Higd1a improves respiratory function in the models of mitochondrial disorder.
Adenosine Triphosphate
/ metabolism
Animals
Animals, Genetically Modified
Biological Transport
/ physiology
Cell Line
Cytochromes c
/ metabolism
Electron Transport
/ physiology
Electron Transport Complex IV
/ metabolism
HEK293 Cells
Humans
Hypoxia
/ metabolism
Intracellular Signaling Peptides and Proteins
/ metabolism
Kinetics
Mitochondria
/ metabolism
Mitochondrial Diseases
/ metabolism
Mitochondrial Proteins
/ metabolism
Oxidation-Reduction
Respiration
Zebrafish
/ metabolism
cytochrome c oxidase
hypoxia
mitochondria
respiratory chain
Journal
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
ISSN: 1530-6860
Titre abrégé: FASEB J
Pays: United States
ID NLM: 8804484
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
27
02
2018
revised:
26
05
2018
accepted:
12
06
2018
entrez:
10
1
2020
pubmed:
10
1
2020
medline:
7
7
2020
Statut:
ppublish
Résumé
The respiratory chain (RC) transports electrons to form a proton motive force that is required for ATP synthesis in the mitochondria. RC disorders cause mitochondrial diseases that have few effective treatments; therefore, novel therapeutic strategies are critically needed. We previously identified Higd1a as a positive regulator of cytochrome c oxidase (CcO) in the RC. Here, we test that Higd1a has a beneficial effect by increasing CcO activity in the models of mitochondrial dysfunction. We first demonstrated the tissue-protective effects of Higd1a via in situ measurement of mitochondrial ATP concentrations ([ATP]
Identifiants
pubmed: 31914602
doi: 10.1096/fj.201800389R
doi:
Substances chimiques
HIGD1A protein, human
0
Intracellular Signaling Peptides and Proteins
0
Mitochondrial Proteins
0
Adenosine Triphosphate
8L70Q75FXE
Cytochromes c
9007-43-6
Electron Transport Complex IV
EC 1.9.3.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1859-1871Informations de copyright
© 2019 Federation of American Societies for Experimental Biology.
Références
Alston CL, Rocha MC, Lax NZ, Turnbull DM, Taylor RW. The genetics and pathology of mitochondrial disease. J Pathol. 2016;241:236‐250.
Gorman GS, Schaefer AM, Ng Y, et al. Prevalence of nuclear and mitochondrial DNA mutations related to adult mitochondrial disease. Ann Neurol. 2015;77:753‐759.
Pfeffer G, Majamaa K, Turnbull DM, Thorburn D, Chinnery PF. Treatment for mitochondrial disorders. Cochrane Database Syst Rev. 2012;45:1193‐1244.
Torraco A, Peralta S, Iommarini L, Diaz F. Mitochondrial diseases part I: mouse models of OXPHOS deficiencies caused by defects in respiratory complex subunits or assembly factors. Mitochondrion. 2015;21:76‐91.
Kruse SE, Watt WC, Marcinek DJ, Kapur RP, Schenkman KA, Palmiter RD. Mice with mitochondrial complex I deficiency develop a fatal encephalomyopathy. Cell Metab. 2008;7:312‐320.
Lake NJ, Bird MJ, Isohanni P, Paetau A. Leigh syndrome: neuropathology and pathogenesis. J Neuropathol Exp Neurol. 2015;74:482‐492.
Jain IH, Zazzeron L, Goli R, et al. Hypoxia as a therapy for mitochondrial disease. Science. 2016;352:1‐14.
Ferrari M, Jain IH, Goldberger O, et al. Hypoxia treatment reverses neurodegenerative disease in a mouse model of Leigh syndrome. Proc Natl Acad Sci U S A. 2017;241:201621511‐201621610.
Johnson SC, Yanos ME, Kayser EB, et al. mTOR inhibition alleviates mitochondrial disease in a mouse model of leigh syndrome. Science. 2013;342:1524‐1528.
Goto Y, Nonaka I, Horai S. A mutation in the tRNA(Leu)(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature. 1990;348:651‐653.
Denko N, Schindler C, Koong A, Laderoute K, Green C, Giaccia A. Epigenetic regulation of gene expression in cervical cancer cells by the tumor microenvironment. Clin Cancer Res. 2000;6:480‐487.
Wang J, Cao Y, Chen Y, Chen Y, Gardner P, Steiner DF. Pancreatic beta cells lack a low glucose and O2‐inducible mitochondrial protein that augments cell survival. Proc Natl Acad Sci U S A. 2006;103:10636‐10641.
An H‐J, Cho G, Lee J‐O, Paik S‐G, Kim YS, Lee H. Higd‐1a interacts with Opa1 and is required for the morphological and functional integrity of mitochondria. Proc Natl Acad Sci U S A. 2013;110:13014‐13019.
Vukotic M, Oeljeklaus S, Wiese S, et al. Rcf1 mediates cytochrome oxidase assembly and respirasome formation, revealing heterogeneity of the enzyme complex. Cell Metab. 2012;15:336‐347.
Chen Y‐C, Taylor EB, Dephoure N, et al. Identification of a protein mediating respiratory supercomplex stability. Cell Metab. 2012;15:348‐360.
Hayashi T, Asano Y, Shintani Y, et al. Higd1a is a positive regulator of cytochrome c oxidase. Proc Natl Acad Sci U S A. 2015;112:1553‐1558.
Imamura H, Nhat KPH, Togawa H, et al. Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer‐based genetically encoded indicators. Proc Natl Acad Sci U S A. 2009;106:15651‐15656.
Kioka H, Kato H, Fujikawa M, et al. Evaluation of intramitochondrial ATP levels identifies G0/G1 switch gene 2 as a positive regulator of oxidative phosphorylation. Proc Natl Acad Sci U S A. 2014;111:273‐278.
Asakawa K, Kawakami K. The Tol2‐mediated Gal4‐UAS method for gene and enhancer trapping in zebrafish. Methods. 2009;49:275‐281.
Fujikawa M, Yoshida M. A sensitive, simple assay of mitochondrial ATP synthesis of cultured mammalian cells suitable for high‐throughput analysis. Biochem Biophys Res Commun. 2010;401:538‐543.
Kioka H, Kato H, Fujita T, et al. In vivo real‐time ATP imaging in zebrafish hearts reveals G0s2 induces ischemic tolerance. FASEB J. 2020;34, in press.
White RM, Sessa A, Burke C, et al. Transparent adult zebrafish as a tool for in vivo transplantation analysis. Cell Stem Cell. 2008;2:183‐189.
Nakano S, Suzuki T, Kawarada L, Iwata H, Asano K, Suzuki T. NSUN3 methylase initiates 5‐formylcytidine biogenesis in human mitochondrial tRNAMet. Nat Chem Biol. 2016;12:546‐551.
Van Haute L, Dietmann S, Kremer L, et al. Deficient methylation and formylation of mt‐tRNAMet wobble cytosine in a patient carrying mutations in NSUN3. Nat Commun. 2016;7:1‐10.
Sasarman F, Antonicka H, Shoubridge EA. The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2. Hum Mol Genet. 2008;17:3697‐3707.
Ma H, Folmes CDL, Wu J, et al. Metabolic rescue in pluripotent cells from patients with mtDNA disease. Nature. 2015;1‐18.
Tsukihara T, Aoyama H, Yamashita E, et al. The whole structure of the 13‐subunit oxidized cytochrome c oxidase at 2.8 A. Science. 1996;272:1136‐1144.
Nakada K, Inoue K, Ono T, et al. Inter‐mitochondrial complementation: Mitochondria‐specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat Med. 2001;7:934‐940.
Horan MP, Pichaud N, Ballard JWO. Review: quantifying mitochondrial dysfunction in complex diseases of aging. J Gerontol. 2012;67:1022‐1035.
Saxena R, de Bakker PIW, Singer K, et al. Comprehensive association testing of common mitochondrial DNA variation in metabolic disease. Am J Hum Genet. 2006;79:54‐61.
Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature. 2006;443:787‐795.