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Volumn 7, Issue , 2017, Pages

PLIN2 is a Key Regulator of the Unfolded Protein Response and Endoplasmic Reticulum Stress Resolution in Pancreatic β Cells

Author keywords

[No Author keywords available]

Indexed keywords

ADIPOPHILIN; FATTY ACID; OLEIC ACID; SMALL INTERFERING RNA; TUNICAMYCIN;

EID: 85010006540     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep40855     Document Type: Article
Times cited : (55)

References (43)
  • 1
    • 0026051640 scopus 로고
    • Measuring the balance between insulin synthesis and insulin release
    • Schuit, F. C., Kiekens, R. & Pipeleers, D. G. Measuring the balance between insulin synthesis and insulin release. Biochem. Biophys. Res. Commun. 178, 1182-1187 (1991).
    • (1991) Biochem. Biophys. Res Commun , vol.178 , pp. 1182-1187
    • Schuit, F.C.1    Kiekens, R.2    Pipeleers, D.G.3
  • 2
    • 0036895383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the development of diabetes: A review
    • Harding, H. P. & Ron, D. Endoplasmic reticulum stress and the development of diabetes: A review. Diabetes 51, Suppl 3, S455-61 (2002).
    • (2002) Diabetes , vol.51 , pp. S455-S461
    • Harding, H.P.1    Ron, D.2
  • 3
    • 84861905329 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and type 2 diabetes
    • Back, S. H. & Kaufman, R. J. Endoplasmic reticulum stress and type 2 diabetes. Annu. Rev. Biochem. 81, 767-793 (2012).
    • (2012) Annu. Rev Biochem , vol.81 , pp. 767-793
    • Back, S.H.1    Kaufman, R.J.2
  • 4
    • 33847677975 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes
    • Laybutt, D. R. et al. Endoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes. Diabetologia 50, 752-763 (2007).
    • (2007) Diabetologia , vol.50 , pp. 752-763
    • Laybutt, D.R.1
  • 5
    • 34547638958 scopus 로고    scopus 로고
    • High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated beta-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes
    • Huang, C. J. et al. High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated beta-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes. Diabetes 56, 2016-2027 (2007).
    • (2007) Diabetes , vol.56 , pp. 2016-2027
    • Huang, C.J.1
  • 6
    • 35848963392 scopus 로고    scopus 로고
    • The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients
    • Marchetti, P. et al. The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients. Diabetologia 50, 2486-2494 (2007).
    • (2007) Diabetologia , vol.50 , pp. 2486-2494
    • Marchetti, P.1
  • 7
    • 8844255630 scopus 로고    scopus 로고
    • Free fatty acids in obesity and type 2 diabetes: Defining their role in the development of insulin resistance and beta-cell dysfunction
    • Boden, G. & Shulman, G. I. Free fatty acids in obesity and type 2 diabetes: defining their role in the development of insulin resistance and beta-cell dysfunction. Eur. J. Clin. Invest. 32 Suppl 3, 14-23 (2002).
    • (2002) Eur. J. Clin Invest , vol.32 , pp. 14-23
    • Boden, G.1    Shulman, G.I.2
  • 8
    • 66349128492 scopus 로고    scopus 로고
    • PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores
    • Bickel, P. E., Tansey, J. T. & Welte, M. A. PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores. Biochim. Biophys. Acta 1791, 419-440 (2009).
    • (2009) Biochim. Biophys Acta , vol.1791 , pp. 419-440
    • Bickel, P.E.1    Tansey, J.T.2    Welte, M.A.3
  • 9
    • 84856656225 scopus 로고    scopus 로고
    • Characterization of the lipid droplet proteome of a clonal insulinproducing beta-cell line (INS-1 832/13)
    • Larsson, S., Resjo, S., Gomez, M. F., James, P. & Holm, C. Characterization of the lipid droplet proteome of a clonal insulinproducing beta-cell line (INS-1 832/13). J. Proteome Res. 11, 1264-1273 (2012).
    • (2012) J Proteome Res , vol.11 , pp. 1264-1273
    • Larsson, S.1    Resjo, S.2    Gomez, M.F.3    James, P.4    Holm, C.5
  • 10
    • 0033546310 scopus 로고    scopus 로고
    • Adipose differentiation related protein (ADRP) expressed in transfected COS-7 cells selectively stimulates long chain fatty acid uptake
    • Gao, J. & Serrero, G. Adipose differentiation related protein (ADRP) expressed in transfected COS-7 cells selectively stimulates long chain fatty acid uptake. J. Biol. Chem. 274, 16825-16830 (1999).
    • (1999) J. Biol Chem , vol.274 , pp. 16825-16830
    • Gao, J.1    Serrero, G.2
  • 11
    • 0036786517 scopus 로고    scopus 로고
    • ADRP stimulates lipid accumulation and lipid droplet formation in murine fibroblasts
    • Imamura, M. et al. ADRP stimulates lipid accumulation and lipid droplet formation in murine fibroblasts. Am. J. Physiol. Endocrinol. Metab. 283, E775-83 (2002).
    • (2002) Am. J. Physiol. Endocrinol Metab , vol.283 , pp. E775-E783
    • Imamura, M.1
  • 12
    • 33646863002 scopus 로고    scopus 로고
    • PPARalpha activators and fasting induce the expression of adipose differentiation-related protein in liver
    • Dalen, K. T., Ulven, S. M., Arntsen, B. M., Solaas, K. & Nebb, H. I. PPARalpha activators and fasting induce the expression of adipose differentiation-related protein in liver. J. Lipid Res. 47, 931-943 (2006).
    • (2006) J Lipid Res , vol.47 , pp. 931-943
    • Dalen, K.T.1    Ulven, S.M.2    Arntsen, B.M.3    Solaas, K.4    Nebb, H.I.5
  • 13
    • 31344437783 scopus 로고    scopus 로고
    • Protection against fatty liver but normal adipogenesis in mice lacking adipose differentiation-related protein
    • Chang, B. H. et al. Protection against fatty liver but normal adipogenesis in mice lacking adipose differentiation-related protein. Mol. Cell. Biol. 26, 1063-1076 (2006).
    • (2006) Mol. Cell Biol , vol.26 , pp. 1063-1076
    • Chang, B.H.1
  • 14
    • 77956800507 scopus 로고    scopus 로고
    • Absence of adipose differentiation related protein upregulates hepatic VLDL secretion, relieves hepatosteatosis, and improves whole body insulin resistance in leptin-deficient mice
    • Chang, B. H., Li, L., Saha, P. & Chan, L. Absence of adipose differentiation related protein upregulates hepatic VLDL secretion, relieves hepatosteatosis, and improves whole body insulin resistance in leptin-deficient mice. J. Lipid Res. 51, 2132-2142 (2010).
    • (2010) J Lipid Res , vol.51 , pp. 2132-2142
    • Chang, B.H.1    Li, L.2    Saha, P.3    Chan, L.4
  • 15
    • 77954890412 scopus 로고    scopus 로고
    • Adipose differentiation-related protein regulates lipids and insulin in pancreatic islets
    • Faleck, D. M. et al. Adipose differentiation-related protein regulates lipids and insulin in pancreatic islets. Am. J. Physiol. Endocrinol. Metab. 299, E249-57 (2010).
    • (2010) Am. J. Physiol. Endocrinol Metab , vol.299 , pp. E249-E257
    • Faleck, D.M.1
  • 16
    • 58149337392 scopus 로고    scopus 로고
    • Cytokine-induced beta-cell death is independent of endoplasmic reticulum stress signaling
    • Akerfeldt, M. C. et al. Cytokine-induced beta-cell death is independent of endoplasmic reticulum stress signaling. Diabetes 57, 3034-3044 (2008).
    • (2008) Diabetes , vol.57 , pp. 3034-3044
    • Akerfeldt, M.C.1
  • 17
    • 33745116619 scopus 로고    scopus 로고
    • Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis
    • Karaskov, E. et al. Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. Endocrinology 147, 3398-3407 (2006).
    • (2006) Endocrinology , vol.147 , pp. 3398-3407
    • Karaskov, E.1
  • 18
    • 9244231766 scopus 로고    scopus 로고
    • Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: Role of nuclear factor-kappaB and endoplasmic reticulum stress
    • Kharroubi, I. et al. Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: role of nuclear factor-kappaB and endoplasmic reticulum stress. Endocrinology 145, 5087-5096 (2004).
    • (2004) Endocrinology , vol.145 , pp. 5087-5096
    • Kharroubi, I.1
  • 19
    • 35448994352 scopus 로고    scopus 로고
    • Insulin gene mutations as a cause of permanent neonatal diabetes
    • Stoy, J. et al. Insulin gene mutations as a cause of permanent neonatal diabetes. Proc. Natl. Acad. Sci. USA 104, 15040-15044 (2007).
    • (2007) Proc. Natl. Acad. Sci USA , vol.104 , pp. 15040-15044
    • Stoy, J.1
  • 20
    • 56849124394 scopus 로고    scopus 로고
    • Permanent neonatal diabetes mellitus due to a C96Y heterozygous mutation in the insulin gene. A case report
    • Ahamed, A. et al. Permanent neonatal diabetes mellitus due to a C96Y heterozygous mutation in the insulin gene. A case report. JOP 9, 715-718 (2008).
    • (2008) JOP , vol.9 , pp. 715-718
    • Ahamed, A.1
  • 21
    • 84973922991 scopus 로고    scopus 로고
    • Monogenic diabetes: What it teaches us on the common forms of Type 1 and Type 2 Diabetes
    • Yang, Y. & Chan, L. Monogenic Diabetes: What It Teaches Us on the Common Forms of Type 1 and Type 2 Diabetes. Endocr. Rev. 37, 190-222 (2016).
    • (2016) Endocr Rev , vol.37 , pp. 190-222
    • Yang, Y.1    Chan, L.2
  • 22
    • 0030907296 scopus 로고    scopus 로고
    • A novel locus, Mody4, distal to D7Mit189 on chromosome 7 determines early-onset NIDDM in nonobese C57BL/6 (Akita) mutant mice
    • Yoshioka, M., Kayo, T., Ikeda, T. & Koizumi, A. A novel locus, Mody4, distal to D7Mit189 on chromosome 7 determines early-onset NIDDM in nonobese C57BL/6 (Akita) mutant mice. Diabetes 46, 887-894 (1997).
    • (1997) Diabetes , vol.46 , pp. 887-894
    • Yoshioka, M.1    Kayo, T.2    Ikeda, T.3    Koizumi, A.4
  • 23
    • 0032918044 scopus 로고    scopus 로고
    • A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse
    • Wang, J. et al. A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse. J. Clin. Invest. 103, 27-37 (1999).
    • (1999) J. Clin Invest , vol.103 , pp. 27-37
    • Wang, J.1
  • 24
    • 1642413540 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+ /Akita pancreatic beta cells
    • Nozaki, J. et al. The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+ /Akita pancreatic beta cells. Genes Cells 9, 261-270 (2004).
    • (2004) Genes Cells , vol.9 , pp. 261-270
    • Nozaki, J.1
  • 25
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa, T. et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403, 98-103 (2000).
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 26
    • 74949118002 scopus 로고    scopus 로고
    • Ablation of C/EBPbeta alleviates ER stress and pancreatic beta cell failure through the GRP78 chaperone in mice
    • Matsuda, T. et al. Ablation of C/EBPbeta alleviates ER stress and pancreatic beta cell failure through the GRP78 chaperone in mice. J. Clin. Invest. 120, 115-126 (2010).
    • (2010) J. Clin Invest , vol.120 , pp. 115-126
    • Matsuda, T.1
  • 27
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales, S., McDonald, K. L. & Walter, P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 4, e423 (2006).
    • (2006) PLoS Biol , vol.4 , pp. e423
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 28
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • Ogata, M. et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol. Cell. Biol. 26, 9220-9231 (2006).
    • (2006) Mol. Cell Biol , vol.26 , pp. 9220-9231
    • Ogata, M.1
  • 29
    • 30044445455 scopus 로고    scopus 로고
    • Post-Translational regulation of adipose differentiation-related protein by the ubiquitin/proteasome pathway
    • Xu, G. et al. Post-Translational regulation of adipose differentiation-related protein by the ubiquitin/proteasome pathway. J. Biol. Chem. 280, 42841-42847 (2005).
    • (2005) J. Biol Chem , vol.280 , pp. 42841-42847
    • Xu, G.1
  • 30
    • 57049111040 scopus 로고    scopus 로고
    • UPR pathways combine to prevent hepatic steatosis caused by ER stress-mediated suppression of transcriptional master regulators
    • Rutkowski, D. T. et al. UPR pathways combine to prevent hepatic steatosis caused by ER stress-mediated suppression of transcriptional master regulators. Dev. Cell. 15, 829-840 (2008).
    • (2008) Dev Cell , vol.15 , pp. 829-840
    • Rutkowski, D.T.1
  • 31
    • 14044261099 scopus 로고    scopus 로고
    • Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3
    • Kim, A. J., Shi, Y., Austin, R. C. & Werstuck, G. H. Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3. J. Cell. Sci. 118, 89-99 (2005).
    • (2005) J. Cell Sci , vol.118 , pp. 89-99
    • Kim, A.J.1    Shi, Y.2    Austin, R.C.3    Werstuck, G.H.4
  • 32
    • 67649646763 scopus 로고    scopus 로고
    • Perilipin is present in islets of Langerhans and protects against lipotoxicity when overexpressed in the beta-cell line INS-1
    • Borg, J. et al. Perilipin is present in islets of Langerhans and protects against lipotoxicity when overexpressed in the beta-cell line INS-1. Endocrinology 150, 3049-3057 (2009).
    • (2009) Endocrinology , vol.150 , pp. 3049-3057
    • Borg, J.1
  • 34
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari, S. et al. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J. Clin. Invest. 109, 525-532 (2002).
    • (2002) J. Clin Invest , vol.109 , pp. 525-532
    • Oyadomari, S.1
  • 35
    • 84892941002 scopus 로고    scopus 로고
    • P85alpha deficiency protects beta-cells from endoplasmic Reticulum Stress-Induced Apoptosis
    • Winnay, J. N., Dirice, E., Liew, C. W., Kulkarni, R. N. & Kahn, C. R. P85alpha Deficiency Protects Beta-Cells from Endoplasmic Reticulum Stress-Induced Apoptosis. Proc. Natl. Acad. Sci. USA 111, 1192-1197 (2014).
    • (2014) Proc. Natl. Acad. Sci USA , vol.111 , pp. 1192-1197
    • Winnay, J.N.1    Dirice, E.2    Liew, C.W.3    Kulkarni, R.N.4    Kahn, C.R.5
  • 36
    • 84875416620 scopus 로고    scopus 로고
    • Stimulation of autophagy improves endoplasmic reticulum stress-induced diabetes
    • Bachar-Wikstrom, E. et al. Stimulation of autophagy improves endoplasmic reticulum stress-induced diabetes. Diabetes 62, 1227-1237 (2013).
    • (2013) Diabetes , vol.62 , pp. 1227-1237
    • Bachar-Wikstrom, E.1
  • 37
    • 52749094770 scopus 로고    scopus 로고
    • Loss of autophagy diminishes pancreatic beta cell mass and function with resultant hyperglycemia
    • Jung, H. S. et al. Loss of autophagy diminishes pancreatic beta cell mass and function with resultant hyperglycemia. Cell. Metab. 8, 318-324 (2008).
    • (2008) Cell Metab , vol.8 , pp. 318-324
    • Jung, H.S.1
  • 38
    • 52749093177 scopus 로고    scopus 로고
    • Autophagy is important in islet homeostasis and compensatory increase of beta cell mass in response to high-fat diet
    • Ebato, C. et al. Autophagy is important in islet homeostasis and compensatory increase of beta cell mass in response to high-fat diet. Cell. Metab. 8, 325-332 (2008).
    • (2008) Cell Metab , vol.8 , pp. 325-332
    • Ebato, C.1
  • 39
    • 84975175105 scopus 로고    scopus 로고
    • Autophagy is a major regulator of beta cell insulin homeostasis
    • Riahi, Y. et al. Autophagy is a major regulator of beta cell insulin homeostasis. Diabetologia 59, 1480-1491 (2016).
    • (2016) Diabetologia , vol.59 , pp. 1480-1491
    • Riahi, Y.1
  • 40
    • 58149463600 scopus 로고    scopus 로고
    • Protective role of autophagy in palmitate-induced INS-1 beta-cell death
    • Choi, S. E. et al. Protective role of autophagy in palmitate-induced INS-1 beta-cell death. Endocrinology 150, 126-134 (2009).
    • (2009) Endocrinology , vol.150 , pp. 126-134
    • Choi, S.E.1
  • 41
    • 84855597740 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and lipid metabolism: Mechanisms and therapeutic potential
    • Basseri, S. & Austin, R. C. Endoplasmic reticulum stress and lipid metabolism: mechanisms and therapeutic potential. Biochem. Res. Int. 2012, 841362 (2012).
    • (2012) Biochem. Res Int , vol.2012 , pp. 841362
    • Basseri, S.1    Austin, R.C.2
  • 42
    • 33846211417 scopus 로고    scopus 로고
    • ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation
    • Kouroku, Y. et al. ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ. 14, 230-239 (2007).
    • (2007) Cell Death Differ , vol.14 , pp. 230-239
    • Kouroku, Y.1
  • 43
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding, W. X. et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am. J. Pathol. 171, 513-524 (2007).
    • (2007) Am. J Pathol , vol.171 , pp. 513-524
    • Ding, W.X.1


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