Specificity and metal sensitivity of renal amino acid transport

Foulkes, E. C.; Gieske, T. H.

doi:10.1016/0005-2736(73)90206-x

Cited by 45 publications

(4 citation statements)

References 4 publications

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“…Interestingly, this system is present in hepatoma cells but does not contribute to the influx ofbasic amino acids across the plasma membrane of the normal hepatocyte . Furthermore, although the peritubular epithelium of the rabbit kidney appears to transport basic amino acids via a selective cationic transport system (Foulkes & Gieske, 1973;Silbernagl, Foulkes & Deetjen, 1975) it remains to be established whether this carrier resembles system y+. We conclude that the salivary epithelium contains a distinct basolateral cationic amino acid transport system, system y+, which operates in parallel with the previously described systems ASC and L (Bustamante et al 1981 ;Mann & Yudilevich, 1984).…”

Section: Discussionmentioning

confidence: 99%

Characteristics of a cationic amino acid transport system in the basolateral membrane of the cat salivary epithelium.

Mann¹,

Wilson²,

Yudilevich³

1984

The Journal of Physiology

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SUMMARY1. The specificity and kinetics of L-lysine influx across the basolateral surface of the cat salivary epithelium have been investigated in the perfused cat submandibular gland using a high-resolution, paired-tracer dilution technique.2. L-lysine influx was measured at several different perfusate concentrations (0-05-2-5 mM) and was found to be saturable. A Michaelis-Menten analysis based on a single entry site gave a Km of 0 49 + 0-08 mm and a Vmax of 231 + 20 nmol/min. g.3. The uptake of L-lysine was highly stereospecific and markedly inhibited by L-arginine (0-25-2-5 mM). The inhibitor constant (Ki) was 0-23 mm, suggesting that the carrier had a greater affinity for L-arginine than L-lysine. 4. When the inhibitory effects of L-histidine (0-5-10 mM) were examined the K1, estimated at 10 mm, was 4-6 mm. Nine other neutral amino acids (L-alanine, L-serine, L-cysteine, glycine, L-proline, L-homoserine, L-leucine, L-phenylalanine and Lglutamine), and an acidic amino acid (L-aspartate) were also tested at 10 mm and, although several caused inhibition, the Ki was always at least 20 times higher than the measured Km for L-lysine. It is concluded the carrier is highly specific for the L-form of the basic amino acids. 5. The sodium dependence ofL-lysine influx was investigated over a range ofL-lysine concentrations (0 05-1 mM), and total removal of sodium from the perfusate had no effect on L-lysine influx.6. In the presence of sodium, L-homoserine, an amino acid not normally present in animal tissues, inhibited L-lysine influx (Ki = 13 mM). This inhibition was not observed in the absence of sodium, and contrasts with the observation that the inhibitory action of L-histidine was sodium independent. 7. The present data suggest that a specific cationic amino acid transport system is operative in the basolateral membrane of the cat salivary epithelium. The properties of this system appear to be similar to the system y+ which has been described in several other cell types. E. MANN, S. M. WILSON AND D. L. YUDILEVICH

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Section: Discussionmentioning

confidence: 99%

Characteristics of a cationic amino acid transport system in the basolateral membrane of the cat salivary epithelium.

Mann¹,

Wilson²,

Yudilevich³

1984

The Journal of Physiology

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“…In addition, since most of the GCs are highly positively charged at physiological pH due to the presence of several nitrogens, their binding to cytoplasmic components or sequestration in intracellular compartments might be facilitated. At present, it is not clear whether all GCs share common or specific carriers to accumulate in the cells as known for amino acids [10,22]. Arg and dimethylarginines use the Y + transporter, as does lysine [32].…”

Section: Discussionmentioning

confidence: 98%

Dehydration modifies guanidino compound concentrations in the different zones of the rat kidney

Levillain

Marescau²,

Possemiers³

et al. 2002

Pflügers Arch - Eur J Physiol

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Guanidino compounds (GCs) related to arginine (Arg) are unevenly distributed along the cortico-papillary axis of the rat kidney. Inasmuch as the concentration of alpha-keto-delta-guanidinovaleric acid (alpha-keto-delta-GVA), guanidinosuccinic acid (GSA), creatinine (CTN), gamma-guanidinobutyric acid (gamma-GBA) and methylguanidine (MG) increased steeply along the inner medulla in parallel to the urea and osmotic gradients, the question arose as to whether dehydration enhances their renal content and distribution. To examine this possibility, adult male rats were dehydrated by removing the drinking water for 24 or 48 h. The kidneys were sliced and cut in seven sections along the cortico-papillary axis. Twelve GCs were determined by liquid chromatography in each renal zone. Dehydration modified GC concentrations and regional distribution. The renal content of Arg, guanidine and MG was decreased while that of alpha-keto-delta-GVA, gamma-GBA, alpha- N-acetyl-arginine and homoarginine remained unchanged. In contrast, GSA, guanidinoacetic acid (GAA), creatine (CT), CTN and beta-guanidinopropionic acid (beta-GPA) concentrations were enhanced significantly in different renal zones after 24 and 48 h dehydration. In addition, the tissue level of GCs supplying energy, such as CT and beta-GPA, the precursor of CT (GAA) and its metabolite (CTN) were enhanced under dehydration. Arg and CT account for 80-90% of the GCs located in the renal cortex. Variations of some GC levels under dehydration may modify enzyme activities, renal metabolism and cell function.

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“…Heterogeneity ofneutral amino acid transport has also been observed in basolateral cell membranes of other epithelia. In vesicles isolated from rat intestinal basolateral membranes (Mircheffet al 1980) uptake ofL-alanine was saturable, stereospecific and, unlike the salivary epithelium, mediated by Systems ASC, A and L. Transport studies in the intact kidney (Foulkes & Gieske, 1973;Silbernagl et al 1975), the isolated perfused proximal tubule (see Schafer & Barfuss, 1980) and a renal LLC-PKl cell line (Rabito & Karish, 1982) demonstrated that several basolateral carrier systems mediate the uptake of neutral amino acids. Interestingly Sytem ASC may be particularly sensitive to inhibition by amino acids which do not serve as substrates SALI VARY GLAND AMINO ACID TRANSPORT (Kilberg et al 1981;Handlogten et al 1981).…”

Section: Discussionmentioning

confidence: 99%

Discrimination of parallel neutral amino acid transport systems in the basolateral membrane of cat salivary epithelium.

Mann¹,

Yudilevich²

1984

The Journal of Physiology

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SUMMARY1. Transport of short-chain and long-chain neutral amino acids across the basolateral membrane of the epithelium in the perfused cat salivary gland has been studied using a rapid (< 30 s) single circulation paired-tracer dilution technique. Amino acid uptake was measured by comparing the venous dilution profiles for a tritiated amino acid and D-[14C]mannitol (extracellular reference) following a bolus intra-arterial injection of a mixture containing both molecules. Unidirectional influx (v) was estimated from the maximal tracer uptake (Umax), the perfusate flow (F) and the perfusate amino acid concentration (Ca):2. L-alanine influx was saturable and apparently mediated by a single entry system (Km = 083+011mM and VmaX = 655+32 nmol/min. g). These kinetic constants were considerably lower than our previously reported values for L-phenylalanine:Km= 6-4 mM and Vmax = 1719 nmol/min . g. 3.In cross-inhibition experiments performed over a wide range of concentrations (0-05-24 mM), influx of L-alanine and L-phenylalanine could be further discriminated, since both L-phenylalanine (Ki = 22 mM) and L-alanine (Ki = 19 mM) behaved as poor competitors.4. Removal of Na+ from the perfusate resulted in a selective inhibition of L-alanine and L-serine influx, whereas influx of the long-chain neutral amino acids L-leucine, L-phenylalanine and L-tryptophan remained unaffected.5. Although prolonged perfusion of glands with dinitrophenol (0-8 mm for 20-30 min) caused a variable but net inhibition of unidirectional uptake, it markedly enhanced the tracer efflux of L-leucine, L-phenylalanine, L-tyrosine and the basic amino acid L-lysine.6. It appears that at least two separate neutral amino acid transport systems are operative at the blood-tissue interface of the salivary epithelium: (i) a Na+-dependent alanine-serine-cysteine preferring type of carrier exhibiting a high affinity for amino acids with short, polar or linear side chains and (ii) a Na+-independent leucine preferring type of carrier selective for large neutral amino acids. E. MANN AND D. L. YUDILEVICH

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Specificity and metal sensitivity of renal amino acid transport

Cited by 45 publications

References 4 publications

Characteristics of a cationic amino acid transport system in the basolateral membrane of the cat salivary epithelium.

Characteristics of a cationic amino acid transport system in the basolateral membrane of the cat salivary epithelium.

Dehydration modifies guanidino compound concentrations in the different zones of the rat kidney

Discrimination of parallel neutral amino acid transport systems in the basolateral membrane of cat salivary epithelium.

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