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Poly(ADP-ribose) polymerase-1 affects vasopressin-mediated AQP2 expression in collecting duct cells of the kidney

Jang, Hyo-Ju ; Park, Euijung ; Jung, Hyun Jun ; Kwon, Tae-Hwan

American journal of physiology. Renal physiology, 2024-01, Vol.326 (1), p.F69-F85 [Periódico revisado por pares]

United States

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  • Título:
    Poly(ADP-ribose) polymerase-1 affects vasopressin-mediated AQP2 expression in collecting duct cells of the kidney
  • Autor: Jang, Hyo-Ju ; Park, Euijung ; Jung, Hyun Jun ; Kwon, Tae-Hwan
  • Assuntos: Animals ; Aquaporin 2 - genetics ; beta Catenin - metabolism ; Biotin - metabolism ; Deamino Arginine Vasopressin - pharmacology ; Kidney - metabolism ; Mice ; NAD - metabolism ; Poly (ADP-Ribose) Polymerase-1 - genetics ; Poly (ADP-Ribose) Polymerase-1 - metabolism ; Poly Adenosine Diphosphate Ribose - metabolism ; Poly(ADP-ribose) Polymerase Inhibitors ; Poly(ADP-ribose) Polymerases - genetics ; Poly(ADP-ribose) Polymerases - metabolism ; RNA, Small Interfering ; Vasopressins - metabolism ; Vasopressins - pharmacology
  • É parte de: American journal of physiology. Renal physiology, 2024-01, Vol.326 (1), p.F69-F85
  • Descrição: Poly(ADP-ribosyl)ation (PARylation), as a posttranslational modification mediated by poly(ADP-ribose) polymerases (PARPs) catalyzing the transfer of ADP-ribose from NAD molecules to acceptor proteins, involves a number of cellular processes. As mice lacking the PARP-1 gene ( ) produce more urine, we investigated the role of PARP-1, the most prevalent member of the PARP family, in the vasopressin-responsive expression of aquaporin-2 (AQP2). In biotin-conjugated nicotinamide adenine dinucleotide (biotin-NAD ) pulldown and immunoprecipitation assays of poly(ADP)-ribose in mpkCCDc14 cells, immunoblots demonstrated that 1-deamino-8-D-arginine vasopressin (dDAVP) induced the PARylation of total proteins, associated with an increase in the cleavage of PARP-1 and cleaved caspase-3 expression. By inhibiting PARP-1 with siRNA, the abundance of dDAVP-induced AQP2 mRNA and protein was significantly diminished. In contrast, despite a substantial decrease in PARylation, the PARP-1 inhibitor (PJ34) had no effect on the dDAVP-induced regulation of AQP2 expression. The findings suggest that PARP-1 protein expression itself, and not PARP-1-mediated PARylation, is necessary for dDAVP-regulated AQP2 expression. Bioinformatic analysis revealed that 408 proteins interact with PARP-1 in the collecting duct (CD) cells of the kidney. Among them, the signaling pathway of the vasopressin V2 receptor was identified for 49 proteins. In particular, β-catenin, which is phosphorylated at Ser by dDAVP, was identified as the PARP-1-interacting protein. A significant decrease of β-catenin phosphorylation (Ser ) in response to dDAVP was associated with siRNA-mediated PARP-1 knockdown. Taken together, PARP-1 is likely to play a role in vasopressin-induced AQP2 expression by interacting with β-catenin in renal CD cells. The poly(ADP-ribose) polymerase (PARP) family catalyzes poly(ADP-ribosylation) (PARylation), which is one of the posttranslational modifications of largely undetermined physiological significance. This study investigated the role of PARP-1, the most prevalent member of the PARP family, in the vasopressin-responsive expression of aquaporin-2 (AQP2). The results demonstrated that PARP-1 protein expression itself, and not PARP-1-mediated PARylation, is necessary for dDAVP-regulated AQP2 expression. β-Catenin, which is phosphorylated at Ser by dDAVP, was identified as the PARP-1-interacting protein.
  • Editor: United States
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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