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Volumn 33, Issue 2, 2012, Pages 346-350

BiP mRNA expression is upregulated by dehydration in vasopressin neurons in the hypothalamus in mice

Author keywords

Arginine vasopressin; Endoplasmic reticulum stress; Immunoglobulin heavy chain binding protein; Paraventricular nucleus; Supraoptic nucleus; Unfolded protein response

Indexed keywords

ARGIPRESSIN; GLUCOSE REGULATED PROTEIN 78; MESSENGER RNA; VASOPRESSIN;

EID: 84858794907     PISSN: 01969781     EISSN: 18735169     Source Type: Journal    
DOI: 10.1016/j.peptides.2011.12.011     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0027250449 scopus 로고
    • Vasopressinergic control of pituitary adrenocorticotropin secretion comes of age
    • DOI 10.1006/frne.1993.1004
    • F.A. Antoni Vasopressinergic control of pituitary adrenocorticotropin secretion comes of age Front Neuroendocrinol 14 1993 76 122 (Pubitemid 23210952)
    • (1993) Frontiers in Neuroendocrinology , vol.14 , Issue.2 , pp. 76-122
    • Antoni, F.A.1
  • 3
    • 77954168616 scopus 로고    scopus 로고
    • Mechanisms underlying progressive polyuria in familial neurohypophysial diabetes insipidus
    • H. Arima, and Y. Oiso Mechanisms underlying progressive polyuria in familial neurohypophysial diabetes insipidus J Neuroendocrinol 22 2010 754 757
    • (2010) J Neuroendocrinol , vol.22 , pp. 754-757
    • Arima, H.1    Oiso, Y.2
  • 4
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • A. Bertolotti, Y. Zhang, L.M. Hendershot, H.P. Harding, and D. Ron Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response Nat Cell Biol 2 2000 326 332
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 5
    • 0023780847 scopus 로고
    • Control of release of vasopressin by neuroendocrine reflexes
    • G.W. Bisset, and H.S. Chowdrey Control of release of vasopressin by neuroendocrine reflexes Q J Exp Physiol 73 1988 811 872
    • (1988) Q J Exp Physiol , vol.73 , pp. 811-872
    • Bisset, G.W.1    Chowdrey, H.S.2
  • 6
    • 0022536233 scopus 로고
    • Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas
    • D.G. Bole, L.M. Hendershot, and J.F. Kearney Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas J Cell Biol 102 1986 1558 1566 (Pubitemid 16078740)
    • (1986) Journal of Cell Biology , vol.102 , Issue.5 , pp. 1558-1566
    • Bole, D.G.1    Hendershot, L.M.2    Kearney, J.F.3
  • 7
    • 0018900882 scopus 로고
    • Synthesis, transport and release of posterior pituitary hormones
    • M.J. Brownstein, J.T. Russell, and H. Gainer Synthesis, transport, and release of posterior pituitary hormones Science 207 1980 373 378 (Pubitemid 10147912)
    • (1980) Science , vol.207 , Issue.4429 , pp. 373-378
    • Brownstein, M.J.1    Russell, J.T.2    Gainer, H.3
  • 8
    • 0034964210 scopus 로고    scopus 로고
    • Gene regulation in the magnocellular hypothalamo-neurohypophysial system
    • J.P. Burbach, S.M. Luckman, D. Murphy, and H. Gainer Gene regulation in the magnocellular hypothalamo-neurohypophysial system Physiol Rev 81 2001 1197 1267 (Pubitemid 32606669)
    • (2001) Physiological Reviews , vol.81 , Issue.3 , pp. 1197-1267
    • Burbach, J.P.H.1    Luckman, S.M.2    Murphy, D.3    Gainer, H.4
  • 9
    • 33646497845 scopus 로고    scopus 로고
    • Familial neurohypophyseal diabetes insipidus - An update
    • J.H. Christensen, and S. Rittig Familial neurohypophyseal diabetes insipidus - an update Semin Nephrol 26 2006 209 223
    • (2006) Semin Nephrol , vol.26 , pp. 209-223
    • Christensen, J.H.1    Rittig, S.2
  • 10
    • 0015853572 scopus 로고
    • The role of blood osmolality and volume in regulating vasopressin secretion in the rat
    • F.L. Dunn, T.J. Brennan, A.E. Nelson, and G.L. Robertson The role of blood osmolality and volume in regulating vasopressin secretion in the rat J Clin Invest 52 1973 3212 3219
    • (1973) J Clin Invest , vol.52 , pp. 3212-3219
    • Dunn, F.L.1    Brennan, T.J.2    Nelson, A.E.3    Robertson, G.L.4
  • 11
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • M.J. Gething Role and regulation of the ER chaperone BiP Semin Cell Dev Biol 10 1999 465 472
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 12
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • I.G. Haas, and M. Wabl Immunoglobulin heavy chain binding protein Nature 306 1983 387 389 (Pubitemid 14242753)
    • (1983) Nature , vol.306 , Issue.5941 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 13
    • 66149083576 scopus 로고    scopus 로고
    • Progressive polyuria without vasopressin neuron loss in a mouse model for familial neurohypophysial diabetes insipidus
    • M. Hayashi, H. Arima, N. Ozaki, Y. Morishita, M. Hiroi, and H. Nagasaki Progressive polyuria without vasopressin neuron loss in a mouse model for familial neurohypophysial diabetes insipidus Am J Physiol Regul Integr Comp Physiol 296 2009 R1641 R1649
    • (2009) Am J Physiol Regul Integr Comp Physiol , vol.296
    • Hayashi, M.1    Arima, H.2    Ozaki, N.3    Morishita, Y.4    Hiroi, M.5    Nagasaki, H.6
  • 14
    • 75449096144 scopus 로고    scopus 로고
    • Activation of vasopressin neurons leads to phenotype progression in a mouse model for familial neurohypophysial diabetes insipidus
    • M. Hiroi, Y. Morishita, M. Hayashi, N. Ozaki, Y. Sugimura, and H. Nagasaki Activation of vasopressin neurons leads to phenotype progression in a mouse model for familial neurohypophysial diabetes insipidus Am J Physiol Regul Integr Comp Physiol 298 2010 R486 R493
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.298
    • Hiroi, M.1    Morishita, Y.2    Hayashi, M.3    Ozaki, N.4    Sugimura, Y.5    Nagasaki, H.6
  • 15
    • 0033696641 scopus 로고    scopus 로고
    • Effects of acute hypotensive stimuli on arginine vasopressin gene transcription in the rat hypothalamus
    • S. Kakiya, H. Arima, H. Yokoi, T. Murase, Y. Yambe, and Y. Oiso Effects of acute hypotensive stimuli on arginine vasopressin gene transcription in the rat hypothalamus Am J Physiol Endocrinol Metab 279 2000 E886 E892
    • (2000) Am J Physiol Endocrinol Metab , vol.279
    • Kakiya, S.1    Arima, H.2    Yokoi, H.3    Murase, T.4    Yambe, Y.5    Oiso, Y.6
  • 16
    • 1442276296 scopus 로고    scopus 로고
    • Osmoregulation of vasopressin release and gene transcription under acute and chronic hypovolemia in rats
    • N. Kondo, H. Arima, R. Banno, S. Kuwahara, I. Sato, and Y. Oiso Osmoregulation of vasopressin release and gene transcription under acute and chronic hypovolemia in rats Am J Physiol Endocrinol Metab 286 2004 E337 E346
    • (2004) Am J Physiol Endocrinol Metab , vol.286
    • Kondo, N.1    Arima, H.2    Banno, R.3    Kuwahara, S.4    Sato, I.5    Oiso, Y.6
  • 17
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • DOI 10.1038/332462a0
    • Y. Kozutsumi, M. Segal, K. Normington, M.J. Gething, and J. Sambrook The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins Nature 332 1988 462 464 (Pubitemid 18090252)
    • (1988) Nature , vol.332 , Issue.6163 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 18
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • DOI 10.1016/S0968-0004(01)01908-9, PII S0968000401019089
    • A.S. Lee The glucose-regulated proteins: stress induction and clinical applications Trends Biochem Sci 26 2001 504 510 (Pubitemid 32735452)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.8 , pp. 504-510
    • Lee, A.S.1
  • 19
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • DOI 10.1016/j.ymeth.2004.10.010, Glycosylation, Glycoprotein Quality Control, and Stress Responses in the Endoplasmic Reticulum
    • A.S. Lee The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress Methods 35 2005 373 381 (Pubitemid 40445371)
    • (2005) Methods , vol.35 , Issue.4 , pp. 373-381
    • Lee, A.S.1
  • 20
    • 33747849846 scopus 로고    scopus 로고
    • Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1
    • DOI 10.1016/j.cmet.2006.07.007, PII S1550413106002701
    • K.L. Lipson, S.G. Fonseca, S. Ishigaki, L.X. Nguyen, E. Foss, and R. Bortell Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1 Cell Metab 4 2006 245 254 (Pubitemid 44283955)
    • (2006) Cell Metabolism , vol.4 , Issue.3 , pp. 245-254
    • Lipson, K.L.1    Fonseca, S.G.2    Ishigaki, S.3    Nguyen, L.X.4    Foss, E.5    Bortell, R.6    Rossini, A.A.7    Urano, F.8
  • 21
    • 33746500168 scopus 로고    scopus 로고
    • GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development
    • DOI 10.1128/MCB.00779-06
    • S. Luo, C. Mao, B. Lee, and A.S. Lee GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development Mol Cell Biol 26 2006 5688 5697 (Pubitemid 44134326)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5688-5697
    • Luo, S.1    Mao, C.2    Lee, B.3    Lee, A.S.4
  • 22
    • 82355163415 scopus 로고    scopus 로고
    • Poly(A) tail length of neurohypophysial hormones is shortened under endoplasmic reticulum stress
    • Y. Morishita, H. Arima, M. Hiroi, M. Hayashi, D. Hagiwara, and N. Asai Poly(A) tail length of neurohypophysial hormones is shortened under endoplasmic reticulum stress Endocrinology 152 2011 4846 4855
    • (2011) Endocrinology , vol.152 , pp. 4846-4855
    • Morishita, Y.1    Arima, H.2    Hiroi, M.3    Hayashi, M.4    Hagiwara, D.5    Asai, N.6
  • 23
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • S. Munro, and H.R. Pelham An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein Cell 46 1986 291 300
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.2
  • 24
    • 79951537603 scopus 로고    scopus 로고
    • Beyond the endoplasmic reticulum: Atypical GRP78 in cell viability, signalling and therapeutic targeting
    • M. Ni, Y. Zhang, and A.S. Lee Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting Biochem J 434 2011 181 188
    • (2011) Biochem J , vol.434 , pp. 181-188
    • Ni, M.1    Zhang, Y.2    Lee, A.S.3
  • 26
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor
    • DOI 10.1074/jbc.275.18.13727
    • U.E. Petaja-Repo, M. Hogue, A. Laperriere, P. Walker, and M. Bouvier Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor J Biol Chem 275 2000 13727 13736 (Pubitemid 30257444)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13727-13736
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Walker, P.4    Bouvier, M.5
  • 28
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • D. Ron, and P. Walter Signal integration in the endoplasmic reticulum unfolded protein response Nat Rev Mol Cell Biol 8 2007 519 529 (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 29
    • 0347600942 scopus 로고    scopus 로고
    • A murine model of autosomal dominant neurohypophyseal diabetes insipidus reveals progressive loss of vasopressin-producing neurons
    • DOI 10.1172/JCI200318616
    • T.A. Russell, M. Ito, R.N. Yu, F.A. Martinson, J. Weiss, and J.L. Jameson A murine model of autosomal dominant neurohypophyseal diabetes insipidus reveals progressive loss of vasopressin-producing neurons J Clin Invest 112 2003 1697 1706 (Pubitemid 38063727)
    • (2003) Journal of Clinical Investigation , vol.112 , Issue.11 , pp. 1697-1706
    • Russell, T.A.1    Ito, M.2    Ito, M.3    Yu, R.N.4    Martinson, F.A.5    Weiss, J.6    Jameson, J.L.7
  • 31
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
    • DOI 10.1016/S1534-5807(02)00203-4
    • J. Shen, X. Chen, L. Hendershot, and R. Prywes ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals Dev Cell 3 2002 99 111 (Pubitemid 34778399)
    • (2002) Developmental Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 32
    • 0022542529 scopus 로고
    • Interaction of osmotic and volume stimuli in regulation of neurohypophyseal secretion in rats
    • E.M. Stricker, and J.G. Verbalis Interaction of osmotic and volume stimuli in regulation of neurohypophyseal secretion in rats Am J Physiol 250 1986 R267 R275
    • (1986) Am J Physiol , vol.250
    • Stricker, E.M.1    Verbalis, J.G.2
  • 33
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • C.L. Ward, and R.R. Kopito Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins J Biol Chem 269 1994 25710 25718
    • (1994) J Biol Chem , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 34
    • 0025291580 scopus 로고
    • Membrane biogenesis during B cell differentiation: Most endoplasmic reticulum proteins are expressed coordinately
    • D.L. Wiest, J.K. Burkhardt, S. Hester, M. Hortsch, D.I. Meyer, and Y. Argon Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately J Cell Biol 110 1990 1501 1511
    • (1990) J Cell Biol , vol.110 , pp. 1501-1511
    • Wiest, D.L.1    Burkhardt, J.K.2    Hester, S.3    Hortsch, M.4    Meyer, D.I.5    Argon, Y.6
  • 35
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the unfolded protein response
    • J. Wu, and R.J. Kaufman From acute ER stress to physiological roles of the unfolded protein response Cell Death Differ 13 2006 374 384
    • (2006) Cell Death Differ , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 36
    • 0022871457 scopus 로고
    • Regulation of vasopressin gene expression in rat hypothalamic neurons. Response to osmotic stimulation
    • H.H. Zingg, D. Lefebvre, and G. Almazan Regulation of vasopressin gene expression in rat hypothalamic neurons. Response to osmotic stimulation J Biol Chem 261 1986 12956 12959 (Pubitemid 17006861)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.28 , pp. 12956-12959
    • Zingg, H.H.1    Lefebvre, D.2    Almazan, G.3


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