Submitted Successfully!
To reward your contribution, here is a gift for you: A free trial for our video production service.
Thank you for your contribution! You can also upload a video entry or images related to this topic.
Version Summary Created by Modification Content Size Created at Operation
1 -- 2157 2022-07-14 15:44:14 |
2 format correct Meta information modification 2157 2022-07-15 07:47:41 |

Video Upload Options

Do you have a full video?

Confirm

Are you sure to Delete?
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
Chin, M.T.;  Conway, S.J. Tafazzin in Mitochondrial Function, Development and Disease. Encyclopedia. Available online: https://encyclopedia.pub/entry/25159 (accessed on 22 June 2024).
Chin MT,  Conway SJ. Tafazzin in Mitochondrial Function, Development and Disease. Encyclopedia. Available at: https://encyclopedia.pub/entry/25159. Accessed June 22, 2024.
Chin, Michael T., Simon J. Conway. "Tafazzin in Mitochondrial Function, Development and Disease" Encyclopedia, https://encyclopedia.pub/entry/25159 (accessed June 22, 2024).
Chin, M.T., & Conway, S.J. (2022, July 14). Tafazzin in Mitochondrial Function, Development and Disease. In Encyclopedia. https://encyclopedia.pub/entry/25159
Chin, Michael T. and Simon J. Conway. "Tafazzin in Mitochondrial Function, Development and Disease." Encyclopedia. Web. 14 July, 2022.
Tafazzin in Mitochondrial Function, Development and Disease
Edit

Tafazzin, an enzyme associated with the rare inherited x-linked disorder Barth Syndrome, is a nuclear encoded mitochondrial transacylase that is highly conserved across multiple species and plays an important role in mitochondrial function. 

Tafazzin mitochondria Barth syndrome rare X-linked genetic disease

1. Introduction

Mitochondria are ubiquitous essential cellular organelles that control mitochondrial respiration and adenosine triphosphate (ATP) generation through the metabolism of key substrates, thereby regulating cellular energy balance. Mitochondria are also unique among organelles in that they contain their own genome and translational apparatus that allows synthesis of a small set of essential proteins specific to the mitochondria. The mitochondrial proteome, however, is complex and includes many proteins that are encoded in the nuclear genome, synthesized in the cytoplasm and transported across the mitochondrial outer membrane, where they are sorted and transported to either the outer membrane, intermembrane space, inner membrane or mitochondrial matrix. Mitochondrial dysfunction is a common feature of many medical disorders, while primary mitochondrial disorders invariably affect multiple organ systems simultaneously. The role of mitochondria in development is poorly understood.

2. Tafazzin Is a Regulator of Mitochondrial Structure and Function

Ultrastructural abnormalities in mitochondria were noted in the original case report describing BTHS [1], and have been associated with defective mitochondrial Complex III function [2], but the nature of BTHS-mediated mitochondrial dysfunction has been complex and variable. In yeast, early reports indicated a defect in energy coupling and membrane stability [3], while studies in patient-derived lymphoblasts indicated abnormal proliferation, altered membrane potential and normal ATP formation, suggesting partial uncoupling and compensatory expansion of the mitochondrial compartment [4]. Changes in ultrastructure are also variable dependent upon model system and organ analyzed, and may be more prominent in differentiated rather than embryonic tissues. The effect has been hypothesized to be greater in mitochondria with higher cristae stacking density [5] and as heart mitochondria have twice the diameter and higher percentages of lamellated cristae (cristae increase surface area and allow for inner membrane cardiolipin assembly) than other organs, this may help explain why BTHS patients exhibit predominantly cardiovascular defects [6] Abnormal cardiolipin remodeling due to Tafazzin deficiency leads to destabilization of mitochondrial inner membrane complexes in yeast [7], disrupts respiratory super complex formation in patient lymphoblasts [8] and also interferes with super complex formation in human iPS cells [9]. Interestingly, despite alterations in cardiolipin profiles and disruption in mitochondrial respiratory super complexes, metabolic flux through the TCA cycle was not disrupted in patient skin fibroblasts [10]. In Drosophila flight muscles, the density of the F1F0 ATP synthase dimers in the inner mitochondrial membrane was reduced at high curvature areas and dimer rows were less extended and more scattered [11]. In mice containing a doxycycline inducible shRNA that knocks down Tafazzin expression, mitochondria developed a wide spectrum of mitochondrial abnormalities [12][13][14]. Both the morphological defects (i.e., mixture of swollen, honeycomb and widened/collapsed/absent cristae) and numbers of mitochondria are variable, as there are reports of increased, decreased and unchanged mitochondrial numbers, depending upon which stage, which organs and doxycycline concentration used. An extensive bioenergetic and lipidomic characterization of these mice revealed differential substrate utilization, and reduction in Complex III and V activities [15]. An independent assessment of mitochondrial function in the same line of mice and in human iPS cell-derived cardiomyocytes (iPSC-CMs) from BTHS patients indicated a tissue-specific reduction in Complex II succinate dehydrogenase activity [16]. A separate BTHS iPSC-CM study implicated a reduction in F1F0 ATP synthase specific activity and overall ATP reduction in cells cultured in galactose, to limit ATP generation from glycolysis [17]. Interestingly, basal oxygen consumption rate is increased in BTHS iPSC-CMs, likely due to compensatory mechanisms, but total respiratory capacity is decreased [16][17]Tafazzin-deficient mitochondria have been noted to generate increased ROS in yeast [18], in Tafazzin knockdown mice [16] and in human iPSC-CMs [17].

3. The Role of Tafazzin in Cellular Differentiation and Development

In vitro studies on cultured cells have suggested a role for Tafazzin in regulation of differentiation. BTHS iPSC-derived cardiomyocytes show irregular sarcomere organization but no difference in differentiation efficiency when cultured for 60 days [16] or when cultured on an un-patterned substrate [17]. This defect in sarcomere organization was only seen with a Tafazzin frameshift variant (c.517delG) but not a missense variant (c.328T > C), however, engineered tissue constructs generated from iPSC-CMs containing each variant demonstrated contractile dysfunction [17]. Targeted disruption of the endogenous Tafazzin locus in a C2C12 mouse myoblast cell line led to altered differentiation into myotubes [19].
The effect of Tafazzin loss of function on in vivo organismal development has been studied in a variety of model organisms. In zebrafish embryos, at 10 h post fertilization (hpf), Tafazzin is expressed ubiquitously with strongest expression in the head area, at 24 hpf is expressed highly in the head, eye and tail and by 30 hpf, becomes more restricted to the head, heart, eyes and region next to the yolk corresponding to endodermal tissue. At 51 hpf, Tafazzin mRNA becomes highly restricted to the zebrafish heart, although this intriguing tissue specificity has yet to be confirmed in mammals or in later mature hearts. Morpholino antisense oligonucleotide-directed knockdown of Tafazzin mRNA led to severe developmental abnormalities in a dose-dependent fashion. The most severely affected structures were in the heart and tail, with some eye abnormalities observed. Morphant embryos at 51 hpf developed marked edema with large pericardial effusions associated with dysmorphic, slowly beating hearts. The heart tube failed to loop, showing a profound effect on heart development. Co-injection of zebrafish Tafazzin mRNA containing a variant analogous to the human mutation G197R rescued bradycardia and tail abnormalities but continue to demonstrate heart failure [20].
In Drosophila, generation of Tafazzin null mutants by imprecise P-element excision upstream of the start codon in exon 1 was associated with abnormal cardiolipin remodeling and abnormal mitochondrial morphology as described above. Lifespan was unchanged, and heart rate was unchanged in pupae and locomotor activity was normal in larvae. Quantitative measurement of motor weakness in adult flies demonstrated reduced ability to climb against gravity [21]. The relatively mild effect of Tafazzin deletion on organism development in Drosophila is likely a reflection of the significant differences between the circulatory systems of insects and vertebrates.
In mice, an understanding of the role of Tafazzin, cardiolipin and mitochondria in organism development are each incompletely understood. For instance, it is unknown when Tafazzin mRNA or protein is initially present within mouse embryos, if there is differential expression levels and when mature cardiolipin is first detectable and within which organs. Similarly, although it is known that mouse embryonic heartbeat starts at five somites (around embryonic day E8) and that blood flow is initiated at seven somites (around embryonic day E8.25), it is unknown when and where the first mitochondria are developed [22][23]. Moreover, as the embryonic heart is thought to initially rely solely on anaerobic glycolysis prior to placental development establishing circulation and rising oxygen levels, it is thought that mitochondria (and hence Tafazzin function) are presumed to be required as the in utero heart transitions to using subsequent aerobic respiration and an increasing reliance upon mitochondrially generated ATP [24][25][26][27]. Until recently, generation of fertile chimeras containing knockout alleles have been unsuccessful, most likely due to profound effects on spermatogenesis [28]. Knockdown induced via doxycyline from the start of gestation resulted in prenatal loss from E12.5–13.5, associated with myocardial thinning, hypertrabeculation, noncompaction and defective ventricular septation. Diastolic dysfunction was also noted. The effect on cardiovascular morphogenesis was recapitulated when knockdown was induced at E7.5 and at E10.5 but not at E13.5 or E14.5, suggesting an important developmental window for Tafazzin function. Tafazzin knockdown was associated with reduced compact zone proliferation but no apoptosis. Some embryos survived gestation, but none survived to adulthood [14]. Mitochondrial and cardiolipin abnormalities were as described above. This report differed from the other mouse studies by administering doxycycline at a higher dose in the drinking water compared to the other studies that used doxycycline containing chow [12][13], which may explain why the same strain of mice receiving doxycycline in chow showed predominantly an adult phenotype. Doxycycline, however, is known to have inhibitory effects on mitochondrial morphology/function itself [29] and continual administration of doxycycline to mice has been shown to adversely affect both cardiac and neutrophil function [30]. Thus, it is challenging to discern from this model whether the effects observed are as a direct result of the reduction of Tafazzin function, or a consequence of doxycycline exposure on the mitochondria, or even a combination of both. Another limitation of this model is that it relies on reduced expression of a normal Tafazzin gene rather than expression of pathogenic Tafazzin variants seen in patients. At present it is not clear whether loss of Tafazzin globally or specifically in the developing heart (or specific heart lineages) is responsible for the developmental and adult cardiac phenotypes observed. A recently developed Tafazzin conditional allele mouse line has enabled the study of both tissue specific and global deletion of Tafazzin [31]. Systemic deletion of Tafazzin in mice resulted in significant embryonic and perinatal lethality, while late embryonic deletion specifically in the heart resulted in adult onset dilated cardiomyopathy without any evidence of cardiac myocyte cell hypertrophy [32]. Systemic deletion also revealed that male Tafazzin knockout mice are sterile, as global loss inhibited germ cell meiosis as demonstrated by the reduced abundance of round spermatids and the near absence of elongated spermatids [31]. Although BTHS is thought to preferentially affect males, this result was unexpected and highlights the usefulness of transgenic mice approaches, as male infertility was not usually associated with BTHS. Further analysis of the embryonic phenotype or the tissue-specific contribution of Tafazzin to embryonic development using hematopoietic, testis, skeletal or early cardiac organ-restricted and lineage-specific deletion strategies has not yet been done, but is more than likely to be highly informative.

4. The Role of Tafazzin in Barth Syndrome, Non-Inherited Diseases and Potential Therapies in Development

The myriad of clinical features of BTHS have been well described [33][34]. The contribution of Tafazzin to mitochondrial dysfunction and subsequent muscle differentiation and dysfunction is easily understood given the enrichment of mitochondria in striated muscle tissue and the heightened energetic demands of muscle contraction. The contribution to left ventricular noncompaction can also be understood in this context as well, as the thickened left ventricle is the predominant chamber as it is responsible for pumping oxygenated blood throughout the entire body. The clinical impact of Tafazzin mutation on fetal loss and stillbirth has also been documented [35], although a clear effect on cardiovascular morphogenesis aside from noncompaction has not been described. Although the presence of cyclic neutropenia is also well documented in some BTHS patients, the mechanism causing this phenotype is poorly understood. Neutropenia makes it more difficult for the body to fight off foreign invaders such as bacteria and viruses, so affected individuals have an increased risk of recurrent infections. There is some evidence that apoptosis of myeloid precursors in the bone marrow results from Tafazzin-deficiency [36], but an explanation of why these cells are particularly susceptible has not been presented. Similarly, it is unclear why the high energy-requiring central nervous system is spared in BTHS, but not in many other mitochondrial diseases [37]
Reduction in mature and total cardiolipin has also been described in a spontaneously hypertensive rat model of heart failure, as well as adult human myocardial samples from patients with idiopathic dilated cardiomyopathy (IDCM) [38]. A subsequent follow up study found that the Tafazzin mRNA is reduced in both the hypertensive rat hearts and IDCM patient hearts but not control samples [39]. An analysis of pediatric cardiomyopathy samples demonstrated a similar reduction in mature and total cardiolpin in failing pediatric hearts but normal mitochondrial content and no change in Tafazzin expression, suggesting that other regulators of cardiolipin metabolism such as MLCL-AT may be important in the development of heart failure [40]. Increased Tafazzin expression has been associated with tumorigenicity of cervical cancer cells [41] and also with tumorigenesis and radiation response in rectal cancer [42]. Moreover, recent data has shown that Tafazzin can reduce stemness and increase differentiation of acute myeloid leukemia cells [43], although whether these are all primary or secondary effects upon cancer stem cells remains unknown.
Published therapeutic interventions for BTHS have focused on nutritional supplementation, reduction of oxidative stress and gene replacement therapy. The predominant mature cardiolipin in human hearts is tetralinoleoyl cardiolipin (L4CL) and BTHS patients show significant reduction in L4CL. Linoleic acid treatment of patient skin fibroblasts restores cardiolipin levels [44] and also partially improves BTHS iPSC-CM performance [17]. Scavenging of ROS in BTHS iPSC-CMs with mitoTEMPO also improved sarcomere organization and contractility [17], but scavenging of ROS in vivo through the use of mitochondrially targeted catalase in Tafazzin-deficient mice did not rescue cardiomyopathy [45]. Chemically modified RNA encoding Tafazzin was also able to rescue mitochondrial dysfunction in BTHS iPSC-CMs [17]. Adeno-associated viruse-9 (AAV9) mediated delivery of Tafazzin under the control of a myogenic-restricted desmin, a ubiquitously driven human cytomegalovirus immediate-early enhancer and promoter (CMV) or a native Tafazzin promoter each improved mitochondrial morphology, mitochondrial function, cardiac function and skeletal muscle performance in the Tafazzin knockdown mouse model [46]. In a separate study, AAV9-mediated delivery of Tafazzin under the control of the desmin promoter was able to normalize the proteomic profile of Tafazzin-deficient hearts [47]. AAV9-TAZ gene therapy was also able to restore mitochondrial morphology and function in BTHS patient fibroblasts [48]. AAV9-TAZ therapy administered to neonatal Taz KO mice was able to improve survival, reduce fibrosis, LV dilation and delay onset of cardiomyopathy when under the control of a CMV promoter but not a cardiomyocyte-restricted cTNT promoter, suggesting that the replacement of Tafazzin activity in skeletal muscle improves survival. It was also able to prevent the onset of cardiomyopathy and reverse established cardiomyopathy in Tafazzin myocardial conditional knockout mice when given at high doses [32].

References

  1. Barth, P.G.; Scholte, H.R.; Berden, J.A.; Van der Klei-Van Moorsel, J.M.; Luyt-Houwen, I.E.; Van’t Veer-Korthof, E.T.; Van der Harten, J.J.; Sobotka-Plojhar, M.A. An X-linked mitochondrial disease affecting cardiac muscle, skeletal muscle and neutrophil leucocytes. J. Neurol. Sci. 1983, 62, 327–355.
  2. Barth, P.G.; Van den Bogert, C.; Bolhuis, P.A.; Scholte, H.R.; van Gennip, A.H.; Schutgens, R.B.; Ketel, A.G. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome): Respiratory-chain abnormalities in cultured fibroblasts. J. Inherit. Metab. Dis. 1996, 19, 157–160.
  3. Ma, L.; Vaz, F.M.; Gu, Z.; Wanders, R.J.; Greenberg, M.L. The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant. Implications for Barth syndrome. J. Biol. Chem. 2004, 279, 44394–44399.
  4. Xu, Y.; Sutachan, J.J.; Plesken, H.; Kelley, R.I.; Schlame, M. Characterization of lymphoblast mitochondria from patients with Barth syndrome. Lab. Investig. 2005, 85, 823–830.
  5. Acehan, D.; Khuchua, Z.; Houtkooper, R.H.; Malhotra, A.; Kaufman, J.; Vaz, F.M.; Ren, M.; Rockman, H.A.; Stokes, D.L.; Schlame, M. Distinct effects of Tafazzin deletion in differentiated and undifferentiated mitochondria. Mitochondrion 2009, 9, 86–95.
  6. Shepard, T.H.; Muffley, L.A.; Smith, L.T. Ultrastructural study of mitochondria and their cristae in embryonic rats and primate (N. nemistrina). Anat. Rec. 1998, 252, 383–392.
  7. Brandner, K.; Mick, D.U.; Frazier, A.E.; Taylor, R.D.; 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, 5202–5214.
  8. McKenzie, M.; Lazarou, M.; Thorburn, D.R.; Ryan, M.T. Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients. J. Mol. Biol. 2006, 361, 462–469.
  9. Dudek, J.; Cheng, I.F.; Balleininger, M.; Vaz, F.M.; Streckfuss-Bomeke, K.; Hubscher, D.; Vukotic, M.; Wanders, R.J.; Rehling, P.; Guan, K. Cardiolipin deficiency affects respiratory chain function and organization in an induced pluripotent stem cell model of Barth syndrome. Stem Cell Res. 2013, 11, 806–819.
  10. Chatzispyrou, I.A.; Guerrero-Castillo, S.; Held, N.M.; Ruiter, J.P.N.; Denis, S.W.; Ljlst, L.; Wanders, R.J.; van Weeghel, M.; Ferdinandusse, S.; Vaz, F.M.; et al. Barth syndrome cells display widespread remodeling of mitochondrial complexes without affecting metabolic flux distribution. Biochim. Biophys. Acta Mol. Basis Dis. 2018, 1864, 3650–3658.
  11. Acehan, D.; Malhotra, A.; Xu, Y.; Ren, M.; Stokes, D.L.; Schlame, M. Cardiolipin affects the supramolecular organization of ATP synthase in mitochondria. Biophys. J. 2011, 100, 2184–2192.
  12. Acehan, D.; Vaz, F.; Houtkooper, R.H.; James, J.; Moore, V.; Tokunaga, C.; Kulik, W.; Wansapura, J.; Toth, M.J.; Strauss, A.; et al. Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome. J. Biol. Chem. 2011, 286, 899–908.
  13. Soustek, M.S.; Falk, D.J.; Mah, C.S.; Toth, M.J.; Schlame, M.; Lewin, A.S.; Byrne, B.J. Characterization of a transgenic short hairpin RNA-induced murine model of Tafazzin deficiency. Hum. Gene Ther. 2011, 22, 865–871.
  14. Phoon, C.K.L.; Acehan, D.; Schlame, M.; Stokes, D.L.; Edelman-Novemsky, I.; Yu, D.; Xu, Y.; Viswanathan, N.; Ren, M. Tafazzin Knockdown in Mice Leads to a Developmental Cardiomyopathy With Early Diastolic Dysfunction Preceding Myocardial Noncompaction. J. Am. Heart Assoc. 2012, 1, jah3-e000455.
  15. Kiebish, M.A.; Yang, K.; Liu, X.; Mancuso, D.J.; Guan, S.; Zhao, Z.; Sims, H.F.; Cerqua, R.; Cade, W.T.; Han, X.; et al. Dysfunctional cardiac mitochondrial bioenergetic, lipidomic, and signaling in a murine model of Barth syndrome. J. Lipid. Res. 2013, 54, 1312–1325.
  16. Dudek, J.; Cheng, I.F.; Chowdhury, A.; Wozny, K.; Balleininger, M.; Reinhold, R.; Grunau, S.; Callegari, S.; Toischer, K.; Wanders, R.J.; et al. Cardiac-specific succinate dehydrogenase deficiency in Barth syndrome. EMBO Mol. Med. 2016, 8, 139–154.
  17. Wang, G.; McCain, M.L.; Yang, L.; He, A.; Pasqualini, F.S.; Agarwal, A.; Yuan, H.; Jiang, D.; Zhang, D.; Zangi, L.; et al. Modeling the mitochondrial cardiomyopathy of Barth syndrome with induced pluripotent stem cell and heart-on-chip technologies. Nat. Med. 2014, 20, 616–623.
  18. Chen, S.; He, Q.; Greenberg, M.L. Loss of Tafazzin in yeast leads to increased oxidative stress during respiratory growth. Mol. Microbiol. 2008, 68, 1061–1072.
  19. Lou, W.; Reynolds, C.A.; Li, Y.; Liu, J.; Huttemann, M.; Schlame, M.; Stevenson, D.; Strathdee, D.; Greenberg, M.L. Loss of Tafazzin results in decreased myoblast differentiation in C2C12 cells: A myoblast model of Barth syndrome and cardiolipin deficiency. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 2018, 1863, 857–865.
  20. Khuchua, Z.; Yue, Z.; Batts, L.; Strauss, A.W. A zebrafish model of human Barth syndrome reveals the essential role of Tafazzin in cardiac development and function. Circ. Res. 2006, 99, 201–208.
  21. Xu, Y.; Condell, M.; Plesken, H.; Edelman-Novemsky, I.; Ma, J.; Ren, M.; Schlame, M. A Drosophila model of Barth syndrome. Proc. Natl. Acad. Sci. USA. 2006, 103, 11584–11588.
  22. Ji, R.P.; Phoon, C.K.; Aristizábal, O.; McGrath, K.E.; Palis, J.; Turnbull, D.H. Onset of cardiac function during early mouse embryogenesis coincides with entry of primitive erythroblasts into the embryo proper. Circ. Res. 2003, 92, 133–135.
  23. Koushik, S.V.; Wang, J.; Rogers, R.; Moskophidis, D.; Lambert, N.A.; Creazzo, T.L.; Conway, S.J. Targeted inactivation of the sodium-calcium exchanger (Ncx1) results in the lack of a heartbeat and abnormal myofibrillar organization. FASEB J. 2001, 15, 1209–1211.
  24. Hom, J.R.; Quintanilla, R.A.; Hoffman, D.L.; de Mesy Bentley, K.L.; Molkentin, J.D.; Sheu, S.S.; Porter, G.A., Jr. The permeability transition pore controls cardiac mitochondrial maturation and myocyte differentiation. Dev. Cell. 2011, 21, 469–478.
  25. Peoples, J.N.R.; Maxmillian, T.; Le, Q.; Nadtochiy, S.M.; Brookes, P.S.; Porter, G.A., Jr.; Davidson, V.L.; Ebert, S.N. Metabolomics reveals critical adrenergic regulatory checkpoints in glycolysis and pentose-phosphate pathways in embryonic heart. J. Biol. Chem. 2018, 293, 6925–6941.
  26. Porter, G.A., Jr.; Hom, J.; Hoffman, D.; Quintanilla, R.; de Mesy Bentley, K.; Sheu, S.S. Bioenergetics, mitochondria, and cardiac myocyte differentiation. Prog. Pediatr. Cardiol. 2011, 31, 75–81.
  27. Beutner, G.; Alanzalon, R.E.; Porter, G.A., Jr. Cyclophilin D regulates the dynamic assembly of mitochondrial ATP synthase into synthasomes. Sci. Rep. 2017, 7, 14488.
  28. Cadalbert, L.C.; Ghaffar, F.N.; Stevenson, D.; Bryson, S.; Vaz, F.M.; Gottlieb, E.; Strathdee, D. Mouse Tafazzin Is Required for Male Germ Cell Meiosis and Spermatogenesis. PLoS ONE 2015, 10, e0131066.
  29. Chatzispyrou, I.A.; Held, N.M.; Mouchiroud, L.; Auwerx, J.; Houtkooper, R.H. Tetracycline Antibiotics Impair Mitochondrial Function and Its Experimental Use Confounds Research. Cancer Res. 2015, 75, 4446–4449.
  30. Vinet, L.; Rouet-Benzineb, P.; Marniquet, X.; Pellegrin, N.; Mangin, L.; Louedec, L.; Samuel, J.L.; Mercadier, J.J. Chronic doxycycline exposure accelerates left ventricular hypertrophy and progression to heart failure in mice after thoracic aorta constriction. Am. J. Physiol. Heart Circ. Physiol. 2008, 295, H352–H360.
  31. Ren, M.; Xu, Y.; Erdjument-Bromage, H.; Donelian, A.; Phoon, C.K.L.; Terada, N.; Strathdee, D.; Neubert, T.A.; Schlame, M. Extramitochondrial cardiolipin suggests a novel function of mitochondria in spermatogenesis. J. Cell Biol. 2019, 218, 1491–1502.
  32. Wang, S.; Li, Y.; Xu, Y.; Ma, Q.; Lin, Z.; Schlame, M.; Bezzerides, V.J.; Strathdee, D.; Pu, W.T. AAV Gene Therapy Prevents and Reverses Heart Failure in a Murine Knockout Model of Barth Syndrome. Circ. Res. 2020, 126, 1024–1039.
  33. Clarke, S.L.; Bowron, A.; Gonzalez, I.L.; Groves, S.J.; Newbury-Ecob, R.; Clayton, N.; Martin, R.P.; Tsai-Goodman, B.; Garratt, V.; Ashworth, M.; et al. Barth syndrome. Orphanet J. Rare Dis. 2013, 8, 23.
  34. Kang, S.L.; Forsey, J.; Dudley, D.; Steward, C.G.; Tsai-Goodman, B. Clinical Characteristics and Outcomes of Cardiomyopathy in Barth Syndrome: The UK Experience. Pediatric Cardiol. 2016, 37, 167–176.
  35. Steward, C.G.; Newbury-Ecob, R.A.; Hastings, R.; Smithson, S.F.; Tsai-Goodman, B.; Quarrell, O.W.; Kulik, W.; Wanders, R.; Pennock, M.; Williams, M.; et al. Barth syndrome: An X-linked cause of fetal cardiomyopathy and stillbirth. Prenat. Diagn. 2010, 30, 970–976.
  36. Makaryan, V.; Kulik, W.; Vaz, F.M.; Allen, C.; Dror, Y.; Dale, D.C.; Aprikyan, A.A. The cellular and molecular mechanisms for neutropenia in Barth syndrome. Eur. J. Haematol. 2012, 88, 195–209.
  37. Lax, N.Z.; Gorman, G.S.; Turnbull, D.M. Review: Central nervous system involvement in mitochondrial disease. Neuropathol. Appl. Neurobiol. 2017, 43, 102–118.
  38. Sparagna, G.C.; Chicco, A.J.; Murphy, R.C.; Bristow, M.R.; Johnson, C.A.; Rees, M.L.; Maxey, M.L.; McCune, S.A.; Moore, R.L. Loss of cardiac tetralinoleoyl cardiolipin in human and experimental heart failure. J. Lipid. Res. 2007, 48, 1559–1570.
  39. Saini-Chohan, H.K.; Holmes, M.G.; Chicco, A.J.; Taylor, W.A.; Moore, R.L.; McCune, S.A.; Hickson-Bick, D.L.; Hatch, G.M.; Sparagna, G.C. Cardiolipin biosynthesis and remodeling enzymes are altered during development of heart failure. J. Lipid. Res. 2009, 50, 1600–1608.
  40. Chatfield, K.C.; Sparagna, G.C.; Sucharov, C.C.; Miyamoto, S.D.; Grudis, J.E.; Sobus, R.D.; Hijmans, J.; Stauffer, B.L. Dysregulation of cardiolipin biosynthesis in pediatric heart failure. J. Mol. Cell Cardiol. 2014, 74, 251–259.
  41. Chen, M.; Zhang, Y.; Zheng, P.S. Tafazzin (TAZ) promotes the tumorigenicity of cervical cancer cells and inhibits apoptosis. PLoS ONE 2017, 12, e0177171.
  42. Pathak, S.; Meng, W.J.; Zhang, H.; Gnosa, S.; Nandy, S.K.; Adell, G.; Holmlund, B.; Sun, X.F. Tafazzin protein expression is associated with tumorigenesis and radiation response in rectal cancer: A study of Swedish clinical trial on preoperative radiotherapy. PLoS ONE 2014, 9, e98317.
  43. Seneviratne, A.K.; Xu, M.; Aristizabal Henao, J.J.; Fajardo, V.A.; Hao, Z.; Voisin, V.; Xu, G.W.; Hurren, R.; Kim, S.; MacLean, N.; et al. The Mitochondrial Transacylase, Tafazzin, Regulates AML Stemness by Modulating Intracellular Levels of Phospholipids. Cell Stem Cell 2019, 24, 1007.
  44. Valianpour, F.; Wanders, R.J.; Overmars, H.; Vaz, F.M.; Barth, P.G.; van Gennip, A.H. Linoleic acid supplementation of Barth syndrome fibroblasts restores cardiolipin levels: Implications for treatment. J. Lipid Res. 2003, 44, 560–566.
  45. Johnson, J.M.; Ferrara, P.J.; Verkerke, A.R.P.; Coleman, C.B.; Wentzler, E.J.; Neufer, P.D.; Kew, K.A.; de Castro Bras, L.E.; Funai, K. Targeted overexpression of catalase to mitochondria does not prevent cardioskeletal myopathy in Barth syndrome. J. Mol. Cell. Cardiol. 2018, 121, 94–102.
  46. Suzuki-Hatano, S.; Saha, M.; Rizzo, S.A.; Witko, R.L.; Gosiker, B.J.; Ramanathan, M.; Soustek, M.S.; Jones, M.D.; Kang, P.B.; Byrne, B.J.; et al. AAV-Mediated TAZ Gene Replacement Restores Mitochondrial and Cardioskeletal Function in Barth Syndrome. Hum. Gene Ther. 2019, 30, 139–154.
  47. Suzuki-Hatano, S.; Saha, M.; Soustek, M.S.; Kang, P.B.; Byrne, B.J.; Cade, W.T.; Pacak, C.A. AAV9-TAZ Gene Replacement Ameliorates Cardiac TMT Proteomic Profiles in a Mouse Model of Barth Syndrome. Mol. Ther. Methods Clin. Dev. 2019, 13, 167–179.
  48. Suzuki-Hatano, S.; Sriramvenugopal, M.; Ramanathan, M.; Soustek, M.; Byrne, B.J.; Cade, W.T.; Kang, P.B.; Pacak, C.A. Increased mtDNA Abundance and Improved Function in Human Barth Syndrome Patient Fibroblasts Following AAV-TAZ Gene Delivery. Int. J. Mol. Sci. 2019, 20, 3416.
More
Information
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register : ,
View Times: 419
Revisions: 2 times (View History)
Update Date: 15 Jul 2022
1000/1000
Video Production Service