scholarly journals FXYD protein isoforms differentially modulate human Na/K pump function

2020 ◽  
Vol 152 (12) ◽  
Author(s):  
Dylan J. Meyer ◽  
Sharan Bijlani ◽  
Marilina de Sautu ◽  
Kerri Spontarelli ◽  
Victoria C. Young ◽  
...  
Keyword(s):  
Xenopus Oocytes ◽  
Surface Expression ◽  
Protein Isoforms ◽  
Turnover Rates ◽  
Drastic Reduction ◽  
Secondary Active Transport ◽  
Apparent Affinity ◽  
Electrode Voltage ◽  
Electrical Signaling ◽  
Intracellular Ions

Tight regulation of the Na/K pump is essential for cellular function because this heteromeric protein builds and maintains the electrochemical gradients for Na+ and K+ that energize electrical signaling and secondary active transport. We studied the regulation of the ubiquitous human α1β1 pump isoform by five human FXYD proteins normally located in muscle, kidney, and neurons. The function of Na/K pump α1β1 expressed in Xenopus oocytes with or without FXYD isoforms was evaluated using two-electrode voltage clamp and patch clamp. Through evaluation of the partial reactions in the absence of K+ but presence of Na+ in the external milieu, we demonstrate that each FXYD subunit alters the equilibrium between E1P(3Na) and E2P, the phosphorylated conformations with Na+ occluded and free from Na+, respectively, thereby altering the apparent affinity for Na+. This modification of Na+ interaction shapes the small effects of FXYD proteins on the apparent affinity for external K+ at physiological Na+. FXYD6 distinctively accelerated both the Na+-deocclusion and the pump-turnover rates. All FXYD isoforms altered the apparent affinity for intracellular Na+ in patches, an effect that was observed only in the presence of intracellular K+. Therefore, FXYD proteins alter the selectivity of the pump for intracellular ions, an effect that could be due to the altered equilibrium between E1 and E2, the two major pump conformations, and/or to small changes in ion affinities that are exacerbated when both ions are present. Lastly, we observed a drastic reduction of Na/K pump surface expression when it was coexpressed with FXYD1 or FXYD6, with the former being relieved by injection of PKA's catalytic subunit into the oocyte. Our results indicate that a prominent effect of FXYD1 and FXYD6, and plausibly other FXYDs, is the regulation of Na/K pump trafficking.

scholarly journals Identification of renal transporters involved in sulfate excretion in marine teleost fish

2009 ◽  
Vol 297 (6) ◽  
pp. R1647-R1659 ◽  
Author(s):  
Akira Kato ◽  
Min-Hwang Chang ◽  
Yukihiro Kurita ◽  
Tsutomu Nakada ◽  
Maho Ogoshi ◽  
...  
Keyword(s):  
Xenopus Oocytes ◽  
Proximal Tubules ◽  
Border Region ◽  
Marine Teleost ◽  
Renal Transporters ◽  
Electrode Voltage ◽  
Cloned Cdna ◽  
Cdna Fragments ◽  
Immunohistochemical Analyses ◽  
Marine Teleost Fish

Sulfate (SO42−) is the second most abundant anion in seawater (SW), and excretion of excess SO42− from ingested SW is essential for marine fish to survive. Marine teleosts excrete SO42− via the urine produced in the kidney. The SO42− transporter that secretes and concentrates SO42− in the urine has not previously been identified. Here, we have identified and characterized candidates for the long-sought transporters. Using sequences from the fugu database, we have cloned cDNA fragments of all transporters belonging to the Slc13 and Slc26 families from mefugu ( Takifugu obscurus ). We compared Slc13 and Slc26 mRNA expression in the kidney between freshwater (FW) and SW mefugu. Among 14 clones examined, the expression of a Slc26a6 paralog (mfSlc26a6A) was the most upregulated (30-fold) in the kidney of SW mefugu. Electrophysiological analyses of Xenopus oocytes expressing mfSlc26a6A, mfSlc26a6B, and mouse Slc26a6 (mSlc26a6) demonstrated that all transporters mediate electrogenic Cl−/SO42−, Cl−/oxalate2−, and Cl−/ nHCO3− exchanges and electroneutral Cl−/formate− exchange. Two-electrode voltage-clamp experiments demonstrated that the SO42−-elicited currents of mfSlc26a6A is quite large (∼35 μA at +60 mV) and 50- to 200-fold higher than those of mfSlc26a6B and mSlc26a6. Conversely, the currents elicited by oxalate and HCO3− are almost identical among mfSlc26a6A, mfSlc26a6B, and mSlc26a6. Kinetic analysis revealed that mfSlc26a6A has the highest SO42− affinity as well as capacity. Immunohistochemical analyses demonstrated that mfSlc26a6A localizes to the apical (brush-border) region of the proximal tubules. Together, these findings suggest that mfSlc26a6A is the most likely candidate for the major apical SO42− transporter that mediates SO42− secretion in the kidney of marine teleosts.

scholarly journals Extracellular Hco3− Dependence of Electrogenic Na/Hco3 Cotransporters Cloned from Salamander and Rat Kidney

2000 ◽  
Vol 115 (5) ◽  
pp. 533-546 ◽  
Author(s):  
Irina I. Grichtchenko ◽  
Michael F. Romero ◽  
Walter F. Boron
Keyword(s):  
Membrane Potential ◽  
Voltage Clamp ◽  
Xenopus Oocytes ◽  
Rat Kidney ◽  
Outward Current ◽  
Membrane Vesicles ◽  
Disulfonic Acid ◽  
Ambystoma Tigrinum ◽  
Ph Titration ◽  
Electrode Voltage

We studied the extracellular [HCOabstract 3 −] dependence of two renal clones of the electrogenic Na/HCO3 cotransporter (NBC) heterologously expressed in Xenopus oocytes. We used microelectrodes to measure the change in membrane potential (ΔVm) elicited by the NBC cloned from the kidney of the salamander Ambystoma tigrinum (akNBC) and by the NBC cloned from the kidney of rat (rkNBC). We used a two-electrode voltage clamp to measure the change in current (ΔI) elicited by rkNBC. Briefly exposing an NBC-expressing oocyte to HCOabstract 3 −/CO2 (0.33–99 mM HCOabstract 3−, pHo 7.5) elicited an immediate, DIDS (4,4-diisothiocyanatostilbene-2,2-disulfonic acid)-sensitive and Na+-dependent hyperpolarization (or outward current). In ΔVm experiments, the apparent Km for HCOabstract 3− of akNBC (10.6 mM) and rkNBC (10.8 mM) were similar. However, under voltage-clamp conditions, the apparent Km for HCOabstract 3− of rkNBC was less (6.5 mM). Because it has been reported that SOabstract 3=/HSO abstract 3− stimulates Na/HCO3 cotransport in renal membrane vesicles (a result that supports the existence of a COabstract 3= binding site with which SOabstract 3= interacts), we examined the effect of SOabstract 3=/HSO abstract 3− on rkNBC. In voltage-clamp studies, we found that neither 33 mM SOabstract 4= nor 33 mM SOabstract 3 =/HSOabstract 3− substantially affects the apparent Km for HCO abstract 3−. We also used microelectrodes to monitor intracellular pH (pHi) while exposing rkNBC-expressing oocytes to 3.3 mM HCOabstract 3 −/0.5% CO2. We found that SO abstract 3=/HSOabstract 3 − did not significantly affect the DIDS-sensitive component of the pHi recovery from the initial CO2 -induced acidification. We also monitored the rkNBC current while simultaneously varying [CO2]o, pHo, and [COabstract 3=]o at a fixed [HCOabstract 3−]o of 33 mM. A Michaelis-Menten equation poorly fitted the data expressed as current versus [COabstract 3=]o . However, a pH titration curve nicely fitted the data expressed as current versus pHo. Thus, rkNBC expressed in Xenopus oocytes does not appear to interact with SOabstract 3 =, HSOabstract 3−, or COabstract 3=.

scholarly journals pH sensitivity of ammonium transport by Rhbg

2010 ◽  
Vol 299 (6) ◽  
pp. C1386-C1397 ◽  
Author(s):  
Nazih L. Nakhoul ◽  
Solange M. Abdulnour-Nakhoul ◽  
Eric Schmidt ◽  
Rienk Doetjes ◽  
Edd Rabon ◽  
...  
Keyword(s):  
Xenopus Oocytes ◽  
Ph Sensitivity ◽  
Ammonium Transport ◽  
Amine Hydrochloride ◽  
Membrane Glycoprotein ◽  
Induced Current ◽  
Inward Current ◽  
Gas Channel ◽  
Methyl Amine ◽  
Electrode Voltage

Rhbg is a membrane glycoprotein that is involved in NH3/NH4+ transport. Several models have been proposed to describe Rhbg, including an electroneutral NH4+/H+ exchanger, a uniporter, an NH4+ channel, or even a gas channel. In this study, we characterized the pH sensitivity of Rhbg expressed in Xenopus oocytes. We used two-electrode voltage clamp and ion-selective microelectrodes to measure NH4+-induced [and methyl ammonium (MA+)] currents and changes in intracellular pH (pHi), respectively. In oocytes expressing Rhbg, 5 mM NH4Cl (NH3/NH4+) at extracellular pH (pHo) of 7.5 induced an inward current, decreased pHi, and depolarized the cell. Raising pHo to 8.2 significantly enhanced the NH4+-induced current and pHi changes, whereas decreasing bath pH to 6.5 inhibited these changes. Lowering pHi (decreased by butyrate) also inhibited the NH4+-induced current and pHi decrease. In oocytes expressing Rhbg, 5 mM methyl amine hydrochloride (MA/MA+), often used as an NH4Cl substitute, induced an inward current, a pHi increase (not a decrease), and depolarization of the cell. Exposing the oocyte to MA/MA+ at alkaline bath pH (8.2) enhanced the MA+-induced current, whereas lowering bath pH to 6.5 inhibited the MA+ current completely. Exposing the oocyte to MA/MA+ at low pHi abolished the MA+-induced current and depolarization; however, pHi still increased. These data indicate that 1) transport of NH4+ and MA/MA+ by Rhbg is pH sensitive; 2) electrogenic NH4+ and MA+ transport are stimulated by alkaline pHo but inhibited by acidic pHi or pHo; and 3) electroneutral transport of MA by Rhbg is likely but is less sensitive to pH changes.

Inhibitory Effect of Glucocorticoids on Human-cloned 5-hydroxytryptamine3AReceptor Expressed in Xenopus  Oocytes

2004 ◽  
Vol 101 (3) ◽  
pp. 660-665 ◽  
Author(s):  
Takahiro Suzuki ◽  
Masahiro Sugimoto ◽  
Hideki Koyama ◽  
Takashi Mashimo ◽  
Ichiro Uchida
Keyword(s):  
Xenopus Oocytes ◽  
Inhibitory Concentration ◽  
Inhibitory Effect ◽  
Combined Effect ◽  
Induced Current ◽  
Direct Effects ◽  
Receptor Antagonists ◽  
Electrode Voltage ◽  
Direct Inhibitory Effect ◽  
Voltage Clamping

Background Methylprednisolone, dexamethasone, and other glucocorticoids have been found effective against nausea and vomiting induced by chemotherapy and surgery. Although the specific 5-hydroxytriptamine3 (5-HT3) receptor antagonists such as ondansetron and ramosetron are used as antiemetics, reports show that the use of 5-HT3 receptor antagonists with some glucocorticoids brings additional effects. Glucocorticoids are reported to be antiemetic. The effect of glucocorticoids on 5-HT3 receptor, however, has not been well characterized. This study was designed to examine whether dexamethasone and methylprednisolone had direct effects on human-cloned 5-HT3A receptor expressed in Xenopus oocytes. Methods Homomeric human-cloned 5-HT3A receptor was expressed in Xenopus oocytes. The authors used the two-electrode voltage-clamping technique to study the effect of methylprednisolone and dexamethasone on 5-HT-induced current. Results Both dexamethasone and methylprednisolone concentration-dependently attenuated 5-HT-induced current. Dexamethasone inhibited 2 microm 5-HT-induced current, which was equivalent to EC30 concentration for 5-HT3A receptor, with an inhibitory concentration 50% of 5.29 +/- 1.02 microm. Methylprednisolone inhibited 2 microm 5-HT-induced current with an inhibitory concentration 50% of 1.07 +/- 0.15 mm. The mode of inhibition with either dexamethasone or methylprednisolone was noncompetitive and voltage-independent. When administered together with the 5-HT3 receptor antagonists, ramosetron or metoclopramide, both glucocorticoids showed an additive effect on 5-HT3 receptor. Conclusion The glucocorticoids had a direct inhibitory effect on 5-HT3 receptors. The combined effect of glucocorticoids and the 5-HT3 receptor antagonists seems additive.

scholarly journals Calcium Current Activated by Depletion of Calcium Stores in Xenopus Oocytes

1997 ◽  
Vol 109 (6) ◽  
pp. 703-715 ◽  
Author(s):  
Yong Yao ◽  
Roger Y. Tsien
Keyword(s):  
Xenopus Oocytes ◽  
Voltage Dependence ◽  
Calcium Stores ◽  
Kinase C ◽  
Electrode Voltage ◽  
Activation Mechanisms ◽  
Electrophysiological Characterization ◽  
Inwardly Rectifying ◽  
A Current

Ca2+ currents activated by depletion of Ca2+ stores in Xenopus oocytes were studied with a two-electrode voltage clamp. Buffering of cytosolic Ca2+ with EGTA and MeBAPTA abolished ICl(Ca) and unmasked a current in oocytes that was activated by InsP3 or ionomycin in minutes and by thapsigargin or the chelators themselves over hours. At −60 mV in 10 mM extracellular CaCl2, the current was typically around −90 or −160 nA in oocytes loaded with EGTA or MeBAPTA, respectively. This current was judged to be a Ca2+-selective current for the following reasons: (a) it was inwardly rectifying and reversed at membrane potentials usually more positive than +40 mV; (b) it was dependent on extracellular [CaCl2] with Km = 11.5 mM; (c) it was highly selective for Ca2+ against monovalent cations Na+ and K+, because replacing Na+ and K+ by N-methyl-d-glucammonium did not reduce the amplitude or voltage dependence of the current significantly; and (d) Ca2+, Sr2+, and Ba2+ currents had similar instantaneous conductances, but Sr2+ and Ba2+ currents appeared to inactivate more strongly than Ca2+. This Ca2+ current was blocked by metal ions with the following potency sequence: Mg2+ << Ni2+ ≈ Co2+ ≈ Mn2+ < Cd2+ << Zn2+ << La3+. It was also inhibited by niflumic acid, which is commonly used to block ICl(Ca). PMA partially inhibited the Ca2+ current, and this effect was mostly abolished by calphostin C, indicating that the Ca2+ current is sensitive to protein kinase C. These results are the first detailed electrophysiological characterization of depletion-activated Ca2+ current in nondialyzed cells. Because exogenous molecules and channels are easy to introduce into oocytes and the distortions in measuring ICl(Ca) can now be bypassed, oocytes are now a superior system in which to analyze the activation mechanisms of capacitative Ca2+ influx.

scholarly journals Regulation of Maximal Open Probability Is a Separable Function of Cavβ Subunit in L-type Ca2+ Channel, Dependent on NH2 Terminus of α1C (Cav1.2α)

2006 ◽  
Vol 128 (1) ◽  
pp. 15-36 ◽  
Author(s):  
Nataly Kanevsky ◽  
Nathan Dascal
Keyword(s):  
Initial Segment ◽  
Xenopus Oocytes ◽  
Surface Expression ◽  
Amino Acid Residues ◽  
Open Probability ◽  
Separable Function ◽  
Voltage Dependent ◽  
Cav1.2 Channels ◽  
Channel Dependent ◽  
Necessary And Sufficient

β subunits (Cavβ) increase macroscopic currents of voltage-dependent Ca2+ channels (VDCC) by increasing surface expression and modulating their gating, causing a leftward shift in conductance–voltage (G-V) curve and increasing the maximal open probability, Po,max. In L-type Cav1.2 channels, the Cavβ-induced increase in macroscopic current crucially depends on the initial segment of the cytosolic NH2 terminus (NT) of the Cav1.2α (α1C) subunit. This segment, which we term the “NT inhibitory (NTI) module,” potently inhibits long-NT (cardiac) isoform of α1C that features an initial segment of 46 amino acid residues (aa); removal of NTI module greatly increases macroscopic currents. It is not known whether an NTI module exists in the short-NT (smooth muscle/brain type) α1C isoform with a 16-aa initial segment. We addressed this question, and the molecular mechanism of NTI module action, by expressing subunits of Cav1.2 in Xenopus oocytes. NT deletions and chimeras identified aa 1–20 of the long-NT as necessary and sufficient to perform NTI module functions. Coexpression of β2b subunit reproducibly modulated function and surface expression of α1C, despite the presence of measurable amounts of an endogenous Cavβ in Xenopus oocytes. Coexpressed β2b increased surface expression of α1C approximately twofold (as demonstrated by two independent immunohistochemical methods), shifted the G-V curve by ∼14 mV, and increased Po,max 2.8–3.8-fold. Neither the surface expression of the channel without Cavβ nor β2b-induced increase in surface expression or the shift in G-V curve depended on the presence of the NTI module. In contrast, the increase in Po,max was completely absent in the short-NT isoform and in mutants of long-NT α1C lacking the NTI module. We conclude that regulation of Po,max is a discrete, separable function of Cavβ. In Cav1.2, this action of Cavβ depends on NT of α1C and is α1C isoform specific.

scholarly journals FXYD3 (Mat-8), a New Regulator of Na,K-ATPase

2005 ◽  
Vol 16 (5) ◽  
pp. 2363-2371 ◽  
Author(s):  
Gilles Crambert ◽  
Ciming Li ◽  
Dirk Claeys ◽  
Käthi Geering
Keyword(s):  
Membrane Proteins ◽  
Transport Properties ◽  
Signal Peptide ◽  
Xenopus Oocytes ◽  
Type I ◽  
Mucous Cells ◽  
Β Subunit ◽  
Apparent Affinity ◽  
Shared Function

Four of the seven members of the FXYD protein family have been identified as specific regulators of Na,K-ATPase. In this study, we show that FXYD3, also known as Mat-8, is able to associate with and to modify the transport properties of Na,K-ATPase. In addition to this shared function, FXYD3 displays some uncommon characteristics. First, in contrast to other FXYD proteins, which were shown to be type I membrane proteins, FXYD3 may have a second transmembrane-like domain because of the presence of a noncleavable signal peptide. Second, FXYD3 can associate with Na,K- as well as H,K-ATPases when expressed in Xenopus oocytes. However, in situ (stomach), FXYD3 is associated only with Na,K-ATPase because its expression is restricted to mucous cells in which H,K-ATPase is absent. Coexpressed in Xenopus oocytes, FXYD3 modulates the glycosylation processing of the β subunit of X,K-ATPase dependent on the presence of the signal peptide. Finally, FXYD3 decreases both the apparent affinity for Na+ and K+ of Na,K-ATPase.

Regulatory interactions of N1303K-CFTR and ENaC in Xenopus oocytes: evidence that chloride transport is not necessary for inhibition of ENaC

2007 ◽  
Vol 292 (4) ◽  
pp. C1553-C1561 ◽  
Author(s):  
Laurence Suaud ◽  
Wusheng Yan ◽  
Marcelo D. Carattino ◽  
Amal Robay ◽  
Thomas R. Kleyman ◽  
...  
Keyword(s):  
Xenopus Oocytes ◽  
Chloride Transport ◽  
Nucleotide Binding ◽  
Functional Expression ◽  
Surface Expression ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Regulatory Interactions ◽  
Low Levels ◽  
Cystic Fibrosis Transmembrane

Regulatory interactions of the cystic fibrosis transmembrane conductance regulator (CFTR) and the epithelial Na+ channel (ENaC) are readily apparent in Xenopus oocytes. However, the mechanism underlying these interactions remains controversial. CFTR's first nucleotide binding fold (NBD-1) may be important in these interactions, as dysfunctional CFTRs containing mutations within NBD-1, such as ΔF508 and G551D, lack such functional interactions with murine ENaC (mENaC). We hypothesized that a dysfunctional CFTR containing a non-NBD-1 mutation would retain regulatory interactions with mENaC and tested this hypothesis for N1303K-CFTR, where the mutation is located in CFTR's second nucleotide binding fold (NBD-2). cRNA for αβγ-mENaC and N1303K-CFTR was injected separately or together into Xenopus oocytes. ENaC and CFTR functional expression was assessed by two-electrode voltage clamp. Injection of N1303K (class II trafficking mutation) yielded low levels of CFTR function on activation with forskolin and 3-isobutyl-1-methylxanthine (IBMX). In coinjected oocytes, N1303K did not alter mENaC functional expression or surface expression before activation of N1303K. This is similar to our prior observations with ΔF508. However, unlike our observations with ΔF508, activation of N1303K acutely decreased mENaC functional and surface expression, and N1303K currents were enhanced by coinjection of mENaC. Furthermore, genistein only mildly enhanced the functional expression of N1303K-CFTR and did not improve regulation of ENaC by N1303K-CFTR. These data suggest that a structurally and functionally intact CFTR NBD-1 in activated CFTR can regulate mENaC surface expression independent of Cl− transport in Xenopus oocytes.

scholarly journals Revisiting the functional properties of NPF6.3/NRT1.1/CHL1 in xenopus oocytes

2018 ◽  
Author(s):  
Mélanie Noguero ◽  
Sophie Léran ◽  
Eléonore Bouguyon ◽  
Chantal Brachet ◽  
Pascal Tillard ◽  
...  
Keyword(s):  
Transport Properties ◽  
Xenopus Oocytes ◽  
Nitrate Concentration ◽  
Functional Characterization ◽  
Nitrate Transport ◽  
Experimental Conditions ◽  
Point Mutant ◽  
Electrode Voltage ◽  
Nitrate Transporters

ABSTRACTWithin the Arabidopsis NPF proteins, most of the characterized nitrate transporters are low-affinity transporters, whereas the functional characterization of NPF6.3/NRT1.1 has revealed interesting transport properties: the transport of nitrate and auxin, the eletrogenicity of the nitrate transport and a dual-affinity transport behavior for nitrate depending on external nitrate concentration. However, some of these properties remained controversial and were challenged here. We functionally express WT NPF6.3/NRT1.1 and some of its mutant in Xenopus oocytes and used a combination of uptake experiments using 15N-labelled nitrate and two-electrode voltage-clamp. In our experimental conditions in xenopus oocytes, in the presence or in the absence of external chloride, NPF6.3/NRT1.1 behaves as a non-electrogenic and pure low-affinity transporter. Moreover, further functional characterization of a NPF6.3/NRT1.1 point mutant, P492L, allowed us to hypothesize that NPF6.3/NRT1.1 is regulated by internal nitrate concentration and that the internal perception site involves the P492 residue.

Identification of a nucleoside/nucleobase transporter from Plasmodium falciparum, a novel target for anti-malarial chemotherapy

2000 ◽  
Vol 349 (1) ◽  
pp. 67-75 ◽  
Author(s):  
Marie D. PARKER ◽  
Ralph J. HYDE ◽  
Sylvia Y. M. YAO ◽  
Louisa MCROBERT ◽  
Carol E. CASS ◽  
...  
Keyword(s):  
Xenopus Oocytes ◽  
De Novo ◽  
Functional Expression ◽  
Nucleoside Transporters ◽  
Pyrimidine Nucleoside ◽  
Parasite Protein ◽  
Apparent Affinity ◽  
Equilibrative Nucleoside Transporters ◽  
Novel Target ◽  
Membrane Spanning

Plasmodium, the aetiologic agent of malaria, cannot synthesize purines de novo, and hence depends upon salvage from the host. Here we describe the molecular cloning and functional expression in Xenopus oocytes of the first purine transporter to be identified in this parasite. This 422-residue protein, which we designate PfENT1, is predicted to contain 11 membrane-spanning segments and is a distantly related member of the widely distributed eukaryotic protein family the equilibrative nucleoside transporters (ENTs). However, it differs profoundly at the sequence and functional levels from its homologous counterparts in the human host. The parasite protein exhibits a broad substrate specificity for natural nucleosides, but transports the purine nucleoside adenosine with a considerably higher apparent affinity (Km 0.32±0.05 mM) than the pyrimidine nucleoside uridine (Km 3.5±1.1 mM). It also efficiently transports nucleobases such as adenine (Km 0.32±0.10 mM) and hypoxanthine (Km 0.41±0.1 mM), and anti-viral 3ʹ-deoxynucleoside analogues. Moreover, it is not sensitive to classical inhibitors of mammalian ENTs, including NBMPR {6-[(4-nitrobenzyl)thio]-9-β-D-ribofuranosylpurine, or nitrobenzylthioinosine} and the coronary vasoactive drugs, dipyridamole, dilazep and draflazine. These unique properties suggest that PfENT1 might be a viable target for the development of novel anti-malarial drugs.

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