197.0 μM, respectively. On the contrary, ADMA uptake was not saturated up to 4000 μM, with a transport rate > 5 nmol × mg protein−1 × min−1. With an IC50 value of 115.8 μM, L-arginine inhibited L-homoarginine uptake. Conversely, L-arginine only exhibited a partial inhibitory effect on ADMA uptake. Taken together, our data indicate that b0,+AT-rBAT may contribute to the differential renal handling of L-arginine, L-homoarginine, and ADMA.

03 Mar 2025·Inorganic Chemistry

Structural Changes at the Zinc Active Site of ACE2 on Binding the SARS-CoV-2 Spike Protein Receptor Binding Domain

Article

Author: Cotelesage, Julien J. H. ; Latimer, Matthew ; Cygler, Miroslaw ; Kroll, Thomas ; Sokaras, Dimosthenis ; Grishin, Andrey ; Vogt, Linda I. ; George, Graham N. ; Dolgova, Natalia V. ; Pickering, Ingrid J. ; Qureshi, Muhammad

The causative agent of Covid-19 is the SARS-CoV-2 virus. Initiation of cell entry by SARS-CoV-2 is critically dependent upon binding of the SARS-CoV-2 spike protein to angiotensin-converting enzyme 2 (ACE2, EC 3.4.17.23). The mechanism of binding of the SARS-CoV-2 spike receptor binding domain to ACE2 is among the most intensively studied infection mechanisms of any pathogen, including a very large number of structural studies. ACE2 is a membrane-associated zinc carboxypeptidase, comprising three domains, the protease domain, a neck domain, and a membrane-spanning α-helical domain. In addition to its role as a carboxypeptidase, ACE2 is also a chaperone for a Na⁺-amino acid cotransporter called B⁰AT1, and in the presence of B⁰AT1, full-length ACE2 forms dimers. Most studies to date related to Covid-19 have employed just the ACE2 protease domain and have neglected any possible roles of the Zn²⁺-containing ACE2 active site. We show here that ACE2, including the neck domain in addition to the protease domain (and in the absence of B⁰AT1), is dimeric and shows distinctive allostery in its catalytic activity. In contrast, the intensively studied protease domain is monomeric and shows no allostery. Binding of the spike receptor binding domain (RBD) to dimeric ACE2 eliminates its allostery. X-ray absorption spectroscopy of Zn²⁺ ACE2 shows distinctive changes in the active site structure upon binding of spike RBD but only in the dimeric form. Taken together, our results indicate that the Zn²⁺-containing active site exhibits a notable level of flexibility and that the dimeric form of ACE2, including both protease and neck domains, likely presents a superior model for the study of ACE2-spike interactions than the monomeric ACE2.

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SLC7A9

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