메뉴 건너뛰기




Volumn 2013, Issue , 2013, Pages

Depletion of luminal pyridine nucleotides in the endoplasmic reticulum activates autophagy with the involvement of mTOR pathway

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE 6 PHOSPHATE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUCOSE TRANSPORTER; INITIATION FACTOR 4E BINDING PROTEIN 1; MAMMALIAN TARGET OF RAPAMYCIN; METYRAPONE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; S6 KINASE; ANTIPORTER; MTOR PROTEIN, HUMAN; NUCLEOTIDE; PYRIDINE DERIVATIVE; SLC37A4 PROTEIN, HUMAN; TARGET OF RAPAMYCIN KINASE;

EID: 84890068740     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/942431     Document Type: Article
Times cited : (6)

References (27)
  • 1
    • 33645980003 scopus 로고    scopus 로고
    • Endoplasmic reticulum: A metabolic compartment
    • 2-s2.0-33645980003 10.1016/j.febslet.2006.03.050
    • Csala M., Bánhegyi G., Benedetti A., Endoplasmic reticulum: a metabolic compartment. FEBS Letters 2006 580 9 2160 2165 2-s2.0-33645980003 10.1016/j.febslet.2006.03.050
    • (2006) FEBS Letters , vol.580 , Issue.9 , pp. 2160-2165
    • Csala, M.1    Bánhegyi, G.2    Benedetti, A.3
  • 2
    • 33750902737 scopus 로고    scopus 로고
    • The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control
    • DOI 10.1089/ars.2006.8.1391
    • Görlach A., Klappa P., Kietzmann T., The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxidants and Redox Signaling 2006 8 9-10 1391 1418 2-s2.0-33750902737 10.1089/ars.2006.8.1391 (Pubitemid 44726319)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.9-10 , pp. 1391-1418
    • Gorlach, A.1    Klappa, P.2    Kietzmann, T.3
  • 3
    • 79952708723 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in liver disease
    • 2-s2.0-79952708723 10.1016/j.jhep.2010.11.005
    • Malhi H., Kaufman R. J., Endoplasmic reticulum stress in liver disease. Journal of Hepatology 2011 54 4 795 809 2-s2.0-79952708723 10.1016/j.jhep.2010. 11.005
    • (2011) Journal of Hepatology , vol.54 , Issue.4 , pp. 795-809
    • Malhi, H.1    Kaufman, R.J.2
  • 4
    • 46649087941 scopus 로고    scopus 로고
    • Metyrapone prevents cortisone-induced preadipocyte differentiation by depleting luminal NADPH of the endoplasmic reticulum
    • 2-s2.0-46649087941 10.1016/j.bcp.2008.05.027
    • Marcolongo P., Senesi S., Gava B., Fulceri R., Sorrentino V., Margittai É., Lizák B., Csala M., Bánhegyi G., Benedetti A., Metyrapone prevents cortisone-induced preadipocyte differentiation by depleting luminal NADPH of the endoplasmic reticulum. Biochemical Pharmacology 2008 76 3 382 390 2-s2.0-46649087941 10.1016/j.bcp.2008.05.027
    • (2008) Biochemical Pharmacology , vol.76 , Issue.3 , pp. 382-390
    • Marcolongo, P.1    Senesi, S.2    Gava, B.3    Fulceri, R.4    Sorrentino, V.5    Margittai, É.6    Lizák, B.7    Csala, M.8    Bánhegyi, G.9    Benedetti, A.10
  • 5
    • 70549099976 scopus 로고    scopus 로고
    • Altered redox state of luminal pyridine nucleotides facilitates the sensitivity towards oxidative injury and leads to endoplasmic reticulum stress dependent autophagy in HepG2 cells
    • 2-s2.0-70549099976 10.1016/j.biocel.2009.10.004
    • Száraz P., Bánhegyi G., Benedetti A., Altered redox state of luminal pyridine nucleotides facilitates the sensitivity towards oxidative injury and leads to endoplasmic reticulum stress dependent autophagy in HepG2 cells. International Journal of Biochemistry and Cell Biology 2010 42 1 157 166 2-s2.0-70549099976 10.1016/j.biocel.2009.10.004
    • (2010) International Journal of Biochemistry and Cell Biology , vol.42 , Issue.1 , pp. 157-166
    • Száraz, P.1    Bánhegyi, G.2    Benedetti, A.3
  • 6
    • 34249814328 scopus 로고    scopus 로고
    • The glucose-6-phosphate transporter-hexose-6-phosphate dehydrogenase- 11β-hydroxysteroid dehydrogenase type 1 system of the adipose tissue
    • DOI 10.1210/en.2006-1472
    • Marcolongo P., Piccirella S., Senesi S., Wunderlich L., Gerin I., Mandl J., Fulceri R., Bánhegyi G., Benedetti A., The glucose-6-phosphate transporter-hexose-6-phosphate dehydrogenase-11 β -hydroxysteroid dehydrogenase type 1 system of the adipose tissue. Endocrinology 2007 148 5 2487 2495 2-s2.0-34249814328 10.1210/en.2006-1472 (Pubitemid 46997033)
    • (2007) Endocrinology , vol.148 , Issue.5 , pp. 2487-2495
    • Marcolongo, P.1    Piccirella, S.2    Senesi, S.3    Wunderlich, L.4    Gerin, I.5    Mandl, J.6    Fulceri, R.7    Banhegyi, G.8    Benedetti, A.9
  • 7
    • 34848854245 scopus 로고    scopus 로고
    • 11β-Hydroxysteroid dehydrogenase type 1 regulation by intracellular glucose 6-phosphate provides evidence for a novel link between glucose metabolism and hypothalamo-pituitary-adrenal axis function
    • DOI 10.1074/jbc.M704144200
    • Walker E. A., Ahmed A., Lavery G. G., Tomlinson J. W., So Y. K., Cooper M. S., Ride J. P., Hughes B. A., Shackleton C. H. L., McKiernan P., Elias E., Chou J. Y., Stewart P. M., 11 β -Hydroxysteroid dehydrogenase type 1 regulation by intracellular glucose 6-phosphate provides evidence for a novel link between glucose metabolism and hypothalamo-pituitary-adrenal axis function. The Journal of Biological Chemistry 2007 282 37 27030 27036 2-s2.0-34848854245 10.1074/jbc.M704144200 (Pubitemid 47501934)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.37 , pp. 27030-27036
    • Walker, E.A.1    Ahmed, A.2    Lavery, G.G.3    Tomlinson, J.W.4    So, Y.K.5    Cooper, M.S.6    Ride, J.P.7    Hughes, B.A.8    Shackleton, C.H.L.9    McKiernan, P.10    Elias, E.11    Chou, J.Y.12    Stewart, P.M.13
  • 8
    • 67449161934 scopus 로고    scopus 로고
    • Hexose-6-phosphate dehydrogenase: Linking endocrinology and metabolism in the endoplasmic reticulum
    • 2-s2.0-67449161934 10.1677/JME-08-0156
    • Bánhegyi G., Csala M., Benedetti A., Hexose-6-phosphate dehydrogenase: linking endocrinology and metabolism in the endoplasmic reticulum. Journal of Molecular Endocrinology 2009 42 4 283 289 2-s2.0-67449161934 10.1677/JME-08-0156
    • (2009) Journal of Molecular Endocrinology , vol.42 , Issue.4 , pp. 283-289
    • Bánhegyi, G.1    Csala, M.2    Benedetti, A.3
  • 9
    • 78249242429 scopus 로고    scopus 로고
    • Decreased prereceptorial glucocorticoid activating capacity in starvation due to an oxidative shift of pyridine nucleotides in the endoplasmic reticulum
    • 2-s2.0-78249242429 10.1016/j.febslet.2010.10.053
    • Kereszturi É., Kálmán F. S., Kardon T., Csala M., Bánhegyi G., Decreased prereceptorial glucocorticoid activating capacity in starvation due to an oxidative shift of pyridine nucleotides in the endoplasmic reticulum. FEBS Letters 2010 584 22 4703 4708 2-s2.0-78249242429 10.1016/j.febslet.2010.10.053
    • (2010) FEBS Letters , vol.584 , Issue.22 , pp. 4703-4708
    • Kereszturi, É.1    Kálmán, F.S.2    Kardon, T.3    Csala, M.4    Bánhegyi, G.5
  • 10
    • 3042595899 scopus 로고    scopus 로고
    • Cooperativity between 11β-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase in the lumen of the endoplasmic reticulum
    • DOI 10.1074/jbc.M404159200
    • Bánhegyi G., Benedetti A., Fulceri R., Senesi S., Cooperativity between 11 β -hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase in the lumen of the endoplasmic reticulum. The Journal of Biological Chemistry 2004 279 26 27017 27021 2-s2.0-3042595899 10.1074/jbc.M404159200 (Pubitemid 38812537)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27017-27021
    • Banhegyi, G.1    Benedetti, A.2    Fulceri, R.3    Senesi, S.4
  • 11
    • 0024422513 scopus 로고
    • Purification and properties of a metyrapone-reducing enzyme from mouse liver microsomes - This ketone is reduced by an aldehyde reductase
    • DOI 10.1016/0006-2952(89)90014-2
    • Maser E., Netter K. J., Purification and properties of a metyrapone-reducing enzyme from mouse liver microsomes-this ketone is reduced by an aldehyde reductase. Biochemical Pharmacology 1989 38 18 3049 3054 2-s2.0-0024422513 10.1016/0006-2952(89)90014-2 (Pubitemid 19222951)
    • (1989) Biochemical Pharmacology , vol.38 , Issue.18 , pp. 3049-3054
    • Maser, E.1    Netter, K.J.2
  • 13
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • 2-s2.0-82255173966 10.1126/science.1209038
    • Walter P., Ron D., The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011 334 6059 1081 1086 2-s2.0-82255173966 10.1126/science.1209038
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 14
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • 2-s2.0-37649005234 10.1016/j.cell.2007.12.018
    • Levine B., Kroemer G., Autophagy in the pathogenesis of disease. Cell 2008 132 1 27 42 2-s2.0-37649005234 10.1016/j.cell.2007.12.018
    • (2008) Cell , vol.132 , Issue.1 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 15
    • 78149475088 scopus 로고    scopus 로고
    • Regulation of mammalian autophagy in physiology and pathophysiology
    • 10.1152/physrev.00030.2009
    • Ravikumar B., Sarkar S., Davies J. E., Regulation of mammalian autophagy in physiology and pathophysiology. Physiological Reviews 2010 90 4 1383 1435 10.1152/physrev.00030.2009
    • (2010) Physiological Reviews , vol.90 , Issue.4 , pp. 1383-1435
    • Ravikumar, B.1    Sarkar, S.2    Davies, J.E.3
  • 16
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • DOI 10.1074/jbc.273.7.3963
    • Noda T., Ohsumi Y., Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. The Journal of Biological Chemistry 1998 273 7 3963 3966 2-s2.0-0032512636 10.1074/jbc.273.7.3963 (Pubitemid 28103257)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.7 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 17
    • 79954592882 scopus 로고    scopus 로고
    • MTOR signaling, function, novel inhibitors, and therapeutic targets
    • 2-s2.0-79954592882 10.2967/jnumed.111.089623
    • Watanabe R., Wei L., Huang J., mTOR signaling, function, novel inhibitors, and therapeutic targets. Journal of Nuclear Medicine 2011 52 4 497 500 2-s2.0-79954592882 10.2967/jnumed.111.089623
    • (2011) Journal of Nuclear Medicine , vol.52 , Issue.4 , pp. 497-500
    • Watanabe, R.1    Wei, L.2    Huang, J.3
  • 18
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • DOI 10.1101/gad.1212704
    • Hay N., Sonenberg N., Upstream and downstream of mTOR. Genes and Development 2004 18 16 1926 1945 2-s2.0-4043171462 10.1101/gad.1212704 (Pubitemid 39071573)
    • (2004) Genes and Development , vol.18 , Issue.16 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 19
    • 78650510609 scopus 로고    scopus 로고
    • MTOR: From growth signal integration to cancer, diabetes and ageing
    • 2-s2.0-78650510609 10.1038/nrm3025
    • Zoncu R., Efeyan A., Sabatini D. M., mTOR: from growth signal integration to cancer, diabetes and ageing. Nature Reviews Molecular Cell Biology 2011 12 1 21 35 2-s2.0-78650510609 10.1038/nrm3025
    • (2011) Nature Reviews Molecular Cell Biology , vol.12 , Issue.1 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 21
    • 79955005054 scopus 로고    scopus 로고
    • Gadd34 induces autophagy through the suppression of the mTOR pathway during starvation
    • 2-s2.0-79955005054 10.1016/j.bbrc.2011.03.077
    • Uddin M. N., Ito S., Nishio N., Suganya T., Isobe K.-I., Gadd34 induces autophagy through the suppression of the mTOR pathway during starvation. Biochemical and Biophysical Research Communications 2011 407 4 692 698 2-s2.0-79955005054 10.1016/j.bbrc.2011.03.077
    • (2011) Biochemical and Biophysical Research Communications , vol.407 , Issue.4 , pp. 692-698
    • Uddin, M.N.1    Ito, S.2    Nishio, N.3    Suganya, T.4    Isobe, K.-I.5
  • 22
    • 84863740827 scopus 로고    scopus 로고
    • The impact of the unfolded protein response on human disease
    • 10.1083/jcb.201110131
    • Wang S. Y., Kaufman R. J., The impact of the unfolded protein response on human disease. Journal of Cell Biology 2012 197 7 857 867 10.1083/jcb.201110131
    • (2012) Journal of Cell Biology , vol.197 , Issue.7 , pp. 857-867
    • Wang, S.Y.1    Kaufman, R.J.2
  • 23
    • 33745167272 scopus 로고    scopus 로고
    • Silencing of the human microsomal glucose-6-phosphate translocase induces glioma cell death: Potential new anticancer target for curcumin
    • DOI 10.1016/j.febslet.2006.05.071, PII S0014579306006880
    • Belkaid A., Copland I. B., Massillon D., Annabi B., Silencing of the human microsomal glucose-6-phosphate translocase induces glioma cell death: potential new anticancer target for curcumin. FEBS Letters 2006 580 15 3746 3752 2-s2.0-33745167272 10.1016/j.febslet.2006.05.071 (Pubitemid 43902814)
    • (2006) FEBS Letters , vol.580 , Issue.15 , pp. 3746-3752
    • Belkaid, A.1    Copland, I.B.2    Massillon, D.3    Annabi, B.4
  • 24
    • 67449161934 scopus 로고    scopus 로고
    • Hexose-6-phosphate dehydrogenase: Linking endocrinology and metabolism in the endoplasmic reticulum
    • 2-s2.0-67449161934 10.1677/JME-08-0156
    • Bánhegyi G., Csala M., Benedetti A., Hexose-6-phosphate dehydrogenase: linking endocrinology and metabolism in the endoplasmic reticulum. Journal of Molecular Endocrinology 2009 42 4 283 289 2-s2.0-67449161934 10.1677/JME-08-0156
    • (2009) Journal of Molecular Endocrinology , vol.42 , Issue.4 , pp. 283-289
    • Bánhegyi, G.1    Csala, M.2    Benedetti, A.3
  • 25
    • 84872076250 scopus 로고    scopus 로고
    • A cellular stress-directed bistable switch controls the crosstalk between autophagy and apoptosis
    • 10.1039/c2mb25261a
    • Kapuy O., Vinod P. K., Mandl J., Bnhegyi G., A cellular stress-directed bistable switch controls the crosstalk between autophagy and apoptosis. Molecular Biosystems 2013 9 2 296 306 10.1039/c2mb25261a
    • (2013) Molecular Biosystems , vol.9 , Issue.2 , pp. 296-306
    • Kapuy, O.1    Vinod, P.K.2    Mandl, J.3    Bnhegyi, G.4
  • 26
    • 61449235398 scopus 로고    scopus 로고
    • Not all substrates are treated equally Implications for mTOR, rapamycin-resistance and cancer therapy
    • 2-s2.0-61449235398
    • Choo A. Y., Blenis J., Not all substrates are treated equally Implications for mTOR, rapamycin-resistance and cancer therapy. Cell Cycle 2009 8 4 567 572 2-s2.0-61449235398
    • (2009) Cell Cycle , vol.8 , Issue.4 , pp. 567-572
    • Choo, A.Y.1    Blenis, J.2
  • 27
    • 81055144867 scopus 로고    scopus 로고
    • S6k1 and 4E-BP1 are independent regulated and control cellular growth in bladder cancer
    • 2-s2.0-81055144867 10.1371/journal.pone.0027509 e27509
    • Nawroth R., Stellwagen F., Schulz W. A., Stoehr R., Hartmann A., Krause B. J., Gschwend J. E., Retz M., S6k1 and 4E-BP1 are independent regulated and control cellular growth in bladder cancer. PLoS ONE 2011 6 11 2-s2.0-81055144867 10.1371/journal.pone.0027509 e27509
    • (2011) PLoS ONE , vol.6 , Issue.11
    • Nawroth, R.1    Stellwagen, F.2    Schulz, W.A.3    Stoehr, R.4    Hartmann, A.5    Krause, B.J.6    Gschwend, J.E.7    Retz, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.