Partial nephrogenic diabetes insipidus caused by a novel AQP2 variation impairing trafficking of the aquaporin-2 water channel

BMC Nephrology

Volumn 16, Issue 1, 2015, Pages

  Dollerup, Pia ^a   Thomsen, Troels Møller ^a   Nejsum, Lene N ^a   Færch, Mia ^b   Österbrand, Martin ^c   Gregersen, Niels ^b   Rittig, Søren ^b   Christensen, Jane H ^a   Corydon, Thomas J ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b AARHUS UNIVERSITY HOSPITAL   (Denmark)

^c QUEEN SILVIA CHILDREN'S HOSPITAL   (Sweden)

Author keywords

Aquaporin 2; Cellular trafficking; Congenital nephrogenic diabetes insipidus; Diabetes insipidus; Intracellular localization; Lentivirus

Indexed keywords

AQUAPORIN 2; ARGININE; ARGIPRESSIN; CYTOSINE; DNA; DYNAMIN II; GREEN FLUORESCENT PROTEIN; THYMINE; TRYPTOPHAN;

ANIMAL CELL; AQP2 GENE; ARTICLE; AUTOSOMAL DOMINANT INHERITANCE; AVP GENE; CELL MIGRATION; CELL SURFACE; CONGENITAL DISORDER; CONGENITAL NEPHROGENIC DIABETES INSIPIDUS; CONTROLLED STUDY; DNA SEQUENCE; EMBRYO; ENDOCYTOSIS; GENETIC CODE; GENETIC VARIATION; HUMAN; HUMAN CELL; MALE; MDCK CELL LINE; NEPHROGENIC DIABETES INSIPIDUS; NONHUMAN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; TRANSIENT EXPRESSION; WATER DEPRIVATION; FEMALE; GENETICS; INFANT; MUTATION; PEDIGREE; PHYSIOLOGY; PROTEIN TRANSPORT;

AQUAPORIN 2; DIABETES INSIPIDUS, NEPHROGENIC; FEMALE; HUMANS; INFANT; MALE; MUTATION; PEDIGREE; PROTEIN TRANSPORT;

EID: 84952057180     PISSN: None     EISSN: 14712369     Source Type: Journal    
DOI: 10.1186/s12882-015-0213-3     Document Type: Article

References (30)

1. Moeller HB, Rittig S, Fenton RA. Nephrogenic Diabetes Insipidus: Essential Insights into the Molecular Background and Potential Therapies for Treatment. Endocr Rev. 2013;34(2):278-301.
2. Nielsen S, Frokiaer J, Marples D, Kwon TH, Agre P, Knepper MA. Aquaporins in the kidney: from molecules to medicine. Physiol Rev. 2002;82(1):205-44.
3. Sun TX, Van Hoek A, Huang Y, Bouley R, McLaughlin M, Brown D. Aquaporin-2 localization in clathrin-coated pits: inhibition of endocytosis by dominantnegative dynamin. Am J Physiol Ren Physiol. 2002;282(6):F998-1011.
4. Gong H, Wang W, Kwon TH, Jonassen T, Frokiaer J, Nielsen S. Reduced renal expression of AQP2, p-AQP2 and AQP3 in haemorrhagic shock-induced acute renal failure. Nephrol Dial Transplant. 2003;18(12):2551-9.
5. Katsura T, Ausiello DA, Brown D. Direct demonstration of aquaporin-2 water channel recycling in stably transfected LLC-PK1 epithelial cells. Am J Physiol. 1996;270(3 Pt 2):F548-553.
6. Katsura T, Gustafson CE, Ausiello DA, Brown D. Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells. Am J Physiol. 1997;272(6 Pt 2):F817-822.
7. Fushimi K, Sasaki S, Marumo F. Phosphorylation of serine 256 is required for cAMP-dependent regulatory exocytosis of the aquaporin-2 water channel. J Biol Chem. 1997;272(23):14800-4.
8. Lu H, Sun TX, Bouley R, Blackburn K, McLaughlin M, Brown D. Inhibition of endocytosis causes phosphorylation (S256)-independent plasma membrane accumulation of AQP2. Am J Physiol Ren Physiol. 2004;286(2):F233-243.
9. van Balkom BW, Savelkoul PJ, Markovich D, Hofman E, Nielsen S, van der Sluijs P, et al. The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel. J Biol Chem. 2002;277(44):41473-9.
10. Kamsteeg EJ, Heijnen I, van Os CH, Deen PM. The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers. J Cell Biol. 2000;151(4):919-30.
11. Nejsum LN, Zelenina M, Aperia A, Frokiaer J, Nielsen S. Bidirectional regulation of AQP2 trafficking and recycling: involvement of AQP2-S256 phosphorylation. Am J Physiol Ren Physiol. 2005;288(5):F930-938.
12. Kuwahara M, Iwai K, Ooeda T, Igarashi T, Ogawa E, Katsushima Y, et al. Three families with autosomal dominant nephrogenic diabetes insipidus caused by aquaporin-2 mutations in the C-terminus. Am J Hum Genet. 2001;69(4):738-48.
13. Marr N, Bichet DG, Lonergan M, Arthus MF, Jeck N, Seyberth HW, et al. Heteroligomerization of an Aquaporin-2 mutant with wild-type Aquaporin-2 and their misrouting to late endosomes/lysosomes explains dominant nephrogenic diabetes insipidus. Hum Mol Genet. 2002;11(7):779-89.
14. de Mattia F, Savelkoul PJ, Kamsteeg EJ, Konings IB, van der Sluijs P, Mallmann R, et al. Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus. J Am Soc Nephrol. 2005;16(10):2872-80.
15. Savelkoul PJ, De Mattia F, Li Y, Kamsteeg EJ, Konings IB, van der Sluijs P, et al. p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressininduced phosphorylation. Hum Mutat. 2009;30(10):E891-903.
16. Kamsteeg EJ, Bichet DG, Konings IB, Nivet H, Lonergan M, Arthus MF, et al. Reversed polarized delivery of an aquaporin-2 mutant causes dominant nephrogenic diabetes insipidus. J Cell Biol. 2003;163(5):1099-109.
17. Kamsteeg EJ, Wormhoudt TA, Rijss JP, van Os CH, Deen PM. An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus. EMBO J. 1999; 18(9):2394-400.
18. Mulders SM, Bichet DG, Rijss JP, Kamsteeg EJ, Arthus MF, Lonergan M, et al. An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex. J Clin Invest. 1998;102(1):57-66.
19. Moldt B, Staunstrup NH, Jakobsen M, Yanez-Munoz RJ, Mikkelsen JG. Genomic insertion of lentiviral DNA circles directed by the yeast Flp recombinase. BMC Biotechnol. 2008;8:60.
20. Askou AL, Aagaard L, Arsenijevic Y, Kostic C, Bek T, Jensen TG, et al. Multigenic lentiviral vectors for combined and tissue-specific expression of miRNA-and protein-based anti-angiogenic factors. Molecular Therapy-Methods and Clinical Development 2015;28(2):14064.
21. Bucci C, Thomsen P, Nicoziani P, McCarthy J, van Deurs B. Rab7: a key to lysosome biogenesis. Mol Biol Cell. 2000;11(2):467-80.
22. Lombardi D, Soldati T, Riederer MA, Goda Y, Zerial M, Pfeffer SR. Rab9 functions in transport between late endosomes and the trans Golgi network. EMBO J. 1993;12(2):677-82.
23. Corydon TJ, Hansen J, Bross P, Jensen TG. Down-regulation of Hsp60 expression by RNAi impairs folding of medium-chain acyl-CoA dehydrogenase wild-type and disease-associated proteins. Mol Genet Metab. 2005;85(4):260-70.
24. Kuwahara M, Asai T, Terada Y, Sasaki S. The C-terminal tail of aquaporin-2 determines apical trafficking. Kidney Int. 2005;68(5):1999-2009.
25. Babey M, Kopp P, Robertson GL. Familial forms of diabetes insipidus: clinical and molecular characteristics. Nat Rev Endocrinol. 2011;7(12):701-14.
26. Faerch M, Christensen JH, Corydon TJ, Kamperis K, de Zegher F, Gregersen N, et al. Partial nephrogenic diabetes insipidus caused by a novel mutation in the AVPR2 gene. Clin Endocrinol. 2008;68(3):395-403.
27. Brown D. The ins and outs of aquaporin-2 trafficking. Am J Physiol Ren Physiol. 2003;284(5):F893-901.
28. Boone M, Deen PM. Congenital nephrogenic diabetes insipidus: what can we learn from mouse models? Exp Physiol. 2009;94(2):186-90.
29. Morello JP, Salahpour A, Laperriere A, Bernier V, Arthus MF, Lonergan M, et al. Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J Clin Invest. 2000;105(7): 887-95.
30. Bernier V, Morello JP, Zarruk A, Debrand N, Salahpour A, Lonergan M, et al. Pharmacologic chaperones as a potential treatment for X-linked nephrogenic diabetes insipidus. J Am Soc Nephrol. 2006;17(1):232-43.