Mitochondrial Dysregulation Secondary to Endoplasmic Reticulum Stress in Autosomal Dominant Tubulointerstitial Kidney Disease - UMOD (ADTKD-UMOD)

Scientific Reports

Volumn 7, Issue , 2017, Pages

  Kemter, Elisabeth ^a   Fröhlich, Thomas ^a   Arnold, Georg J ^a   Wolf, Eckhard ^a   Wanke, Rüdiger ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

FIS1 PROTEIN, MOUSE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MITOCHONDRIAL PROTEIN; NRF1 PROTEIN, MOUSE; NUCLEAR RESPIRATORY FACTOR 1; PROTEIN SERINE THREONINE KINASE; PROTEOME; STK11 PROTEIN, MOUSE; TAMM HORSFALL GLYCOPROTEIN;

ANIMAL; AUTOPHAGY; DISEASE MODEL; ENDOPLASMIC RETICULUM STRESS; ENERGY METABOLISM; GENETICS; INTERSTITIAL NEPHRITIS; KIDNEY MEDULLA; METABOLISM; MITOCHONDRION; MOUSE; PATHOLOGY; PEROXISOME; ULTRASTRUCTURE; UNFOLDED PROTEIN RESPONSE;

AMP-ACTIVATED PROTEIN KINASES; ANIMALS; AUTOPHAGY; DISEASE MODELS, ANIMAL; ENDOPLASMIC RETICULUM STRESS; ENERGY METABOLISM; KIDNEY MEDULLA; MICE; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; NEPHRITIS, INTERSTITIAL; NUCLEAR RESPIRATORY FACTOR 1; PEROXISOMES; PROTEIN-SERINE-THREONINE KINASES; PROTEOME; UNFOLDED PROTEIN RESPONSE; UROMODULIN;

EID: 85013367904     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep42970     Document Type: Article

References (34)

1. Rampoldi, L., Scolari, F., Amoroso, A., Ghiggeri, G. & Devuyst, O. The rediscovery of uromodulin (Tamm-Horsfall protein): from tubulointerstitial nephropathy to chronic kidney disease. Kidney international 80, 338-347, doi: 10.1038/ki.2011.134 (2011)
2. Eckardt, K. U. et al. Autosomal dominant tubulointerstitial kidney disease: diagnosis, classification, and management-A KDIGO consensus report. Kidney international 88, 676-683, doi: 10.1038/ki.2015.28 (2015)
3. Serafini-Cessi, F., Malagolini, N. & Cavallone, D. Tamm-Horsfall glycoprotein: biology and clinical relevance. Am.J. Kidney Dis. 42, 658-676 (2003)
4. Kemter, E. et al. No amelioration of uromodulin maturation and trafficking defect by sodium 4-phenylbutyrate in vivo: studies in mouse models of uromodulin-associated kidney disease. J Biol Chem 289, 10715-10726, doi: 10.1074/jbc.M113.537035 (2014)
5. Eckardt, K. U. et al. Autosomal dominant tubulointerstitial kidney disease: diagnosis, classification, and management-A KDIGO consensus report. Kidney international, doi: 10.1038/ki.2015.28 (2015)
6. Kemter, E. et al. Type of uromodulin mutation and allelic status influence onset and severity of uromodulin-associated kidney disease in mice. Hum Mol Genet 22, 4148-4163, doi: 10.1093/hmg/ddt263 (2013)
7. Seo, A. Y. et al. New insights into the role of mitochondria in aging: mitochondrial dynamics and more. Journal of cell science 123, 2533-2542, doi: 10.1242/jcs.070490 (2010)
8. Kluge, M. A., Fetterman, J. L. & Vita, J. A. Mitochondria and endothelial function. Circulation research 112, 1171-1188, doi: 10.1161/CIRCRESAHA.111.300233 (2013)
9. Smith, J. J. & Aitchison, J. D. Peroxisomes take shape. Nat Rev Mol Cell Biol 14, 803-817, doi: 10.1038/nrm3700 (2013)
10. Mishra, P. & Chan, D. C. Metabolic regulation of mitochondrial dynamics. The Journal of cell biology 212, 379-387, doi: 10.1083/jcb.201511036 (2016)
11. Lin, J., Handschin, C. & Spiegelman, B. M. Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab 1, 361-370, doi: 10.1016/j.cmet.2005.05.004 (2005)
12. Zhang, Y. & Hayes, J. D. The membrane-topogenic vectorial behaviour of Nrf1 controls its post-translational modification and transactivation activity. Sci Rep 3, 2006, doi: 10.1038/srep02006 (2013)
13. Hardie, D. G. AMPK: positive and negative regulation, and its role in whole-body energy homeostasis. Curr Opin Cell Biol 33, 1-7, doi: 10.1016/j.ceb.2014.09.004 (2015)
14. Alexander, A. & Walker, C. L. The role of LKB1 and AMPK in cellular responses to stress and damage. FEBS letters 585, 952-957, doi: 10.1016/j.febslet.2011.03.010 (2011)
15. Kemter, E. et al. Novel missense mutation of uromodulin in mice causes renal dysfunction with alterations in urea handling, energy, and bone metabolism. Am J Physiol Renal Physiol 297, F1391-1398, doi: 10.1152/ajprenal.00261.2009 (2009)
16. Wang, L., Zheng, Y., Xu, H., Yan, X. & Chang, X. Investigate pathogenic mechanism of TXNDC5 in rheumatoid arthritis. PLoS One 8, e53301, doi: 10.1371/journal.pone.0053301 (2013)
17. Gess, B. et al. The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. Eur J Biochem 270, 2228-2235 (2003)
18. Bando, Y. et al. ORP150/HSP12A protects renal tubular epithelium from ischemia-induced cell death. Faseb J 18, 1401-1403, doi: 10.1096/fj.03-1161fje (2004)
19. Sullivan, D. C. et al. EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor. J Biol Chem 278, 47079-47088, doi: 10.1074/jbc.M308124200 (2003)
20. Arrington, D. D. & Schnellmann, R. G. Targeting of the molecular chaperone oxygen-regulated protein 150 (ORP150) to mitochondria and its induction by cellular stress. Am J Physiol Cell Physiol 294, C641-650, doi: 10.1152/ajpcell.00400.2007 (2008)
21. Wu, Y. B. et al. CHOP/ORP150 ratio in endoplasmic reticulum stress: A new mechanism for diabetic peripheral neuropathy. Cell Physiol Biochem 32, 367-379, doi: 10.1159/000354444 (2013)
22. Ventura-Clapier, R., Garnier, A. & Veksler, V. Transcriptional control of mitochondrial biogenesis: the central role of PGC-1alpha. Cardiovascular research 79, 208-217, doi: 10.1093/cvr/cvn098 (2008)
23. Dimitrov, L., Lam, S. K. & Schekman, R. The role of the endoplasmic reticulum in peroxisome biogenesis. Cold Spring Harb Perspect Biol 5, a013243, doi: 10.1101/cshperspect.a013243 (2013)
24. Quiros, P. M., Langer, T. & Lopez-Otin, C. New roles for mitochondrial proteases in health, ageing and disease. Nat Rev Mol Cell Biol 16, 345-359, doi: 10.1038/nrm3984 (2015)
25. Venkatesh, S., Lee, J., Singh, K., Lee, I. & Suzuki, C. K. Multitasking in the mitochondrion by the ATP-dependent Lon protease. Biochimica et biophysica acta 1823, 56-66, doi: 10.1016/j.bbamcr.2011.11.003 (2012)
26. Raturi, A. & Simmen, T. Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM). Biochimica et biophysica acta 1833, 213-224, doi: 10.1016/j.bbamcr.2012.04.013 (2013)
27. Gilady, S. Y. et al. Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). Cell Stress Chaperones 15, 619-629, doi: 10.1007/s12192-010-0174-1 (2010)
28. Liberti, M. V. & Locasale, J. W. The Warburg Effect: How Does it Benefit Cancer Cells Trends Biochem Sci 41, 211-218, doi: 10.1016/j.tibs.2015.12.001 (2016)
29. Pinti, M. et al. Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer. Cell Mol Life Sci 72, 4807-4824, doi: 10.1007/s00018-015-2039-3 (2015)
30. Che, R., Yuan, Y., Huang, S. & Zhang, A. Mitochondrial dysfunction in the pathophysiology of renal diseases. Am J Physiol Renal Physiol 306, F367-378, doi: 10.1152/ajprenal.00571.2013 (2014)
31. Nunnari, J. & Suomalainen, A. Mitochondria: in sickness and in health. Cell 148, 1145-1159, doi: 10.1016/j.cell.2012.02.035 (2012)
32. Rampoldi, L. et al. Allelism of MCKD, FJHN and GCKD caused by impairment of uromodulin export dynamics. Hum. Mol. Genet. 12, 3369-3384 (2003)
33. Nasr, S. H., Lucia, J. P., Galgano, S. J., Markowitz, G. S. & D'Agati, V. D. Uromodulin storage disease. Kidney Int. 73, 971-976 (2008)
34. Huang da, W., Sherman, B. T. & Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4, 44-57, doi: 10.1038/nprot.2008.211 (2009)