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Volumn 45, Issue 3, 2003, Pages 305-311

Osmotic stress increases cullin-5 (cul-5) mRNA in the rat cerebral cortex, hypothalamus and kidney

Author keywords

Cul 5; Cullin; Osmotic stress; Protein degradation; Ubiquitination; Water deprivation

Indexed keywords

CULLIN 5; MESSENGER RNA; PROTEIN; UNCLASSIFIED DRUG;

EID: 0345269739     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-0102(02)00228-6     Document Type: Article
Times cited : (11)

References (37)
  • 1
    • 0031734667 scopus 로고    scopus 로고
    • Cellular response to osmotic stress in the renal medulla
    • Beck F.X., Burger-Kentischer A., Muller E. Cellular response to osmotic stress in the renal medulla. Pflugers Arch. 436:1998;814-827.
    • (1998) Pflugers Arch. , vol.436 , pp. 814-827
    • Beck, F.X.1    Burger-Kentischer, A.2    Muller, E.3
  • 2
    • 0030467846 scopus 로고    scopus 로고
    • Osmotic regulation of gene expression
    • Burg M.B., Kwon E.D., Kultz D. Osmotic regulation of gene expression. FASEB J. 10:1996;1598-1606.
    • (1996) FASEB J. , vol.10 , pp. 1598-1606
    • Burg, M.B.1    Kwon, E.D.2    Kultz, D.3
  • 5
    • 0031050354 scopus 로고    scopus 로고
    • Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23
    • Byrd P.J., Stankovic T., McConville C.M., Smith A.D., Cooper P.R., Taylor A.M. Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23. Genome Res. 7:1997;71-75.
    • (1997) Genome Res. , vol.7 , pp. 71-75
    • Byrd, P.J.1    Stankovic, T.2    McConville, C.M.3    Smith, A.D.4    Cooper, P.R.5    Taylor, A.M.6
  • 7
    • 0035671658 scopus 로고    scopus 로고
    • Vasopressin-activated calcium-mobilizing (VACM-1) receptor mRNA is present in peripheral organs and the central nervous system of the laboratory rat
    • Ceremuga T.E., Yao X.L., McCabe J.T. Vasopressin-activated calcium-mobilizing (VACM-1) receptor mRNA is present in peripheral organs and the central nervous system of the laboratory rat. Endocr. Res. 27:2001;433-445.
    • (2001) Endocr. Res. , vol.27 , pp. 433-445
    • Ceremuga, T.E.1    Yao, X.L.2    McCabe, J.T.3
  • 8
    • 0035930582 scopus 로고    scopus 로고
    • UV-damaged DNA-binding proteins are targets of cul-4a-mediated ubiquitination and degradation
    • Chen X., Zhang Y., Douglas L., Zhou P. UV-damaged DNA-binding proteins are targets of cul-4a-mediated ubiquitination and degradation. J. Biol. Chem. 276:2001;48175-48182.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48175-48182
    • Chen, X.1    Zhang, Y.2    Douglas, L.3    Zhou, P.4
  • 9
    • 0033643742 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mode of action and clinical implications
    • Ciechanover A., Orian A., Schwartz A.L. The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications. J. Cell Biochem. Suppl. 34:2000;40-51.
    • (2000) J. Cell Biochem. Suppl. , vol.34 , pp. 40-51
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 10
    • 0033279836 scopus 로고    scopus 로고
    • SCF and cullin/ring H2-based ubiquitin ligases
    • Deshaies R.J. SCF and cullin/ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15:1999;435-467.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 12
    • 0029924518 scopus 로고    scopus 로고
    • Ion transport in hepatocytes: Mechanisms and correlations to cell volume, hormone actions and metabolism
    • Graf J., Haussinger D. Ion transport in hepatocytes: mechanisms and correlations to cell volume, hormone actions and metabolism. J. Hepatol. 1:(24):1996;S53-S77.
    • (1996) J. Hepatol. , vol.1 , Issue.24 , pp. 53-S77
    • Graf, J.1    Haussinger, D.2
  • 13
    • 0027499670 scopus 로고
    • Control of brain volume during hyperosmolar and hypoosmolar conditions
    • Gullans S.R., Verbalis J.G. Control of brain volume during hyperosmolar and hypoosmolar conditions. Annu. Rev. Med. 44:1993;289-301.
    • (1993) Annu. Rev. Med. , vol.44 , pp. 289-301
    • Gullans, S.R.1    Verbalis, J.G.2
  • 14
    • 0031004311 scopus 로고    scopus 로고
    • Osmotic regulation of amino acids and system A transport in Madin-Darby canine kidney cells
    • Horio M., Yamauchi A., Moriyama T., Imai E., Orita Y. Osmotic regulation of amino acids and system A transport in Madin-Darby canine kidney cells. Am. J. Physiol. 272:1997;C804-809.
    • (1997) Am. J. Physiol. , vol.272 , pp. 804-809
    • Horio, M.1    Yamauchi, A.2    Moriyama, T.3    Imai, E.4    Orita, Y.5
  • 15
    • 0034038728 scopus 로고    scopus 로고
    • Expression of the genes encoding the vasopressin-activated calcium-mobilizing receptor and the dual angiotensin II/vasopressin receptor in the rat central nervous system
    • Hurbin A., Orcel H., Ferraz C., Moos F.C., Rabie A. Expression of the genes encoding the vasopressin-activated calcium-mobilizing receptor and the dual angiotensin II/vasopressin receptor in the rat central nervous system. J. Neuroendocrinol. 12:2000;677-684.
    • (2000) J. Neuroendocrinol. , vol.12 , pp. 677-684
    • Hurbin, A.1    Orcel, H.2    Ferraz, C.3    Moos, F.C.4    Rabie, A.5
  • 18
    • 0029953780 scopus 로고    scopus 로고
    • Cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family
    • Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M. Cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. Cell. 85:1996;829-839.
    • (1996) Cell , vol.85 , pp. 829-839
    • Kipreos, E.T.1    Lander, L.E.2    Wing, J.P.3    He, W.W.4    Hedgecock, E.M.5
  • 19
    • 0035956920 scopus 로고    scopus 로고
    • Altered ubiquitination and stability of aquaporin-1 in hypertonic stress
    • Leitch V., Agre P., King L.S. Altered ubiquitination and stability of aquaporin-1 in hypertonic stress. Proc. Natl. Acad. Sci. USA. 98:2001;2894-2898.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2894-2898
    • Leitch, V.1    Agre, P.2    King, L.S.3
  • 20
    • 0028958463 scopus 로고
    • Role of organic osmolytes in myelinolysis. A topographic study in rats after rapid correction of hyponatremia
    • Lien Y.H. Role of organic osmolytes in myelinolysis. A topographic study in rats after rapid correction of hyponatremia. J. Clin. Invest. 95:1995;1579-1586.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1579-1586
    • Lien, Y.H.1
  • 21
    • 0023762179 scopus 로고
    • Effect of acute and chronic hypernatremia on myoinositol and sorbitol concentration in rat brain and kidney
    • Lohr J.W., McReynolds J., Grimaldi T., Acara M. Effect of acute and chronic hypernatremia on myoinositol and sorbitol concentration in rat brain and kidney. Life Sci. 43:1988;271-276.
    • (1988) Life Sci. , vol.43 , pp. 271-276
    • Lohr, J.W.1    McReynolds, J.2    Grimaldi, T.3    Acara, M.4
  • 24
  • 25
    • 0036079677 scopus 로고    scopus 로고
    • Involvement of multiple kinase pathways in stimulation of gene transcription by hypertonicity
    • Nahm O., Woo S.K., Handler J.S., Kwon H.M. Involvement of multiple kinase pathways in stimulation of gene transcription by hypertonicity. Am. J. Physiol. Cell Physiol. 282:2002;C49-58.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282 , pp. 49-58
    • Nahm, O.1    Woo, S.K.2    Handler, J.S.3    Kwon, H.M.4
  • 28
    • 0035955629 scopus 로고    scopus 로고
    • Regulation of insulin/insulin-like growth factor-1 signaling by proteasome-mediated degradation of insulin receptor substrate-2
    • Rui L., Fisher T.L., Thomas J., White M.F. Regulation of insulin/insulin-like growth factor-1 signaling by proteasome-mediated degradation of insulin receptor substrate-2. J. Biol. Chem. 276:2001;40362-40367.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40362-40367
    • Rui, L.1    Fisher, T.L.2    Thomas, J.3    White, M.F.4
  • 29
    • 0033568639 scopus 로고    scopus 로고
    • Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cells
    • Singer J.D., Gurian-West M., Clurman B., Roberts J.M. Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cells. Genes Dev. 13:1999;2375-2387.
    • (1999) Genes Dev. , vol.13 , pp. 2375-2387
    • Singer, J.D.1    Gurian-West, M.2    Clurman, B.3    Roberts, J.M.4
  • 30
    • 0025622841 scopus 로고
    • Hyperosmolar states
    • Star R.A. Hyperosmolar states. Am. J. Med. Sci. 300:1990;402-412.
    • (1990) Am. J. Med. Sci. , vol.300 , pp. 402-412
    • Star, R.A.1
  • 32
    • 0021112355 scopus 로고
    • The complete nucleotide sequence of the rat 18S ribosomal RNA gene and comparison with the respective yeast and frog genes
    • Torczynski R., Bollon A.P., Fuke M. The complete nucleotide sequence of the rat 18S ribosomal RNA gene and comparison with the respective yeast and frog genes. Nucleic Acids Res. 11:1983;4879-4890.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 4879-4890
    • Torczynski, R.1    Bollon, A.P.2    Fuke, M.3
  • 33
    • 0029937266 scopus 로고    scopus 로고
    • Quantitative analysis of aquaporin mRNA expression in rat tissues by RNase protection assay
    • Umenishi F., Verkman A.S., Gropper M.A. Quantitative analysis of aquaporin mRNA expression in rat tissues by RNase protection assay. DNA Cell Biol. 15:1996;475-480.
    • (1996) DNA Cell Biol. , vol.15 , pp. 475-480
    • Umenishi, F.1    Verkman, A.S.2    Gropper, M.A.3
  • 34
    • 0034534732 scopus 로고    scopus 로고
    • The hypertonicity-induced Na(+) conductance of rat hepatocytes: Physiological significance and molecular correlate
    • Wehner F., Bohmer C., Heinzinger H., van den Boom F., Tinel H. The hypertonicity-induced Na(+) conductance of rat hepatocytes: physiological significance and molecular correlate. Cell Physiol. Biochem. 10:2000;335-340.
    • (2000) Cell Physiol. Biochem. , vol.10 , pp. 335-340
    • Wehner, F.1    Bohmer, C.2    Heinzinger, H.3    Van den Boom, F.4    Tinel, H.5
  • 36
    • 0000899038 scopus 로고    scopus 로고
    • Nuclear redistribution of tonicity-responsive enhancer binding protein requires proteasome activity
    • Woo S.K., Maouyo D., Handler J.S., Kwon H.M. Nuclear redistribution of tonicity-responsive enhancer binding protein requires proteasome activity. Am. J. Physiol. Cell Physiol. 278:2000;C323-330.
    • (2000) Am. J. Physiol. Cell Physiol. , vol.278 , pp. 323-330
    • Woo, S.K.1    Maouyo, D.2    Handler, J.S.3    Kwon, H.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.