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  • Essential hypertension  (9)
  • Microperfusion  (3)
  • Springer  (12)
  • 11
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 371 (1977), S. 141-145 
    ISSN: 1432-2013
    Keywords: Renal tubule ; Disaccharide reabsorption ; Maltase ; Brush border enzymes ; Microperfusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Renal tubular reabsorption of maltose, sucose and lactose were studied in vivo et situ by continuous microperfusion of single proximal convolutions of rat kidney. The14C-label of maltose (2.5 mmol/l) was removed from the lumen of the proximal tubule at about the same rate as found for glucose. Maltose reabsorption was completely inhibited in presence of 30 mmol/l glucose or of 0.1 mmol/l phlorizin. Chemical analysis of the samples showed a complete conversion of maltose into glucose within a perfusion distance of 2 mm. It is concluded from these results that within the tubular lumen maltose is split very rapidly by a brush border glucosidase. The short half time of this process permits the breakdown product glucose to be almost completely reabsorbed subsequently within the proximal tubule. In contrast, sucrose and lactose were neither split nor reabsorbed by the tubule brush border.
    Type of Medium: Electronic Resource
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  • 12
    ISSN: 1432-2013
    Keywords: Kidney ; Tubular resorption ; Microperfusion ; Specificity ; Glutamate ; Aspartate ; Cysteate ; γ-Carboxyglutamate ; Pyroglutamate ; 5-oxo-proline
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Single sections of superficial proximal convolutions of rat kidney were microperfused in vivo and in situ. The perfusion fluids contained radioactively labelledl- ord-aspartate,l-glutamate,l-pyroglutamate, or N-methyl-d-aspartate.l-γ-Carboxyglutamate as well as the other amino acids were added in the unlabelled from. Results.l- andd-Aspartate (0.073 mmol·1−1) are quickly resorbed at about the same rate.d-Aspartate resorption was blocked byl-aspartate (5 mmol·1−1) but not by β-alanine (5 mmol·1−1).l-Aspartate resorption was inhibited byl-glutamate (2 mmol·1−1) but not byd-glutamate,l-asparagine,l-phenylalanine or by succinate (2 mmol·1−1, each). The fast resorption ofl-glutamate (0.073 mmol·1−1) was blocked byd-aspartate,l-cysteate (2 mmol·1−1), but not by 3-mercaptopicolinic acid (0.15 mmol·1−1),l-glutamine, 2-oxoglutarate, taurine, N-methyl-l-glutamate or kainic acid (2 mmol·1−1, each).l-γ-Carboxyglutamate (0.66 mmol·1−1) and N-methyl-d-aspartate (2μmol·1−1) were found to be resorbed only at an extremely small rate.l-pyroglutamate (0.076 mmol·1−1) resorption was not influenced byl-glutamate (1 mmol·1−1). Fractional excretion of γ-carboxyglutamate was 7–25% (l-from) or 45–70% (d-form) at an artificially elevated plasma level of 12μmol·1−1. It is concluded thatl- andd-aspartate,l-glutamate,l-cysteate and, to a much smaller extent,l-γ-carboxyglutamate, are accepted by the tubular resorption mechanism highly specific for “acidic” amino acids. N-Substitution, the amidation of the β- or γ-carboxyl group, or the removal of the α-amino moiety almost completely abolish the ability of such compounds to be resorbed via this carrier; N-methylated or γ-carboxylated derivatives of “acidic” amino acids are not resorbed at all from the proximal tubule. The resorption of glutamate, but not of aspartate, is highly stereospecific.
    Type of Medium: Electronic Resource
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