Publication

Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells

Robben, J. H., Knoers, N. V. A. M. & Deen, P. M. T., Dec-2004, In : Molecular Biology of the Cell. 15, 12, p. 5693-9 7 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Robben, J. H., Knoers, N. V. A. M., & Deen, P. M. T. (2004). Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells. Molecular Biology of the Cell, 15(12), 5693-9. https://doi.org/10.1091/mbc.e04-04-0337

Author

Robben, J H ; Knoers, N V A M ; Deen, P M T. / Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells. In: Molecular Biology of the Cell. 2004 ; Vol. 15, No. 12. pp. 5693-9.

Harvard

Robben, JH, Knoers, NVAM & Deen, PMT 2004, 'Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells', Molecular Biology of the Cell, vol. 15, no. 12, pp. 5693-9. https://doi.org/10.1091/mbc.e04-04-0337

Standard

Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells. / Robben, J H; Knoers, N V A M; Deen, P M T.

In: Molecular Biology of the Cell, Vol. 15, No. 12, 12.2004, p. 5693-9.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Robben JH, Knoers NVAM, Deen PMT. Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells. Molecular Biology of the Cell. 2004 Dec;15(12):5693-9. https://doi.org/10.1091/mbc.e04-04-0337


BibTeX

@article{8449309cd1b24b719536b23ec0eb5e6b,
title = "Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells",
abstract = "Binding of arginine-vasopressin (AVP) to its V2 receptor (V2R) in the basolateral membrane of principal cells induces Aquaporin-2-mediated water reabsorption in the kidney. To study the regulation of the V2R by dDAVP in a proper model, a polarized renal cell line stably-expressing V2R-GFP was generated. Labeled AVP-binding studies revealed an equal basolateral vs. apical membrane distribution for V2R-GFP and endogenous V2R. In these cells, GFP-V2R was expressed in its mature form and localized for 75{\%} in the basolateral membrane and for 25{\%} to late endosomes/lysosomes. dDAVP caused a dose- and time-dependent internalization of V2R-GFP, which was completed within 1 h with 100 nM dDAVP, was prevented by coincubation with a V2R antagonist, and which reduced its half-life from 11.5 to 2.8 h. Semiquantification of the V2R-GFP colocalization with E-cadherin (basolateral membrane), early endosomal antigen-1 (EEA-1) and lysosome-associated membrane protein-2 (LAMP-2) in time revealed that most dDAVP-bound V2R was internalized via early endosomes to late endosomes/lysosomes, where it was degraded. The dDAVP-internalized V2R did not recycle to the basolateral membrane. In conclusion, we established the itinerary of the V2R in a polarized cell model that likely resembles the in vivo V2R localization and regulation by AVP to a great extent.",
keywords = "Animals, Cell Line, Cell Polarity, Dogs, Glycosylation, Kidney Tubules, Collecting/cytology, Lysosomes/drug effects, Organelles/metabolism, Protein Processing, Post-Translational/drug effects, Receptors, Vasopressin/genetics, Time Factors, Vasopressins/pharmacology",
author = "Robben, {J H} and Knoers, {N V A M} and Deen, {P M T}",
year = "2004",
month = "12",
doi = "10.1091/mbc.e04-04-0337",
language = "English",
volume = "15",
pages = "5693--9",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "AMER SOC CELL BIOLOGY",
number = "12",

}

RIS

TY - JOUR

T1 - Regulation of the vasopressin V2 receptor by vasopressin in polarized renal collecting duct cells

AU - Robben, J H

AU - Knoers, N V A M

AU - Deen, P M T

PY - 2004/12

Y1 - 2004/12

N2 - Binding of arginine-vasopressin (AVP) to its V2 receptor (V2R) in the basolateral membrane of principal cells induces Aquaporin-2-mediated water reabsorption in the kidney. To study the regulation of the V2R by dDAVP in a proper model, a polarized renal cell line stably-expressing V2R-GFP was generated. Labeled AVP-binding studies revealed an equal basolateral vs. apical membrane distribution for V2R-GFP and endogenous V2R. In these cells, GFP-V2R was expressed in its mature form and localized for 75% in the basolateral membrane and for 25% to late endosomes/lysosomes. dDAVP caused a dose- and time-dependent internalization of V2R-GFP, which was completed within 1 h with 100 nM dDAVP, was prevented by coincubation with a V2R antagonist, and which reduced its half-life from 11.5 to 2.8 h. Semiquantification of the V2R-GFP colocalization with E-cadherin (basolateral membrane), early endosomal antigen-1 (EEA-1) and lysosome-associated membrane protein-2 (LAMP-2) in time revealed that most dDAVP-bound V2R was internalized via early endosomes to late endosomes/lysosomes, where it was degraded. The dDAVP-internalized V2R did not recycle to the basolateral membrane. In conclusion, we established the itinerary of the V2R in a polarized cell model that likely resembles the in vivo V2R localization and regulation by AVP to a great extent.

AB - Binding of arginine-vasopressin (AVP) to its V2 receptor (V2R) in the basolateral membrane of principal cells induces Aquaporin-2-mediated water reabsorption in the kidney. To study the regulation of the V2R by dDAVP in a proper model, a polarized renal cell line stably-expressing V2R-GFP was generated. Labeled AVP-binding studies revealed an equal basolateral vs. apical membrane distribution for V2R-GFP and endogenous V2R. In these cells, GFP-V2R was expressed in its mature form and localized for 75% in the basolateral membrane and for 25% to late endosomes/lysosomes. dDAVP caused a dose- and time-dependent internalization of V2R-GFP, which was completed within 1 h with 100 nM dDAVP, was prevented by coincubation with a V2R antagonist, and which reduced its half-life from 11.5 to 2.8 h. Semiquantification of the V2R-GFP colocalization with E-cadherin (basolateral membrane), early endosomal antigen-1 (EEA-1) and lysosome-associated membrane protein-2 (LAMP-2) in time revealed that most dDAVP-bound V2R was internalized via early endosomes to late endosomes/lysosomes, where it was degraded. The dDAVP-internalized V2R did not recycle to the basolateral membrane. In conclusion, we established the itinerary of the V2R in a polarized cell model that likely resembles the in vivo V2R localization and regulation by AVP to a great extent.

KW - Animals

KW - Cell Line

KW - Cell Polarity

KW - Dogs

KW - Glycosylation

KW - Kidney Tubules, Collecting/cytology

KW - Lysosomes/drug effects

KW - Organelles/metabolism

KW - Protein Processing, Post-Translational/drug effects

KW - Receptors, Vasopressin/genetics

KW - Time Factors

KW - Vasopressins/pharmacology

U2 - 10.1091/mbc.e04-04-0337

DO - 10.1091/mbc.e04-04-0337

M3 - Article

C2 - 15469988

VL - 15

SP - 5693

EP - 5699

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 12

ER -

ID: 92706089