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  • Articles: DFG German National Licenses  (4)
  • Acetazolamide  (2)
  • Sodium Cotransport  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 377 (1978), S. 33-42 
    ISSN: 1432-2013
    Keywords: Renal tubule ; Phosphate transport ; Extracellular pH ; Intracellular pH ; Acetazolamide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Inorganic phosphate (Pi) transport was evaluated using the standing droplet method with simultaneous microperfusion of the peritubular capillaries. To evaluate rather small differences in Pi transport and to eliminate the influence of tubular heterogeneity, the technique of crossed paired samples was applied. 1. In chronic PTX rat changing the luminal or both luminal and peritubular pH by varying the HCO 3 − -concentration between 4 and 50 mmol/l at constant 5% CO2 had no influence on Pi transport. 2. If, however, bicarbonate was omitted from the perfusate and 2 mmol/l phosphate (pH 7.4) was the only buffer, Pi transport was decreased from the control. It was, however, further reduced when the perfusates were gased with 5% CO2 i. e. the starting pH was 5.6. 3. When the solutions contained HEPES buffer (25 mmol/l), Pi transport at pH 8 was much larger than at pH 6.0. 4. Raising the CO2 pressure from 35 to 70 mm Hg did not change the Pi transport when both perfusates had a HCO 3 − -concentration of 25 mmol/l. It reduced, however, the Pi transport, when the luminal perfusate had only 4 mmol/l bicarbonate. 5. Lowering the CO2 pressure from 38 to 7.6 mm Hg did hardly change the Pi transport when the luminal perfusate contained 4 mmol/l bicarbonate. It lowered, however, the Pi transport significantly when the luminal perfusate had 25 mmol/l bicarbonate. 6. Acetazolamide, 10−4 M, lowered the Pi transport when the luminal perfusate contained 4 or 25 mmol/l bicarbonate. At 4 mmol/l luminal HCO 3 − , raising thepCO2 to 228 mmol/l depressed Pi transport even more. At 25 mmol/l luminal bicarbonate, raising thepCO2 from 38 to 114 mm Hg reversed the acetazolamide inhibition of the Pi transport almost completely. The data indicate that luminal acidosis and intracellular alkalosis inhibits the transtubular Pi transport. A shift of the intracellular pH to a more alkaline value seems to be responsible for the inhibition of Pi transport by acetazolamide, while omission of buffer from the perfusate inhibits Pi transport by effecting an acidic luminal pH.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 395 (1982), S. 212-219 
    ISSN: 1432-2013
    Keywords: SITS ; Probenecid ; Phloretin ; Acetazolamide ; Lactate ; Renal tubule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The transport ofd-lactate across the epithelium of the late proximal convolution was investigated by two methods: 1. by measuring the zero net flux transtubular concentration difference (Δc tt,45s) and the permeability (P) ofd-lactate and calculating from both the transtubular active transport rate (J lac act ). 2. By measuring the 3.5 s efflux ofd-lactate from the tubular lumen, while blood was flowing through the capillaries. The 3.5 s efflux comprises two components, one going through the brush border (J lac bb ) and one going the paracellular pathway (J lac paracell =P lac·c lac lumen). Both,J lac act andJ lac bb ofd-lactate gave the sameK m 1.9 and 1.7 mmol/l and the same maximal transport rate 3.2 and 2.9 pmol cm−1 s−1. TheK i ofl-lactate tested againstJ lac act andJ lac bb ofd-lactate was also the same: 1.1 and 1.0 mmol/l. These data indicate that under our experimental conditions only the flux through the brush border seems to be rate limiting and thatd-lactate uses the same transport system asl-lactate. When Na+ was omitted from the perfusatesJ lac act disappeared completely, whileJ lac bb was reduced by 64%. These data reflect the Na+ dependence of thed-lactate transport through the brush border. Variation of intra-and extracellular pH by raisingpCO2, omitting HCO 3 − from the perfusates or adding acetazolamide had no effect on the transport ofd-lactate when α-ketoglutarate was used as fuel. However, when acetate was used as fuel, intracellular acidosis brought the reducedJ lac act back to the values obtained with α-ketoglutarate as fuel. It is suggested that this is an effect on a contraluminal transport step. Probenecid (5 mmol/l) and phloretin (0.25 mmol/l) inhibitedJ lac act significantly.J lac bb , however, was only inhibited by probenecid when acetate was used as fuel. These data indicate that both compounds act on thed-lactate exit at the contraluminal cell side, but that probenecid acts in addition at the luminal cell side. SITS (1 mmol/l) augmentedJ lac bb when acetate was used as fuel and is similar to the effect of lowering intracellular pH as described above. The SH reagents mersalyl (1.0 mmol/l) and maleolylglycine (1 mmol/l) did not influenceJ lac bb .
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2013
    Keywords: Hexose Transport ; Sodium Cotransport ; Kidney Tubules ; Sugar Specificity ; Kidney Micropuncture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary With the technique of stop flow microperfusion with simultaneous capillary perfusion, the zero net flux transtubular concentration difference (Δc) of labelled sugars was measured. The following sequence of Δc values, which are a measure for the active transtubular transport rate, were evaluated:d-glucose ≅β methyl-d-glycoside 〉α-methyl-d-glycoside 〉d-galactose 〉3-O-methyl-glucose 〉d-allose. When 10−4 M phlorrhizin was given in the luminal perfusate the Δc's dropped to zero (±8%). Δc-values in the same range i.e. indicating no active transport, were found for:l-glucose,d-mannose, 2-deoxy-d-glucose,d-fructose,d-glucosamine, 6-deoxy-d-galactose (=d-fucose),d-ribose and the reference polyalcohold-mannitol. Inhibition of thed-galactose δc was achieved by 15 mmol/l of the following sugars: α-methyl-d-glycoside ≅d-glucose ≅ 6-deoxy-d-glucose 〉3-O-methyl-d-glucose an no significant inhibition byd-xylose andd-mannose. Against Δc of α-methyl-d-glucose the following inhibitory potency was observed:d-glucose 〉6-deoxy-d-glucose 〉3-O-methyl-d-glucose ≅d-galactose 〉d-xylose and no inhibition byd-mannose. When the ambient sodium was replaced by choline, the Δc values of all actively transported sugars dropped toward zero. An analysis of the Na+ dependence of the α-methyl-d-glycoside transport revealed that the sodium dependence is of the affinity type i.e. that onlyK m increased with increasing Na+ concentration whileV max remained almost constant. From these data one can conclude: 1. The Crane specificity, i.e. that only the α-position of the OH-group on carbon atom 2 is essential, which was found for the intestinal hexose transport holds for the rat proximal kidney tubule, too. 2. The hexose transport system in the rat works only when Na+-ions are present. The sodium ions augment the affinity of the hexose transport system for the hexoses.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 351 (1974), S. 49-60 
    ISSN: 1432-2013
    Keywords: Amino Acid Transport ; Sodium Cotransport ; Kidney Tubules ; Kidney Micropuncture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary With the technique of stop flow microperfusion with simultaneous capillary microperfusion the zero net flux transtubular concentration differences (Δc) of labelled amino acids which are equivalent to their active transport rates were measured. Alll-amino acids tested (phenylalanine, histidine, aminobicycloheptane-carboxylic acid, aminoisobutyric acid; lysine, ornithine, arginine; aspartic acid; proline and glycine) showed a considerable Δc, i.e. active transport rate. When, however, the ambient sodium was replaced by choline the Δc values dropped to zero. An analysis of the Na+ dependence of the ornithine transport revealed that the sodium-dependence is of the mixed type, i.e. thatK m decreased andV max increased with increasing Na+ concentration to the same extent. In contrast to other biological systems no mutual interaction between the Na+-dependentd-glucose andl-histidine transport could be observed. Incidental to these studies it was observed that the active transport rate ofd-histidine was in the range of 40% of that of thel-isomer while ford-phenylalanine it was only in the range of 10% of the active transport of thel-isomer. Furthermore it was found that thel-aspartic acid transport was already saturated at a luminall-aspartic acid concentration of 0.05 mmol/l while that ofl-phenylalanine was not saturated even at a luminal concentration of 9 mmol/l.
    Type of Medium: Electronic Resource
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