Endoplasmic reticulum stress in vasopressin neurons of familial diabetes insipidus model mice: Aggregate formation and mRNA poly(A) tail shortening

Experimental Physiology

Volumn 99, Issue 1, 2014, Pages 66-71

  Arima, Hiroshi ^a   Morishita, Yoshiaki ^a   Hagiwara, Daisuke ^a   Hayashi, Masayuki ^a   Oiso, Yutaka ^a  

^a NAGOYA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; POLYADENYLATED RNA; VASOPRESSIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; DEHYDRATION; DIABETES INSIPIDUS; ELECTRON MICROSCOPY; ENDOPLASMIC RETICULUM STRESS; FAMILIAL DISEASE; FAMILIAL NEUROHYPOPHYSIAL DIABETES INSIPIDUS; FEMALE; GENE EXPRESSION; GENE LOCUS; GENE MUTATION; MOUSE; NERVE CELL; NONHUMAN; POLYURIA; SUPRAOPTIC NUCLEUS; TAIL; WILD TYPE;

ANIMALS; DIABETES INSIPIDUS, NEUROGENIC; DISEASE MODELS, ANIMAL; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; HUMANS; HYPOTHALAMUS; MICE; NEURONS; PROTEIN FOLDING; RNA, MESSENGER; VASOPRESSINS;

EID: 84892410422     PISSN: 09580670     EISSN: 1469445X     Source Type: Journal    
DOI: 10.1113/expphysiol.2013.072553     Document Type: Article

References (25)

1. Arima H, Kondo K, Kakiya S, Nagasaki H, Yokoi H, Yambe Y, Murase T, Iwasaki Y & Oiso Y (1999). Rapid and sensitive vasopressin heteronuclear RNA responses to changes in plasma osmolality. J Neuroendocrinol 11, 337-341.
2. Bernstein P & Ross J (1989). Poly(A), poly(A) binding protein and the regulation of mRNA stability. Trends Biochem Sci 14, 373-377.
3. Carrazana EJ, Pasieka KB & Majzoub JA (1988). The vasopressin mRNA poly(A) tract is unusually long and increases during stimulation of vasopressin gene expression in vivo. Mol Cell Biol 8, 2267-2274.
4. Carter DA & Murphy D (1991). Rapid changes in poly (A) tail length of vasopressin and oxytocin mRNAs form a common early component of neurohypophyseal peptide gene activation following physiological stimulation. Neuroendocrinology 53, 1-6.
5. Castino R, Isidoro C & Murphy D (2005). Autophagy-dependent cell survival and cell death in an autosomal dominant familial neurohypophyseal diabetes insipidus in vitro model. FASEB J 19, 1024-1026.
6. Chooi KF, Carter DA & Murphy D (1992). Decrease in hypothalamic vasopressin mRNA poly(A) tail length following physiological stimulation. Cell Mol Neurobiol 12, 557-567.
7. Christensen JH & Rittig S (2006). Familial neurohypophyseal diabetes insipidus-an update. Semin Nephrol 26, 209-223.
8. Gething MJ (1999). Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 10, 465-472.
9. Haas IG & Wabl M (1983). Immunoglobulin heavy chain binding protein. Nature 306, 387-389.
10. Hagiwara D, Arima H, Morishita Y, Goto M, Banno R, Sugimura Y & Oiso Y (2012). BiP mRNA expression is upregulated by dehydration in vasopressin neurons in the hypothalamus in mice. Peptides 33, 346-350.
11. Hayashi M, Arima H, Ozaki N, Morishita Y, Hiroi M, Ozaki N, Nagasaki H, Kinoshita N, Ueda M, Shiota A & Oiso Y (2009). Progressive polyuria without vasopressin neuron loss in a mouse model for familial neurohypophysial diabetes insipidus. Am J Physiol Regul Integr Comp Physiol 296, R1641-R1649.
12. Ito M, Jameson JL & Ito M (1997). Molecular basis of autosomal dominant neurohypophyseal diabetes insipidus. Cellular toxicity caused by the accumulation of mutant vasopressin precursors within the endoplasmic reticulum. J Clin Invest 99, 1897-1905.
13. Ito M, Oiso Y, Murase T, Kondo K, Saito H, Chinzei T, Racchi M & Lively MO (1993). Possible involvement of inefficient cleavage of preprovasopressin by signal peptidase as a cause for familial central diabetes insipidus. J Clin Invest 91, 2565-2571.
14. Ito M, Yu RN & Jameson JL (1999). Mutant vasopressin precursors that cause autosomal dominant neurohypophyseal diabetes insipidus retain dimerization and impair the secretion of wild-type proteins. J Biol Chem 274, 9029-9037.
15. Kuraishi T, Mizoguchi Y, Sun Y, Aoki F, Imakawa K & Sakai S (2002). The casein mRNA decay changes in parallel with the poly(A) tail length in the mouse mammary gland. Mol Cell Endocrinol 190, 101-107.
16. Morishita Y, Arima H, Hiroi M, Hayashi M, Hagiwara D, Asai N, Ozaki N, Sugimura Y, Nagasaki H, Shiota A, Takahashi M & Oiso Y (2011). Poly(A) tail length of neurohypophysial hormones is shortened under endoplasmic reticulum stress. Endocrinology 152, 4846-4855.
17. Petaja-Repo UE, Hogue M, Laperriere A, Walker P & Bouvier M (2000). Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor. J Biol Chem 275, 13727-13736.
18. Robinson BG, Frim DM, Schwartz WJ & Majzoub JA (1988). Vasopressin mRNA in the suprachiasmatic nuclei: daily regulation of polyadenylate tail length. Science 241, 342-344.
19. Ron D & Walter P (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8, 519-529.
20. Russell TA, Ito M, Ito M, Yu RN, Martinson FA, Weiss J & Jameson JL (2003). A murine model of autosomal dominant neurohypophyseal diabetes insipidus reveals progressive loss of vasopressin-producing neurons. J Clin Invest 112, 1697-1706.
21. Si-Hoe SL, De Bree FM, Nijenhuis M, Davies JE, Howell LM, Tinley H, Waller SJ, Zeng Q, Zalm R, Sonnemans M, Van Leeuwen FW, Burbach JP & Murphy D (2000). Endoplasmic reticulum derangement in hypothalamic neurons of rats expressing a familial neurohypophyseal diabetes insipidus mutant vasopressin transgene. FASEB J 14, 1680-1684.
22. Svane PC, Thorn NA, Richter D & Mohr E (1995). Effect of hypoosmolality on the abundance, poly(A) tail length and axonal targeting of arginine vasopressin and oxytocin mRNAs in rat hypothalamic magnocellular neurons. FEBS Lett 373, 35-38.
23. Wakiyama M, Futami T & Miura K (1997). Poly(A) dependent translation in rabbit reticulocyte lysate. Biochimie 79, 781-785.
24. Wu J & Kaufman RJ (2006). From acute ER stress to physiological roles of the Unfolded Protein Response. Cell Death Differ 13, 374-384.
25. Zingg HH, Lefebvre DL & Almazan G (1988). Regulation of poly(A) tail size of vasopressin mRNA. J Biol Chem 263, 11041-11043.