In:
The Journal of Physiology, Wiley, Vol. 588, No. 12 ( 2010-06-15), p. 2205-2218
Abstract:
Aquaporin‐2 (AQP2), exclusively found in the kidney, is a water channel responsible for the final concentration of urine. Consequently, altered forms of AQP2 induce nephrogenic diabetes insipidus (NDI), a condition characterized by the production of large urinary volumes. In this study, three mutations (K228E, V24A and R187C) identified in NDI‐affected individuals are analysed in comparison to the wild‐type protein using amphibian ( Xenopus laevis ) oocytes and a mammalian kidney cell line (mIMCD‐3 cells) as expression systems. Data show that K228E and V24A are intrinsically functional water channels (in oocytes) which lack proper targeting in more developed systems (mIMCD‐3 cells) while R187C displays no functionality, even in oocytes. The consequences of mixed wild‐type/mutant structures are discussed as they sometimes generate NDI through ineffective water channels.
Type of Medium:
Online Resource
ISSN:
0022-3751
,
1469-7793
DOI:
10.1113/tjp.2010.588.issue-12
DOI:
10.1113/jphysiol.2010.187674
Language:
English
Publisher:
Wiley
Publication Date:
2010
detail.hit.zdb_id:
1475290-6
SSG:
12
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