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Monensin-resistant LLC-PK1 cell mutants are affected in recycling of the adenylate cyclase-stimulating vasopressin V2-receptor

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Jans,  David A.
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Jans,  Patricia
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Luzius,  Heike
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Fahrenholz,  Falk
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Jans, D. A., Jans, P., Luzius, H., & Fahrenholz, F. (1990). Monensin-resistant LLC-PK1 cell mutants are affected in recycling of the adenylate cyclase-stimulating vasopressin V2-receptor. Molecular and Cellular Endocrinology, 81(1-3), 165-174. doi:10.1016/0303-7207(91)90215-e.


Cite as: http://hdl.handle.net/21.11116/0000-0007-E5E4-5
Abstract
The ionophore monensin was found to markedly reduce the rate of return of vasopressin V2-receptors to the membrane following down-regulation with [Arg8]vasopressin (AVP), as well as hormone dissociation (unloading) from cells following ligand binding and internalization in LLC-PK1 renal epithelial cells. Monensin-resistant LLC-PK1 mutants were isolated and characterized for V2-receptor recycling. Whilst the MN-41 mutant appeared to be impaired in [3H]AVP internalization, the MN-11 and MN-21 mutants exhibited parental V2-receptor binding and internalization, but markedly impaired receptor recycling subsequent to ligand-dependent receptor down-regulation. Unloading subsequent to ligand binding and internalization at 37 degrees C was also much slower in the mutants either at 37 degrees C or 23 degrees C. In contrast, unloading subsequent to binding at 23 degrees C, or to binding at 37 degrees C in the presence of NH4Cl, was comparable in LLC-PK1 and mutant cells implying the active nature of the recycling process impaired in the mutants. The mutations conferring resistance to monesin thus concomitantly impaired V2-receptor recycling in the mutants. Results argue for a monensin-sensitive endosomal/lysosomal pathway for the renal V2-receptor, representing the first such report for an adenylate cyclase stimulating receptor.