Intrinsic carnosine metabolism in the human kidney

• Verfasst von: Peters, Verena [VerfasserIn]
• Verfasst von: Klessens, Celine Q. F. [VerfasserIn]
• Verfasst von: Baelde, Hans [VerfasserIn]
• Verfasst von: Singler, Benjamin [VerfasserIn]
• Verfasst von: Veraar, Kimberley A. M. [VerfasserIn]
• Verfasst von: Zutinic, Ana [VerfasserIn]
• Verfasst von: Drozak, Jakub [VerfasserIn]
• Verfasst von: Zschocke, Johannes [VerfasserIn]
• Verfasst von: Schmitt, Claus P. [VerfasserIn]
• Verfasst von: de Heer, Emile [VerfasserIn]
• Titel: Intrinsic carnosine metabolism in the human kidney
• Verf.angabe: Verena Peters · Celine Q.F. Klessens · Hans J. Baelde · Benjamin Singler · Kimberley A.M. Veraar · Ana Zutinic · Jakub Drozak · Johannes Zschocke · Claus P. Schmitt · Emile de Heer
• E-Jahr: 2015
• Jahr: 24 July 2015
• Umfang: 10 S.
• Fussnoten: Gesehen am 02.07.2020
• Titel Quelle: Enthalten in: Amino acids
• Ort Quelle: Wien [u.a.] : Springer, 1991
• Jahr Quelle: 2015
• Band/Heft Quelle: 47(2015), 12, Seite 2541-2550
• ISSN Quelle: 1438-2199
• DOI: doi:10.1007/s00726-015-2045-7
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1703277031

Abstract

Histidine-containing dipeptides like carnosine and anserine have protective functions in both health and disease. Animal studies suggest that carnosine can be metabolized within the kidney. The goal of this study was to obtain evidence of carnosine metabolism in the human kidney and to provide insight with regards to diabetic nephropathy. Expression, distribution, and localization of carnosinase-1 (CNDP1), carnosine synthase (CARNS), and taurine transporters (TauT) were measured in human kidneys. CNDP1 and CARNS activities were measured in vitro. CNDP1 and CARNS were located primarily in distal and proximal tubules, respectively. Specifically, CNDP1 levels were high in tubular cells and podocytes (20.3 ± 3.4 and 15 ± 3.2 ng/mg, respectively) and considerably lower in endothelial cells (0.5 ± 0.1 ng/mg). CNDP1 expression was correlated with the degradation of carnosine and anserine (r = 0.88 and 0.81, respectively). Anserine and carnosine were also detectable by HPLC in the renal cortex. Finally, TauT mRNA and protein were found in all renal epithelial cells. In diabetic patients, CNDP1 seemed to be reallocated to proximal tubules. We report compelling evidence that the kidney has an intrinsic capacity to metabolize carnosine. Both CNDP1 and CARNS are expressed in glomeruli and tubular cells. Carnosine-synthesizing and carnosine-hydrolyzing enzymes are localized in distinct compartments in the nephron and increased CNDP1 levels suggest a higher CNDP1 activity in diabetic kidneys.