메뉴 건너뛰기




Volumn 367, Issue 1-2, 2013, Pages 1-10

Microarray analysis of isolated human islet transcriptome in type 2 diabetes and the role of the ubiquitin-proteasome system in pancreatic beta cell dysfunction

Author keywords

Beta cells; Lipotoxicity; Microarray; Type 2 diabetes; Ubiquitin proteasome system

Indexed keywords

PROTEASOME; TRANSCRIPTOME; UBIQUITIN;

EID: 84873523692     PISSN: 03037207     EISSN: 18728057     Source Type: Journal    
DOI: 10.1016/j.mce.2012.12.001     Document Type: Article
Times cited : (75)

References (70)
  • 1
    • 84855161991 scopus 로고    scopus 로고
    • American Diabetes Association Diagnosis and classification of diabetes mellitus
    • American Diabetes Association Diagnosis and classification of diabetes mellitus. Diabetes Care 2012, 35(1):S64-S71.
    • (2012) Diabetes Care , vol.35 , Issue.1
  • 3
    • 22744459667 scopus 로고    scopus 로고
    • Is insulin signaling molecules misguided in diabetes for ubiquitin-proteasome mediated degradation?
    • Balasubramanyam M., Sampathkumar R., Mohan V. Is insulin signaling molecules misguided in diabetes for ubiquitin-proteasome mediated degradation?. Mol. Cell Biochem. 2005, 275:117-125.
    • (2005) Mol. Cell Biochem. , vol.275 , pp. 117-125
    • Balasubramanyam, M.1    Sampathkumar, R.2    Mohan, V.3
  • 5
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • Bedford L., Lowe J., Dick L.R., Mayer R.J., Brownell J.E. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nat. Rev. Drug. Discov. 2011, 10:29-46.
    • (2011) Nat. Rev. Drug. Discov. , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5
  • 7
    • 79953220639 scopus 로고    scopus 로고
    • The direct effects of tacrolimus and cyclosporin A on isolated human islets: a functional, survival and gene expression study
    • Bugliani M., Masini M., Liechti R., Marselli L., Xenarios I., Boggi U., Filipponi F., Masiello P., Marchetti P. The direct effects of tacrolimus and cyclosporin A on isolated human islets: a functional, survival and gene expression study. Islets 2009, 1:106-110.
    • (2009) Islets , vol.1 , pp. 106-110
    • Bugliani, M.1    Masini, M.2    Liechti, R.3    Marselli, L.4    Xenarios, I.5    Boggi, U.6    Filipponi, F.7    Masiello, P.8    Marchetti, P.9
  • 8
    • 0037219411 scopus 로고    scopus 로고
    • Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes
    • Butler A.E., Janson J., Bonner-Weir S., Ritzel R., Rizza R.A., Butler P.C. Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes. Diabetes 2003, 52:102-110.
    • (2003) Diabetes , vol.52 , pp. 102-110
    • Butler, A.E.1    Janson, J.2    Bonner-Weir, S.3    Ritzel, R.4    Rizza, R.A.5    Butler, P.C.6
  • 11
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: same molecule, different degradation pathways
    • Clague M.J., Urbé S. Ubiquitin: same molecule, different degradation pathways. Cell 2010, 143:682-685.
    • (2010) Cell , vol.143 , pp. 682-685
    • Clague, M.J.1    Urbé, S.2
  • 14
    • 78751490442 scopus 로고    scopus 로고
    • β-Cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency
    • Costes S., Huang C.J., Gurlo T., Daval M., Matveyenko A.V., Rizza R.A., Butler A.E., Butler P.C. β-Cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency. Diabetes 2011, 60:227-238.
    • (2011) Diabetes , vol.60 , pp. 227-238
    • Costes, S.1    Huang, C.J.2    Gurlo, T.3    Daval, M.4    Matveyenko, A.V.5    Rizza, R.A.6    Butler, A.E.7    Butler, P.C.8
  • 17
    • 84885838500 scopus 로고    scopus 로고
    • Type 2 diabetes (T2D) susceptibility loci and beta cell defects in islets (ISLs) from non-diabetic (ND) and T2D subjects
    • Del Guerra S., Groves C., D'aleo V., Lupi R., McCarthy M., Marchetti P. Type 2 diabetes (T2D) susceptibility loci and beta cell defects in islets (ISLs) from non-diabetic (ND) and T2D subjects. Diabetes 2011, 60(1):A387.
    • (2011) Diabetes , vol.60 , Issue.1
    • Del Guerra, S.1    Groves, C.2    D'aleo, V.3    Lupi, R.4    McCarthy, M.5    Marchetti, P.6
  • 19
    • 1842844414 scopus 로고    scopus 로고
    • Decreased beta-cell mass in diabetes: significance, mechanisms and therapeutic implications
    • Donath M.Y., Halban P.A. Decreased beta-cell mass in diabetes: significance, mechanisms and therapeutic implications. Diabetologia 2004, 47:581-589.
    • (2004) Diabetologia , vol.47 , pp. 581-589
    • Donath, M.Y.1    Halban, P.A.2
  • 20
    • 50049086521 scopus 로고    scopus 로고
    • The emerging genetic architecture of type 2 diabetes
    • Doria A., Patti M.E., Kahn C.R. The emerging genetic architecture of type 2 diabetes. Cell Metab. 2008, 8:186-200.
    • (2008) Cell Metab. , vol.8 , pp. 186-200
    • Doria, A.1    Patti, M.E.2    Kahn, C.R.3
  • 21
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • Eizirik D.L., Cardozo A.K., Cnop M. The role for endoplasmic reticulum stress in diabetes mellitus. Endocr. Rev. 2008, 29:42-61.
    • (2008) Endocr. Rev. , vol.29 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 23
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • Fenteany G., Schreiber S.L. Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 1998, 273:8545-8548.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8545-8548
    • Fenteany, G.1    Schreiber, S.L.2
  • 24
  • 25
    • 1342288026 scopus 로고    scopus 로고
    • Affy-analysis of Affymetrix GeneChip data at the probe level
    • Gautier L., Cope L., Bolstad B.M., Irizarry R.A. Affy-analysis of Affymetrix GeneChip data at the probe level. Bioinformatics 2004, 20:307-315.
    • (2004) Bioinformatics , vol.20 , pp. 307-315
    • Gautier, L.1    Cope, L.2    Bolstad, B.M.3    Irizarry, R.A.4
  • 28
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation
    • Hoseki J., Ushioda R., Nagata K. Mechanism and components of endoplasmic reticulum-associated degradation. J. Biochem. 2010, 147:19-25.
    • (2010) J. Biochem. , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 29
    • 65649124922 scopus 로고    scopus 로고
    • Proteasome regulators: activators and inhibitors
    • Huang L., Chen C.H. Proteasome regulators: activators and inhibitors. Curr. Med. Chem. 2009, 16:931-939.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 931-939
    • Huang, L.1    Chen, C.H.2
  • 34
    • 33744965755 scopus 로고    scopus 로고
    • Essential role of ubiquitin-proteasome system in normal regulation of insulin secretion
    • Kawaguchi M., Minami K., Nagashima K., Seino S. Essential role of ubiquitin-proteasome system in normal regulation of insulin secretion. J. Biol. Chem. 2006, 281:13015-13020.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13015-13020
    • Kawaguchi, M.1    Minami, K.2    Nagashima, K.3    Seino, S.4
  • 37
    • 18144363161 scopus 로고    scopus 로고
    • Proteasome inhibition alters glucose-stimulated (pro)insulin secretion and turnover in pancreatic {beta}-cells
    • Kitiphongspattana K., Mathews C.E., Leiter E.H., Gaskins H.R. Proteasome inhibition alters glucose-stimulated (pro)insulin secretion and turnover in pancreatic {beta}-cells. J. Biol. Chem. 2005, 280:15727-15734.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15727-15734
    • Kitiphongspattana, K.1    Mathews, C.E.2    Leiter, E.H.3    Gaskins, H.R.4
  • 38
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: valuable new tools for cell biologists
    • Lee D.H., Goldberg A.L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 1998, 8:397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 41
    • 79952455513 scopus 로고    scopus 로고
    • Prevention of diabetic nephropathy in rats through enhanced renal antioxidative capacity by inhibition of the proteasome
    • Luo Z.F., Qi W., Feng B., Mu J., Zeng W., Guo Y.H., Pang Q., Ye Z.L., Liu L., Yuan F.H. Prevention of diabetic nephropathy in rats through enhanced renal antioxidative capacity by inhibition of the proteasome. Life Sci. 2011, 88:512-520.
    • (2011) Life Sci. , vol.88 , pp. 512-520
    • Luo, Z.F.1    Qi, W.2    Feng, B.3    Mu, J.4    Zeng, W.5    Guo, Y.H.6    Pang, Q.7    Ye, Z.L.8    Liu, L.9    Yuan, F.H.10
  • 45
    • 38149042694 scopus 로고    scopus 로고
    • An overview of pancreatic beta-cell defects in human type 2 diabetes: implications for treatment
    • Marchetti P., Dotta F., Lauro D., Purrello F. An overview of pancreatic beta-cell defects in human type 2 diabetes: implications for treatment. Regul. Pept. 2008, 146:4-11.
    • (2008) Regul. Pept. , vol.146 , pp. 4-11
    • Marchetti, P.1    Dotta, F.2    Lauro, D.3    Purrello, F.4
  • 49
    • 78649842241 scopus 로고    scopus 로고
    • Genomics, type 2 diabetes, and obesity
    • McCarthy M.I. Genomics, type 2 diabetes, and obesity. N. Engl. J. Med. 2010, 363:2339-2350.
    • (2010) N. Engl. J. Med. , vol.363 , pp. 2339-2350
    • McCarthy, M.I.1
  • 50
    • 41849097354 scopus 로고    scopus 로고
    • Beta cell mass in diabetes: a realistic therapeutic target?
    • Mejer J.J. Beta cell mass in diabetes: a realistic therapeutic target?. Diabetologia 2008, 51:703-713.
    • (2008) Diabetologia , vol.51 , pp. 703-713
    • Mejer, J.J.1
  • 51
    • 33644772589 scopus 로고    scopus 로고
    • Impaired gene and protein expression of exocytotic soluble N-ethylmaleimide attachment protein receptor complex proteins in pancreatic islets of type 2 diabetic patients
    • Ostenson C.G., Gaisano H., Sheu L., Tibell A., Bartfai T. Impaired gene and protein expression of exocytotic soluble N-ethylmaleimide attachment protein receptor complex proteins in pancreatic islets of type 2 diabetic patients. Diabetes 2006, 55:435-440.
    • (2006) Diabetes , vol.55 , pp. 435-440
    • Ostenson, C.G.1    Gaisano, H.2    Sheu, L.3    Tibell, A.4    Bartfai, T.5
  • 53
    • 54249104026 scopus 로고    scopus 로고
    • The ubiquitin system, disease, and drug discovery
    • Petroski M.D. The ubiquitin system, disease, and drug discovery. BMC Biochem. 2008, 9(1):S7.
    • (2008) BMC Biochem. , vol.9 , Issue.1
    • Petroski, M.D.1
  • 57
    • 45849141304 scopus 로고    scopus 로고
    • Type 2 diabetes: pathogenesis and treatment
    • Stumvoll M., Goldstein B.J., van Haeften T.W. Type 2 diabetes: pathogenesis and treatment. Lancet 2008, 371:2153-2156.
    • (2008) Lancet , vol.371 , pp. 2153-2156
    • Stumvoll, M.1    Goldstein, B.J.2    van Haeften, T.W.3
  • 60
    • 0033790297 scopus 로고    scopus 로고
    • Lactacystin, a proteasome inhibitor: discovery and its application in cell biology
    • Tomoda H., Omura S. Lactacystin, a proteasome inhibitor: discovery and its application in cell biology. Yakugaku Zasshi 2000, 120:935-949.
    • (2000) Yakugaku Zasshi , vol.120 , pp. 935-949
    • Tomoda, H.1    Omura, S.2
  • 62
    • 34249682591 scopus 로고    scopus 로고
    • Beta-cell failure in diabetes and preservation by clinical treatment
    • Wajchenberg B.L. Beta-cell failure in diabetes and preservation by clinical treatment. Endocr. Rev. 2007, 28:187-218.
    • (2007) Endocr. Rev. , vol.28 , pp. 187-218
    • Wajchenberg, B.L.1
  • 63
    • 2642561229 scopus 로고    scopus 로고
    • Palmitate, but not unsaturated fatty acids, induces the expression of interleukin-6 in human myotubes through proteasome-dependent activation of nuclear factor-kappaB
    • Weigert C., Brodbeck K., Staiger H., Kausch C., Machicao F., Häring H.U., Schleicher E.D. Palmitate, but not unsaturated fatty acids, induces the expression of interleukin-6 in human myotubes through proteasome-dependent activation of nuclear factor-kappaB. J. Biol. Chem. 2004, 279:23942-23952.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23942-23952
    • Weigert, C.1    Brodbeck, K.2    Staiger, H.3    Kausch, C.4    Machicao, F.5    Häring, H.U.6    Schleicher, E.D.7
  • 64
    • 70350330155 scopus 로고    scopus 로고
    • Towards better understanding of the contributions of overwork and glucotoxicity to the beta-cell inadequacy of type 2 diabetes
    • Weir G.C., Marselli L., Marchetti P., Katsuta H., Jung M.H., Bonner-Weir S. Towards better understanding of the contributions of overwork and glucotoxicity to the beta-cell inadequacy of type 2 diabetes. Diabetes Obes. Metab. 2009, 11(Suppl 4):82-90.
    • (2009) Diabetes Obes. Metab. , vol.11 , Issue.SUPPL 4 , pp. 82-90
    • Weir, G.C.1    Marselli, L.2    Marchetti, P.3    Katsuta, H.4    Jung, M.H.5    Bonner-Weir, S.6
  • 65
    • 56649083754 scopus 로고    scopus 로고
    • The UPS in diabetes and obesity
    • Wing S.S. The UPS in diabetes and obesity. BMC Biochem. 2008, 9(1):S6.
    • (2008) BMC Biochem. , vol.9 , Issue.1
    • Wing, S.S.1
  • 66
    • 79952585579 scopus 로고    scopus 로고
    • Integration of clearance mechanisms: the proteasome and autophagy
    • Wong E., Cuervo A.M. Integration of clearance mechanisms: the proteasome and autophagy. Cold. Spring Harb. Perspect Biol. 2010, 2:a006734.
    • (2010) Cold. Spring Harb. Perspect Biol. , vol.2
    • Wong, E.1    Cuervo, A.M.2
  • 67
    • 79951483258 scopus 로고    scopus 로고
    • Structure, assembly and homeostatic regulation of the 26S proteasome
    • Xie Y. Structure, assembly and homeostatic regulation of the 26S proteasome. J. Mol. Cell Biol. 2010, 2:308-317.
    • (2010) J. Mol. Cell Biol. , vol.2 , pp. 308-317
    • Xie, Y.1
  • 68
    • 26844459794 scopus 로고    scopus 로고
    • Role of ubiquitin-proteasome degradation pathway in biogenesis efficiency of {beta}-cell ATP-sensitive potassium channels
    • Yan F.F., Lin C.W., Cartier E.A., Shyng S.L. Role of ubiquitin-proteasome degradation pathway in biogenesis efficiency of {beta}-cell ATP-sensitive potassium channels. Am. J. Physiol. Cell Physiol. 2005, 289:C1351-C1359.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Yan, F.F.1    Lin, C.W.2    Cartier, E.A.3    Shyng, S.L.4
  • 69
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida H. ER stress and diseases. FEBS J. 2007, 274:630-658.
    • (2007) FEBS J. , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 70
    • 70350350874 scopus 로고    scopus 로고
    • Covalent complexes of proteasome model with peptide aldehyde inhibitors MG132 and MG101: docking and molecular dynamics study
    • Zhang S., Shi Y., Jin H., Liu Z., Zhang L., Zhang L. Covalent complexes of proteasome model with peptide aldehyde inhibitors MG132 and MG101: docking and molecular dynamics study. J. Mol. Model. 2009, 15:1481-1490.
    • (2009) J. Mol. Model. , vol.15 , pp. 1481-1490
    • Zhang, S.1    Shi, Y.2    Jin, H.3    Liu, Z.4    Zhang, L.5    Zhang, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.