REFERENCES
2. Chatham JC, Young ME. Metabolic remodeling in the hypertrophic heart: fuel for thought. Circ Res. 2012;111:666-8.
3. Nickel A, Löffler J, Maack C. Myocardial energetics in heart failure. Basic Res Cardiol. 2013;108:358.
4. Brault JJ, Conway SJ. What can ATP content tell us about Barth syndrome muscle phenotypes? J Transl Genet Genom. 2025;9:1-10.
5. Barth PG, Scholte HR, Berden JA, et al. An X-linked mitochondrial disease affecting cardiac muscle, skeletal muscle and neutrophil leucocytes. J Neurol Sci. 1983;62:327-55.
6. Brand MD, Nicholls DG. Assessing mitochondrial dysfunction in cells. Biochem J. 2011;435:297-312.
7. Wu M, Neilson A, Swift AL, et al. Multiparameter metabolic analysis reveals a close link between attenuated mitochondrial bioenergetic function and enhanced glycolysis dependency in human tumor cells. Am J Physiol Cell Physiol. 2007;292:C125-36.
8. Yurista SR, Nguyen CT, Rosenzweig A, de Boer RA, Westenbrink BD. Ketone bodies for the failing heart: fuels that can fix the engine? Trends Endocrinol Metab. 2021;32:814-26.
9. Saric A, Andreau K, Armand AS, Møller IM, Petit PX. Barth syndrome: from mitochondrial dysfunctions associated with aberrant production of reactive oxygen species to pluripotent stem cell studies. Front Genet. 2015;6:359.
10. Neustein HB, Lurie PR, Dahms B, et al. An X-linked recessive cardiomyopathy with abnormal mitochondria. Pediatrics. 1979;64:24-9.
11. Barth PG, Valianpour F, Bowen VM, et al. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome): an update. Am J Med Genet A. 2004;126A:349-54.
12. Gonzalvez F, Pariselli F, Dupaigne P, et al. tBid interaction with cardiolipin primarily orchestrates mitochondrial dysfunctions and subsequently activates Bax and Bak. Cell Death Differ. 2005;12:614-26.
13. Bazán S, Mileykovskaya E, Mallampalli VK, Heacock P, Sparagna GC, Dowhan W. Cardiolipin-dependent reconstitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV. J Biol Chem. 2013;288:401-11.
14. Pfeiffer K, Gohil V, Stuart RA, et al. Cardiolipin stabilizes respiratory chain supercomplexes. J Biol Chem. 2003;278:52873-80.
15. Gonzalvez F, D’Aurelio M, Boutant M, et al. Barth syndrome: cellular compensation of mitochondrial dysfunction and apoptosis inhibition due to changes in cardiolipin remodeling linked to tafazzin (TAZ) gene mutation. Biochim Biophys Acta. 2013;1832:1194-206.
16. Gonzalvez F, Schug ZT, Houtkooper RH, et al. Cardiolipin provides an essential activating platform for caspase-8 on mitochondria. J Cell Biol. 2008;183:681-96.
17. Saini-Chohan HK, Holmes MG, Chicco AJ, et al. Cardiolipin biosynthesis and remodeling enzymes are altered during development of heart failure. J Lipid Res. 2009;50:1600-8.
18. Khuchua Z, Yue Z, Batts L, Strauss AW. A zebrafish model of human Barth syndrome reveals the essential role of tafazzin in cardiac development and function. Circ Res. 2006;99:201-8.
19. Li XX, Tsoi B, Li YF, Kurihara H, He RR. Cardiolipin and its different properties in mitophagy and apoptosis. J Histochem Cytochem. 2015;63:301-11.
21. Gebert N, Joshi AS, Kutik S, et al. Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome. Curr Biol. 2009;19:2133-9.
22. Jiang F, Ryan MT, Schlame M, et al. Absence of cardiolipin in the crd1 null mutant results in decreased mitochondrial membrane potential and reduced mitochondrial function. J Biol Chem. 2000;275:22387-94.
23. Zhang M, Mileykovskaya E, Dowhan W. Gluing the respiratory chain together: Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane. J Biol Chem. 2002;277:43553-6.
24. Ban T, Heymann JA, Song Z, Hinshaw JE, Chan DC. OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum Mol Genet. 2010;19:2113-22.
25. DeVay RM, Dominguez-Ramirez L, Lackner LL, Hoppins S, Stahlberg H, Nunnari J. Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion. J Cell Biol. 2009;186:793-803.
26. Joshi AS, Thompson MN, Fei N, Hüttemann M, Greenberg ML. Cardiolipin and mitochondrial phosphatidylethanolamine have overlapping functions in mitochondrial fusion in Saccharomyces cerevisiae. J Biol Chem. 2012;287:17589-97.
27. Patil VA, Greenberg ML. Cardiolipin-mediated cellular signaling. In: Capelluto DG, editor. Lipid-mediated protein signaling. Dordrecht: Springer Netherlands; 2013. pp. 195-213.
28. Ikon N, Su B, Hsu FF, Forte TM, Ryan RO. Exogenous cardiolipin localizes to mitochondria and prevents TAZ knockdown-induced apoptosis in myeloid progenitor cells. Biochem Biophys Res Commun. 2015;464:580-5.
29. Heit B, Yeung T, Grinstein S. Changes in mitochondrial surface charge mediate recruitment of signaling molecules during apoptosis. Am J Physiol Cell Physiol. 2011;300:C33-41.
30. Kim TH, Zhao Y, Ding WX, et al. Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C release. Mol Biol Cell. 2004;15:3061-72.
31. Manganelli V, Capozzi A, Recalchi S, et al. Altered Traffic of cardiolipin during apoptosis: exposure on the cell surface as a trigger for “antiphospholipid antibodies”. J Immunol Res. 2015;2015:847985.
32. Chu CT, Bayır H, Kagan VE. LC3 binds externalized cardiolipin on injured mitochondria to signal mitophagy in neurons: implications for Parkinson disease. Autophagy. 2014;10:376-8.
33. Gu Z, Valianpour F, Chen S, et al. Aberrant cardiolipin metabolism in the yeast taz1 mutant: a model for Barth syndrome. Mol Microbiol. 2004;51:149-58.
34. Schlame M, Rua D, Greenberg ML. The biosynthesis and functional role of cardiolipin. Prog Lipid Res. 2000;39:257-88.
35. Koshkin V, Greenberg ML. Oxidative phosphorylation in cardiolipin-lacking yeast mitochondria. Biochem J. 2000;347:687-91.
36. Kadenbach B, Mende P, Kolbe HV, Stipani I, Palmieri F. The mitochondrial phosphate carrier has an essential requirement for cardiolipin. FEBS Lett. 1982;139:109-12.
37. Robinson NC. Functional binding of cardiolipin to cytochrome c oxidase. J Bioenerg Biomembr. 1993;25:153-63.
38. Noël H, Pande SV. An essential requirement of cardiolipin for mitochondrial carnitine acylcarnitine translocase activity. Lipid requirement of carnitine acylcarnitine translocase. Eur J Biochem. 1986;155:99-102.
39. Vaz FM, Houtkooper RH, Valianpour F, Barth PG, Wanders RJ. Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism. J Biol Chem. 2003;278:43089-94.
40. Brandner K, Mick DU, Frazier AE, Taylor RD, Meisinger C, Rehling P. Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome. Mol Biol Cell. 2005;16:5202-14.
41. Xu Y, Kelley RI, Blanck TJ, Schlame M. Remodeling of cardiolipin by phospholipid transacylation. J Biol Chem. 2003;278:51380-5.
42. Acehan D, Xu Y, Stokes DL, Schlame M. Comparison of lymphoblast mitochondria from normal subjects and patients with Barth syndrome using electron microscopic tomography. Lab Invest. 2007;87:40-8.
43. Xu Y, Malhotra A, Ren M, Schlame M. The enzymatic function of tafazzin. J Biol Chem. 2006;281:39217-24.
44. McKenzie M, Lazarou M, Thorburn DR, Ryan MT. Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients. J Mol Biol. 2006;361:462-9.
45. Xu Y, Sutachan JJ, Plesken H, Kelley RI, Schlame M. Characterization of lymphoblast mitochondria from patients with Barth syndrome. Lab Invest. 2005;85:823-30.
46. Xu Y, Condell M, Plesken H, et al. A Drosophila model of Barth syndrome. Proc Natl Acad Sci U S A. 2006;103:11584-8.
47. Phoon CK, Acehan D, Schlame M, et al. Tafazzin knockdown in mice leads to a developmental cardiomyopathy with early diastolic dysfunction preceding myocardial noncompaction. J Am Heart Assoc. 2012:1.
48. Acehan D, Vaz F, Houtkooper RH, et al. Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome. J Biol Chem. 2011;286:899-908.
49. Zhu S, Chen Z, Zhu M, et al. Cardiolipin remodeling defects impair mitochondrial architecture and function in a murine model of Barth syndrome cardiomyopathy. Circ Heart Fail. 2021;14:e008289.
50. Wang G, McCain ML, Yang L, et al. Modeling the mitochondrial cardiomyopathy of Barth syndrome with induced pluripotent stem cell and heart-on-chip technologies. Nat Med. 2014;20:616-23.
51. He Q. Tafazzin knockdown causes hypertrophy of neonatal ventricular myocytes. Am J Physiol Heart Circ Physiol. 2010;299:H210-6.
52. Desousa BR, Kim KK, Jones AE, et al. Calculation of ATP production rates using the seahorse XF analyzer. EMBO Rep. 2023;24:e56380.
53. Doerrier C, Garcia-souza LF, Krumschnabel G, Wohlfarter Y, Mészáros AT, Gnaiger E. High-resolution FluoRespirometry and OXPHOS protocols for human cells, permeabilized fibers from small biopsies of muscle, and isolated mitochondria. In: Palmeira CM, Moreno AJ, editors. Mitochondrial bioenergetics. New York: Springer; 2018. pp. 31-70.
54. Gu X, Ma Y, Liu Y, Wan Q. Measurement of mitochondrial respiration in adherent cells by seahorse XF96 cell mito stress test. STAR Protoc. 2021;2:100245.
55. Mookerjee SA, Gerencser AA, Nicholls DG, Brand MD. Quantifying intracellular rates of glycolytic and oxidative ATP production and consumption using extracellular flux measurements. J Biol Chem. 2017;292:7189-207.
56. Pelletier M, Billingham LK, Ramaswamy M, Siegel RM. Extracellular flux analysis to monitor glycolytic rates and mitochondrial oxygen consumption. Methods Enzymol. 2014;542:125-49.
57. Divakaruni AS, Jastroch M. A practical guide for the analysis, standardization and interpretation of oxygen consumption measurements. Nat Metab. 2022;4:978-94.
58. Miller SG, Hafen PS, Brault JJ. Increased adenine nucleotide degradation in skeletal muscle atrophy. Int J Mol Sci. 2019;21:88.
59. de Kok MJC, Schaapherder AF, Wüst RCI, et al. Circumventing the crabtree effect in cell culture: a systematic review. Mitochondrion. 2021;59:83-95.
60. Handel ME, Brand MD, Mookerjee SA. The whys and hows of calculating total cellular ATP production rate. Trends Endocrinol Metab. 2019;30:412-6.
61. Tullson PC, Whitlock DM, Terjung RL. Adenine nucleotide degradation in slow-twitch red muscle. Am J Physiol. 1990;258:C258-65.
62. Law AS, Hafen PS, Brault JJ. Liquid chromatography method for simultaneous quantification of ATP and its degradation products compatible with both UV-Vis and mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2022;1206:123351.
63. Petit PX, Gendron M, Schrantz N, et al. Oxidation of pyridine nucleotides during Fas- and ceramide-induced apoptosis in Jurkat cells: correlation with changes in mitochondria, glutathione depletion, intracellular acidification and caspase 3 activation. Biochem J. 2001;353:357-67.
64. Hancock CR, Brault JJ, Wiseman RW, Terjung RL, Meyer RA. 31P-NMR observation of free ADP during fatiguing, repetitive contractions of murine skeletal muscle lacking AK1. Am J Physiol Cell Physiol. 2005;288:C1298-304.
65. Marvin JS, Kokotos AC, Kumar M, et al. iATPSnFR2: A high-dynamic-range fluorescent sensor for monitoring intracellular ATP. Proc Natl Acad Sci U S A. 2024;121:e2314604121.
66. Stanley PE, Williams SG. Use of the liquid scintillation spectrometer for determining adenosine triphosphate by the luciferase enzyme. Anal Biochem. 1969;29:381-92.
67. Yang NC, Ho WM, Chen YH, Hu ML. A convenient one-step extraction of cellular ATP using boiling water for the luciferin-luciferase assay of ATP. Anal Biochem. 2002;306:323-7.
68. Tullson PC, Terjung RL. Adenine nucleotide degradation in striated muscle. Int J Sports Med. 1990;11 Suppl 2:S47-55.
69. de Taffin de Tilques M, Lasserre JP, Godard F, et al. Decreasing cytosolic translation is beneficial to yeast and human Tafazzin-deficient cells. Microb Cell. 2018;5:220-32.
70. Wang X, Chen XJ. A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death. Nature. 2015;524:481-4.
