Taurine and β-alanine transport in an established human kidney cell line derived from the proximal tubule

Jessen, Henrik

doi:10.1016/0005-2736(94)90201-1

Cited by 37 publications

(28 citation statements)

References 25 publications

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“…Most of these studies concluded that taurine and ß-alanine are transported via the common transporter specific to ß-amino acids [4,5,25]. In neurons and astrocytes [6], and cultured glioma cells [26], ß-alanine competitively interacts with the transport system for taurine.…”

Section: Discussionmentioning

confidence: 99%

“…The transport of ß-amino acids in Ehrlich cells has been studied principally by Christensen [3]. Some later studies showed that ß-alanine and taurine share a common transport system, the so-called ß-amino acid transport system, in various tissues [4,5]. The study of transport mechanism of ß-alanine in brain was restricted in neurons, astrocytes or synaptosomal membrane vesicles [6,7].…”

Section: Introductionmentioning

confidence: 99%

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Brain‐to‐blood active transport of β‐alanine across the blood–brain barrier

et al. 1997

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A high-affinity antiluminal uptake system for ß-alanine was demonstrated in primary cultured bovine brain capillary endothelial cells (BCEC) for which K, is 66.9 μΜ. β-alanine uptake was energy-, sodium-and chloride ion-dependent. ß-amino acids strongly inhibited the uptake, while a-and γ-amino acids had a little or no inhibitory effect. In ATP-depleted cells, the uptake was stimulated by preloading ß-alanine or taurine but not by L-leucine. These results suggest that ß-alanine is actively transported across the antiluminal membrane of BCECs that is common to ß-amino acids. The system may function for the efflux from the brain to blood.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Brain‐to‐blood active transport of β‐alanine across the blood–brain barrier

et al. 1997

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“…It has been shown before that IHKE-1 cells can transport AIB [5,6] and -alanine as well as taurine [4], indicating the existence of the A or imino as well as the system. Our data favor the existence of the imino system since AIB was added to the apical membrane and strongly depolarized the V m of IHKE-1 cells.…”

Section: Namentioning

confidence: 99%

“…In several uptake studies it was proven that these cells are able to transport neutral α-and -AA, taurine and -alanine as well as the non-metabolizable neutral α-aminoisobutyric acid (AIB) [4][5][6]. The aim of this study was to further characterize the different AA transport systems in these cells using the patch-clamp technique to monitor changes in membrane voltage (V m ).…”

Section: Introductionmentioning

confidence: 99%

Na+ -Dependent and -Independent Amino Acid Transport Systems in Immortalized Human Kidney Epithelial Cells Derived from the Proximal Tubule

Hirsch

Gonska

Waldegger

et al. 1998

Kidney Blood Press Res

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In the proximal tubule Na⁺-dependent (SDAT) and Na⁺-independent (SIAT) amino acid (AA) transporters are present. The effects of neutral, basic, and acidic AA on membrane voltage (V_m) of immortalized human kidney epithelial (IHKE-1) cells derived from the proximal tubule were examined using the slow whole-cell patch-clamp technique. In the presence of Na⁺ AA depolarized V_m in a concentration-dependent manner (0.05–5 mM) with Asp = Arg = Glu =2Cys < Pro = Leu < Phe = AIB = Ala = Pro = Asn < Gly. In the absence of extracellular Na⁺ a decreased depolarization was seen with most neutral AA (Ala, Pro, Asn, Gly, Phe, and Leu), and the depolarization was increased with Asp, Glu, Arg, and 2Cys (1 mM each). In the absence of Na⁺ and a reduction in Cl^– (5 mM) the depolarization by Arg was reduced. Unlike that predicted for transport by system b^0,+ which exchanges neutral against dibasic amino acids, Leu does not hyperpolarize but depolarize V_m of IHKE-1 cells in the absence of extracellular Na⁺. After removal of Na⁺ (0 mM) and a reduction in Cl^– (5 mM) in the extracellular solution, Leu or Glu hyperpolarized V_m, indicating that IHKE-1 cells possess two different SIAT systems, one Cl^–-independent and similar to system b^0,+ and one novel Cl^–-dependent system, which might be a Cl^–/AA exchanger and can be blocked by the Cl^–-channel blockers 5-nitro-2-(3-phenylpropylamino)-benzoate (10 μM) and 4,4′-diisothiocyanostibene-2,2′-disulfonic acid (50 μM). B system-related AA transporters might be responsible for the C^–-independent SIAT, since we were able to detect its signal by Northern blot analysis.

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“…β-Alanine is the rate limiting amino acid in the biosynthesis of these histidinecontaining peptides, but can be provided by oral intake. β-Alanine is internalized by cells via the taurine transporter in order to be synthesized into carnosine or anserine for subsequent intracellular storage [10,11]. Carnosine is synthesized by the enzyme carnosine synthase (CARNS) [12].…”

Section: Introductionmentioning

confidence: 99%

Tissue Storage of Dipeptides as Protein Guards Against Oxidative Injury in Patients with Type 2 Diabetes and Its Microvascular Complications

Heer

2015

ICPJL

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Histidine-containing dipeptides such as carnosine (β-alanine-L-histidine) and anserine (β-alanine-L-methyl histidine) are not incorporated into proteins; instead, they are stored in peripheral skeletal muscle and other organs, including the kidney, retina, and myocardium. Carnosine has several protective functions in health and disease state. This mini review provides a current overview of the knowledge of the histidine containing dipeptides in disease accompanied by oxidative stress like diabetes and diabetic microvascular complications. It also highlights the performed experimental studies of histidine-containing dipeptides in relation to tissue damage related to (non-invasive) human studies. Finally, it describes future perspectives of the therapeutic use of histidine-containing dipeptides in health and disease.

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Taurine and β-alanine transport in an established human kidney cell line derived from the proximal tubule

Cited by 37 publications

References 25 publications

Brain‐to‐blood active transport of β‐alanine across the blood–brain barrier

Brain‐to‐blood active transport of β‐alanine across the blood–brain barrier

Na+ -Dependent and -Independent Amino Acid Transport Systems in Immortalized Human Kidney Epithelial Cells Derived from the Proximal Tubule

Tissue Storage of Dipeptides as Protein Guards Against Oxidative Injury in Patients with Type 2 Diabetes and Its Microvascular Complications

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