NDLI: Altered ubiquitination and stability of aquaporin-1 in hypertonic stress.

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Altered ubiquitination and stability of aquaporin-1 in hypertonic stress.

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Altered ubiquitination and stability of aquaporin-1 in hypertonic stress.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Leitch, V. King, L. S. Agre, P.
Description	Author Affiliation: Leitch V ( Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.);
Abstract	Aquaporin-1 (AQP1) water channel protein expression is increased by hypertonic stress. The contribution of changes in protein stability to hypertonic induction of AQP1 have not been described. Incubation of BALB/c fibroblasts spontaneously expressing AQP1 with proteasome inhibitors increased AQP1 expression, suggesting basal proteasome-dependent degradation of the protein. Degradation by the proteasome is thought to be triggered by polyubiquitination of a target protein. To determine whether AQP1 is ubiquitinated, immunoprecipitation with anti-AQP1 antibodies was performed, and the resultant samples were probed by protein immunoblot for the presence of ubiquitin. Immunoblots demonstrated ubiquitination of AQP1 under control conditions that increased after treatment with proteasome inhibitors (MG132, lactacystin). Exposure of cells to hypertonic medium for as little as 4 h decreased ubiquitination of AQP1, an effect that persisted through 24 h in hypertonic medium. Using metabolic labeling with [(35)S]methionine, the half-life of AQP1 protein under isotonic conditions was found to be <4 h. AQP1 protein half-life was markedly increased by exposure of cells to hypertonic medium. These observations provide evidence that aquaporins are a target for ubiquitination and proteasome-dependent degradation. Additionally, these studies demonstrate that reduced protein ubiquitination and increased protein stability lead to increased levels of AQP1 expression during hypertonic stress.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aquaporins Metabolism Ubiquitins Animals Aquaporin 1 Cells, Cultured Cysteine Endopeptidases Drug Effects Cysteine Proteinase Inhibitors Pharmacology Mice Mice, Inbred BALB C Multienzyme Complexes Osmotic Pressure Proteasome Endopeptidase Complex Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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