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Volumn 1842, Issue 9, 2014, Pages 1762-1769

Extra-nuclear telomerase reverse transcriptase (TERT) regulates glucose transport in skeletal muscle cells

Author keywords

Ageing; Diabetes; Glucose transporter; Insulin; Muscle; TERT

Indexed keywords

DEOXYGLUCOSE; GLUCOSE TRANSPORTER; GLUCOSE TRANSPORTER 1; GLUCOSE TRANSPORTER 12; GLUCOSE TRANSPORTER 4; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; TELOMERASE REVERSE TRANSCRIPTASE; UNCLASSIFIED DRUG; INSULIN; SMALL INTERFERING RNA;

EID: 84904343124     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2014.06.018     Document Type: Article
Times cited : (25)

References (37)
  • 1
    • 77049106292 scopus 로고    scopus 로고
    • Association of telomere length with type 2 diabetes, oxidative stress and UCP2 gene variation
    • Salpea K.D., Talmud P.J., Cooper J.A., Maubaret C.G., Stephens J.W., et al. Association of telomere length with type 2 diabetes, oxidative stress and UCP2 gene variation. Atherosclerosis 2010, 209:42-50.
    • (2010) Atherosclerosis , vol.209 , pp. 42-50
    • Salpea, K.D.1    Talmud, P.J.2    Cooper, J.A.3    Maubaret, C.G.4    Stephens, J.W.5
  • 3
    • 84860244616 scopus 로고    scopus 로고
    • Accelerated aging as evidenced by increased telomere shortening and mitochondrial DNA depletion in patients with type 2 diabetes
    • Monickaraj F., Aravind S., Gokulakrishnan K., Sathishkumar C., Prabu P., et al. Accelerated aging as evidenced by increased telomere shortening and mitochondrial DNA depletion in patients with type 2 diabetes. Mol. Cell. Biochem. 2012, 365:343-350.
    • (2012) Mol. Cell. Biochem. , vol.365 , pp. 343-350
    • Monickaraj, F.1    Aravind, S.2    Gokulakrishnan, K.3    Sathishkumar, C.4    Prabu, P.5
  • 4
    • 0037148271 scopus 로고    scopus 로고
    • Telomerase in the human organism
    • Collins K., Mitchell J.R. Telomerase in the human organism. Oncogene 2002, 21:564-579.
    • (2002) Oncogene , vol.21 , pp. 564-579
    • Collins, K.1    Mitchell, J.R.2
  • 6
    • 34548710739 scopus 로고    scopus 로고
    • Telomere dynamics in arteries and mononuclear cells of diabetic patients: effect of diabetes and of glycemic control
    • Uziel O., Singer J.A., Danicek V., Sahar G., Berkov E., et al. Telomere dynamics in arteries and mononuclear cells of diabetic patients: effect of diabetes and of glycemic control. Exp. Gerontol. 2007, 42:971-978.
    • (2007) Exp. Gerontol. , vol.42 , pp. 971-978
    • Uziel, O.1    Singer, J.A.2    Danicek, V.3    Sahar, G.4    Berkov, E.5
  • 7
  • 8
    • 79952500119 scopus 로고    scopus 로고
    • Short telomeres compromise β-cell signaling and survival
    • Guo N., Parry E.M., Li L.S., Kembou F., Lauder N., et al. Short telomeres compromise β-cell signaling and survival. PLoS One 2011, 6:e17858.
    • (2011) PLoS One , vol.6
    • Guo, N.1    Parry, E.M.2    Li, L.S.3    Kembou, F.4    Lauder, N.5
  • 9
    • 0036711651 scopus 로고    scopus 로고
    • Subnuclear shuttling of human telomerase induced by transformation and DNA damage
    • Wong J.M., Kusdra L., Collins K. Subnuclear shuttling of human telomerase induced by transformation and DNA damage. Nat. Cell Biol. 2002, 4:731-736.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 731-736
    • Wong, J.M.1    Kusdra, L.2    Collins, K.3
  • 11
    • 43149087522 scopus 로고    scopus 로고
    • Telomerase does not counteract telomere shortening but protects mitochondrial function under oxidative stress
    • Ahmed S., Passos J.F., Birket M.J., Beckmann T., Brings S., et al. Telomerase does not counteract telomere shortening but protects mitochondrial function under oxidative stress. J. Cell Sci. 2008, 121:1046-1053.
    • (2008) J. Cell Sci. , vol.121 , pp. 1046-1053
    • Ahmed, S.1    Passos, J.F.2    Birket, M.J.3    Beckmann, T.4    Brings, S.5
  • 12
    • 0036311278 scopus 로고    scopus 로고
    • Nucleolar localization of hTERT protein is associated with telomerase function
    • Yang Y., Chen Y., Zhang C., Huang H., Weissman S.M. Nucleolar localization of hTERT protein is associated with telomerase function. Exp. Cell Res. 2002, 277:201-209.
    • (2002) Exp. Cell Res. , vol.277 , pp. 201-209
    • Yang, Y.1    Chen, Y.2    Zhang, C.3    Huang, H.4    Weissman, S.M.5
  • 14
    • 0037148277 scopus 로고    scopus 로고
    • Protection of mammalian telomeres
    • de Lange T. Protection of mammalian telomeres. Oncogene 2002, 21:532-540.
    • (2002) Oncogene , vol.21 , pp. 532-540
    • de Lange, T.1
  • 15
    • 66349130192 scopus 로고    scopus 로고
    • Mitochondrial telomerase reverse transcriptase binds to and protects mitochondrial DNA and function from damage
    • Haendeler J., Dröse S., Büchner N., Jakob S., Altschmied J., et al. Mitochondrial telomerase reverse transcriptase binds to and protects mitochondrial DNA and function from damage. Arterioscler. Thromb. Vasc. Biol. 2009, 29:929-935.
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 929-935
    • Haendeler, J.1    Dröse, S.2    Büchner, N.3    Jakob, S.4    Altschmied, J.5
  • 16
    • 33744745014 scopus 로고    scopus 로고
    • Mitochondrial localization of telomerase as a determinant for hydrogen peroxide-induced mitochondrial DNA damage and apoptosis
    • Santos J.H., Meyer J.N., Van Houten B. Mitochondrial localization of telomerase as a determinant for hydrogen peroxide-induced mitochondrial DNA damage and apoptosis. Hum. Mol. Genet. 2006, 15:1757-1768.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1757-1768
    • Santos, J.H.1    Meyer, J.N.2    Van Houten, B.3
  • 17
    • 67650627734 scopus 로고    scopus 로고
    • Telomerase, mitochondria and oxidative stress
    • Saretzki G. Telomerase, mitochondria and oxidative stress. Exp. Gerontol. 2009, 44:485-492.
    • (2009) Exp. Gerontol. , vol.44 , pp. 485-492
    • Saretzki, G.1
  • 18
    • 0029264736 scopus 로고
    • Fuel selection at the level of mitochondria in mammalian tissues
    • Denton R.M., McCormack J.G. Fuel selection at the level of mitochondria in mammalian tissues. Proc. Nutr. Soc. 1995, 54:11-22.
    • (1995) Proc. Nutr. Soc. , vol.54 , pp. 11-22
    • Denton, R.M.1    McCormack, J.G.2
  • 19
    • 18244401352 scopus 로고    scopus 로고
    • Mitochondrial tissue specificity of substrates utilisation in rat cardiac and skeletal muscles
    • Ponsot E., Zoll J., N'guessan B., Ribera F., Lampert E., et al. Mitochondrial tissue specificity of substrates utilisation in rat cardiac and skeletal muscles. J. Cell. Physiol. 2005, 203:479-486.
    • (2005) J. Cell. Physiol. , vol.203 , pp. 479-486
    • Ponsot, E.1    Zoll, J.2    N'guessan, B.3    Ribera, F.4    Lampert, E.5
  • 20
    • 79951787601 scopus 로고    scopus 로고
    • Telomerase deficiency impairs glucose metabolism and insulin secretion
    • Kuhlow D., Florian S., von Figura G., Weimer S., Schulz N., et al. Telomerase deficiency impairs glucose metabolism and insulin secretion. Aging 2010, 2:650-658.
    • (2010) Aging , vol.2 , pp. 650-658
    • Kuhlow, D.1    Florian, S.2    von Figura, G.3    Weimer, S.4    Schulz, N.5
  • 21
    • 77952305618 scopus 로고    scopus 로고
    • Glucose restriction can extend normal cell lifespan and impair precancerous cell growth through epigenetic control of hTERT and p16 expression
    • Li Y., Liu L., Tollefsbol T.O. Glucose restriction can extend normal cell lifespan and impair precancerous cell growth through epigenetic control of hTERT and p16 expression. FASEB J. 2010, 24:1442-1453.
    • (2010) FASEB J. , vol.24 , pp. 1442-1453
    • Li, Y.1    Liu, L.2    Tollefsbol, T.O.3
  • 22
    • 3042672437 scopus 로고    scopus 로고
    • Induction of hTERT expression and phosphorylation by estrogen via Akt cascade in human ovarian cancer cell lines
    • Kimura A., Ohmichi M., Kawagoe J., Kyo S., Mabuchi S., et al. Induction of hTERT expression and phosphorylation by estrogen via Akt cascade in human ovarian cancer cell lines. Oncogene 2004, 23:4505-4515.
    • (2004) Oncogene , vol.23 , pp. 4505-4515
    • Kimura, A.1    Ohmichi, M.2    Kawagoe, J.3    Kyo, S.4    Mabuchi, S.5
  • 23
    • 0035937503 scopus 로고    scopus 로고
    • Pro-atherogenic factors induce telomerase inactivation in endothelial cells through an Akt-dependent mechanism
    • Breitschopf K., Zeiher A.M., Dimmeler S. Pro-atherogenic factors induce telomerase inactivation in endothelial cells through an Akt-dependent mechanism. FEBS Lett. 2001, 493:21-25.
    • (2001) FEBS Lett. , vol.493 , pp. 21-25
    • Breitschopf, K.1    Zeiher, A.M.2    Dimmeler, S.3
  • 24
    • 0032765047 scopus 로고    scopus 로고
    • Studies of the molecular mechanisms in the regulation of telomerase activity
    • Liu J.P. Studies of the molecular mechanisms in the regulation of telomerase activity. FASEB J. 1999, 13:2091-2104.
    • (1999) FASEB J. , vol.13 , pp. 2091-2104
    • Liu, J.P.1
  • 25
    • 0033532056 scopus 로고    scopus 로고
    • Akt protein kinase enhances human telomerase activity through phosphorylation of telomerase reverse transcriptase subunit
    • Kang S.S., Kwon T., Kwon D.Y., Do S.I. Akt protein kinase enhances human telomerase activity through phosphorylation of telomerase reverse transcriptase subunit. J. Biol. Chem. 1999, 274:13085-13090.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13085-13090
    • Kang, S.S.1    Kwon, T.2    Kwon, D.Y.3    Do, S.I.4
  • 26
    • 1542512436 scopus 로고    scopus 로고
    • TNFalpha induces rapid activation and nuclear translocation of telomerase in human lymphocytes
    • Akiyama M., Yamada O., Hideshima T., Yanagisawa T., Yokoi K., et al. TNFalpha induces rapid activation and nuclear translocation of telomerase in human lymphocytes. Biochem. Biophys. Res. Commun. 2004, 316:528-532.
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 528-532
    • Akiyama, M.1    Yamada, O.2    Hideshima, T.3    Yanagisawa, T.4    Yokoi, K.5
  • 27
    • 0027140017 scopus 로고
    • A rapid preparation of primary cultures of mouse skeletal muscle cells
    • Metzinger L., Poindron P., Passaquin A.C. A rapid preparation of primary cultures of mouse skeletal muscle cells. Cytotechnology 1993, 13:55-60.
    • (1993) Cytotechnology , vol.13 , pp. 55-60
    • Metzinger, L.1    Poindron, P.2    Passaquin, A.C.3
  • 28
    • 33749240737 scopus 로고    scopus 로고
    • Regulation of glucose transporters by insulin and extracellular glucose in C2C12 myotubes
    • Nedachi T., Kanzaki M. Regulation of glucose transporters by insulin and extracellular glucose in C2C12 myotubes. Am. J. Physiol. Endocrinol. Metab. 2006, 291:E817-E828.
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.291
    • Nedachi, T.1    Kanzaki, M.2
  • 30
  • 31
    • 84866602930 scopus 로고    scopus 로고
    • Progranulin compensates for blocked IGF-1 signaling to promote myotube hypertrophy in C2C12 myoblasts via the PI3K/Akt/mTOR pathway
    • Hu S.Y., Tai C.C., Li Y.H., Wu J.L. Progranulin compensates for blocked IGF-1 signaling to promote myotube hypertrophy in C2C12 myoblasts via the PI3K/Akt/mTOR pathway. FEBS Lett. 2012, 586:3485-3492.
    • (2012) FEBS Lett. , vol.586 , pp. 3485-3492
    • Hu, S.Y.1    Tai, C.C.2    Li, Y.H.3    Wu, J.L.4
  • 32
    • 78449241484 scopus 로고    scopus 로고
    • Resveratrol inhibits mTOR signaling by promoting the interaction between mTOR and DEPTOR
    • Liu M., Wilk S.A., Wang A., Zhou L., Wang R.H., et al. Resveratrol inhibits mTOR signaling by promoting the interaction between mTOR and DEPTOR. J. Biol. Chem. 2010, 285:36387-36394.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36387-36394
    • Liu, M.1    Wilk, S.A.2    Wang, A.3    Zhou, L.4    Wang, R.H.5
  • 33
    • 0035965295 scopus 로고    scopus 로고
    • The mammalian target of rapamycin regulates C2C12 myogenesis via a kinase-independent mechanism
    • Erbay E., Chen J. The mammalian target of rapamycin regulates C2C12 myogenesis via a kinase-independent mechanism. J. Biol. Chem. 2001, 276:36079-36082.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36079-36082
    • Erbay, E.1    Chen, J.2
  • 34
    • 84889024832 scopus 로고    scopus 로고
    • Distinct amino acid-sensing mTOR pathways regulate skeletal myogenesis
    • Yoon M.S., Chen J. Distinct amino acid-sensing mTOR pathways regulate skeletal myogenesis. Mol. Biol. Cell 2013, 24:3754-3763.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3754-3763
    • Yoon, M.S.1    Chen, J.2
  • 35
    • 0000664619 scopus 로고
    • Expression of two glucose transporters, GLUT1 and GLUT3, in cultured cerebellar neurons: evidence for neuron-specific expression of GLUT3
    • Maher F., Davies-Hill T.M., Lysko P.G., Henneberry R.C., Simpson I.A. Expression of two glucose transporters, GLUT1 and GLUT3, in cultured cerebellar neurons: evidence for neuron-specific expression of GLUT3. Mol. Cell. Neurosci. 1991, 2:351-360.
    • (1991) Mol. Cell. Neurosci. , vol.2 , pp. 351-360
    • Maher, F.1    Davies-Hill, T.M.2    Lysko, P.G.3    Henneberry, R.C.4    Simpson, I.A.5
  • 36
    • 0344839033 scopus 로고    scopus 로고
    • Expression and localization of GLUT1 and GLUT12 in prostate carcinoma
    • Chandler J.D., Williams E.D., Slavin J.L., Best J.D., Rogers S. Expression and localization of GLUT1 and GLUT12 in prostate carcinoma. Cancer 2003, 97:2035-2042.
    • (2003) Cancer , vol.97 , pp. 2035-2042
    • Chandler, J.D.1    Williams, E.D.2    Slavin, J.L.3    Best, J.D.4    Rogers, S.5
  • 37
    • 20944449149 scopus 로고    scopus 로고
    • C2C12 skeletal muscle cells exposure to phosphatidylcholine triggers IGF-1 like-responses
    • Rauch C., Loughna P. C2C12 skeletal muscle cells exposure to phosphatidylcholine triggers IGF-1 like-responses. Cell. Physiol. Biochem. 2005, 15:211-224.
    • (2005) Cell. Physiol. Biochem. , vol.15 , pp. 211-224
    • Rauch, C.1    Loughna, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.