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     2026:7/4

International Journal of Medical and All Body Health Research

e-ISSN: 2582-8940 | Open Access

Synergistic anti-oxidant Actions of Mitochondrial Palatin-like PhosphoLipaseA2Domain-Containing Protein-8(PNPLA8/ iPLA2γ) with the Fatty Acids (FA)-Translocating-SLC-25 Gene Family Transporters with their Sequelae-A Review

Dr. Kulvinder Kochar Kaur, Dr. Gautam Allahbadia, Dr. Mandeep Singh

Centre for Human Reproduction, GTB Nagar, Jalandhar, Punjab, India; Centre for Human Reproduction, KALPAK Garden, Bandra West, Mumbai, India; Consultant Neurologist, Swami Satyanand Hospital, Baradri, Jalandhar, Punjab, India

Article Information

Volume / Issue1 / 4 (October-December 2020)
Pages01-15
AccessOpen Access

Publication Timeline

  • Received20 September 2020
  • Accepted07 October 2020

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Abstract

Palatin –like PhosphoLipaseA2Domain –Containing Protein-8(PNPLA8)alias Ca2+ independent phospholipase A2γ(iPLA2γ)is the one that is restricted to the mitochondrial matrix or peroxisomes where it might demonstrate its individual action of cleaving of the phospholipid side chain from sn1 awa sn2 position, leading to liberation of either saturated FAs or poly unsaturated FAs(PUFA)that include oxidized fatty acids. Furthermore iPLA2γ gets directly activated by H2O2 as well as thus get stimulated by redox signaling or oxidative stress. This redox stimulation allows the anti oxidant synergism with the mitochondrial uncoupling protein(UCPs)or other SLC25 mitochondrial family agents acting as carriers by the FA- modulated protonophoretic action also termed mild uncoupling which results in reduction of mitochondrial superoxide generation. This mode permits for the sustenance of the steady state redox status of the cell. Other than its anti oxidant part here the association of iPLA2γ to lipid peroxidation is reviewed here as iPLA2γ gets alternatively stimulated by cardiolipin hydroperoxides in addition to supposedly by structural changes of the lipid bilayer secondary to lipid peroxidation. Rest of iPLA2γ part are mitochondrial (or peroxisomal) membranes besides the production of particular lipid second messengers. Hence like at the time of FAs β oxidationin case of pancreatic β cells, H2O2 stimulated iPLA2γ provides the G- protein coupled receptor (GPR40)metabotropic receptor for multiplication of FA- stimulated insulin liberation. Moreover the cytoshielding part of iPLA2γ in the heart as well as brain,along with role in brown adipose tissue (BAT) metabolism is further detailed. The major work in this field has been by the groups of Jezek P from Chez and Gross RW, Mancuso DJ gourps. Thus this knowledge gives further insight in unraveling the alterations in lipid metabolism in diseases like obesity, non-alcoholic fatty liver disease (NAFLD), non-alcoholic steatohepapititis (NASH), where ectopic fat deposition and accumulation is behind the pathophysiology of these diseases, besides understanding the severity of generation of APS Syndrome resulting in life threatening conditions.

Keywords

antioxidant synergismiPLA2γmitochondrial uncoupling proteinmitochondrial Adeninw nucleotide translocase (ANT)SLC25 mitochondrial family agentslipid peroxidation

References

  1. Kulvinder Kochar Kaur,Allahbadia GN,Singh M. Therapeutic Applications of the Recent Understanding of Brown or Beige Adipocyte Physiology Adv Tech Biol Med. 2015; 3:2 http://dx.doi.org/10.4172/2379-1764.1000128 [Google Scholar][Crossref]
  2. Kulvinder Kochar Kaur, Allahbadia GN, Singh M. A Review of Nutrient Metabolism in Obesity with Special Emphasis on Fatty Acid Metabolism; BAOJ Food Sci&Tec. 2017; 1:1 [Google Scholar][Crossref]
  3. Kulvinder Kochar Kaur, Allahbadia GN, Singh M. Advances in BAT physiology for understanding and translating into Pharmacotherapies for obesity and comorbidities. MOJ Drug Des Develop Ther. 2018; 2(5):166-176. DOI: 10.15406/mojddt.2018.02.00057 [Google Scholar][Crossref]
  4. Kulvinder Kochar Kaur, Allahbadia GN, Singh M. An Update on Microrna’s and Metabolic Regulation with Future Therapeutic Potentials Regarding Diagnosis and Treatment of Obesity, Metabolic Syndrome and Other Related Disorders. J Health Med Informat 6:184. doi:10.4172/2157-7420.1000184. [Google Scholar][Crossref]
  5. Kulvinder Kochar Kaur, Allahbadia GN, Singh M. Utilization of β3 Adrenergic Receptors as Targets for Treating Diabesity-Mirabegron and Beyond-A Systematic Review. All rights reserved. International Journal of Innovations in Biological and Chemical Sciences. 2018; 11:1-13. [Google Scholar][Crossref]
  6. Kulvinder Kochar Kaur, Allahbadia GN, Singh M. Role of Mitochondrial Unfolding Protein Response in Reproduction and Aging with Utilization of Autologous Mitochondrial Injections in Mitochondrial Diseases along within Aging Oocytes. J Gynecol. 2020; 5(1):000187. DOI: 10.23880/oajg-16000187. [Google Scholar][Crossref]
  7. Kulvinder Kochar Kaur, Allahbadia GN, Singh M. The association of dietary fatty acids and gut Microbiota alterations in the development of neuropsychiatric diseases: A systematic review. Obes Res Open J. 2020; 7(1):19-45. doi: 10.17140/OROJ-7-143. [Google Scholar][Crossref]
  8. Kulvinder Kochar Kaur, Allahbadia GN, Singh M. Role of Adipocyte impairment in Heart Failure Induction in subjects that are obese along with prediabetes and overt Diabetes mellitus -A Systematic Review. International Journal of Cardiology and Cardiovascular Disorder. 2021; 2(1):1-21. [Google Scholar][Crossref]
  9. Jezek P, Hlavata L. Mitochondria in homeostasis of Reactive oxygen species in cells, tissues and organisms. Int J Biochem Cell Biol. 2005; 37:2478-503. [Google Scholar][Crossref]
  10. Jezek P, Holendova B, Garid KD, Jaburek M. Mitochondrial uncoupling proteins: Subtle regions of cellular redox signaling. Antioxidant Redox Signal. 2018; 29:557-714. [Google Scholar][Crossref]
  11. Jezek P, Holendova B, Plecita Hlavata L. Redox signaling from mitochondria: Signal propagation and its targets. Biomolecules. 2020; 10:93. [Google Scholar][Crossref]
  12. Jezek P, Holendova B, Jaburek M, Tauber J, Dlaskova International Journal of Medical and all body Health Research www.allmedicaljournal.com 12 A, Plecita Hlavata L. The pancreatic β cells: The perfect redox system. Antioxidants. 2021; 10:197 [Google Scholar][Crossref]
  13. Skulachev VP. Fatty acid circuit as a physiological mechanism of uncoupling of Oxidative phosphorylation. FEBS Lett. 1991; 294:158-62. [Google Scholar][Crossref]
  14. Bertholet AM, Chouchani ET, Kazak L, Angelin A, Fedorenko A, Long JZ, et al. H Transport is an integral function of the mitochondrial ADP/ATP carrier. Nature. 2019; 571:515-20. [Google Scholar][Crossref]
  15. Fedorenko A, Lishkov PV, Kirchov Y. Mechanism of Fatty acid dependent UCP1 uncoupling in brown fat mitochondria. Cell. 2012; 151:400-13. [Google Scholar][Crossref]
  16. Ramanadham S, Tomader A, Ashley JW, Bone RN, Hancock WD, Lei X. Calcium independent phospholipase A2 and their roles in biological processes and diseases. J Lipid Res. 2015; 56:1643-668. [Google Scholar][Crossref]
  17. Hara S,Yoda E,Sasaki Y,Nakatani Y,Kuwata H. Calcium independent phospholipase A2 γ (iPLA2γ )and its roles in cellular function and diseases. Biochim Biophys Acta Mol Cell Biol Lipids 2019;1864:861-68. [Google Scholar][Crossref]
  18. Jezek J, Jaburek M, Zelenka J, Jezek P. Mitochondrial phospholipase A2 activated by Reactive oxygen speciesin heart mitochondria induces mild uncoupling. Physiol Res. 2010; 59:737-47. [Google Scholar][Crossref]
  19. Jaburek M, Jezek J, Zelenka J, Jezek P. Antioxidant activity by a synergy of redox –sensitive Mitochondrial phospholipase A2 and uncoupling protein in lung and spleen. Int J Biochem Cell Biol. 2013; 45:816-25. [Google Scholar][Crossref]
  20. Jezek J, Dlaskova A, Zelenka J, Jaburek M, Jezek P. H2O2 activated Mitochondrial phospholipase A2 iPLA2γ Prevents lipotoxic Oxidative stress in synergy with UCP2,amplifies signaling via G- protein coupled receptor GPR40, and regulates insulin secretion in pancreatic β cells. Antioxidant Redox Signal. 2015; 23:958-72. [Google Scholar][Crossref]
  21. Jaburek M, Jezek J, Jezek P. Cytoprotective activity of Mitochondrial uncoupling protein in lung and spleen. FEBS Open Bio. 2018; 8:692-701. [Google Scholar][Crossref]
  22. Murakami M, Taketomi Y, Miki Y, Sato H, Hirabayashi T, Yamamoto K. Recent progress in phospholipase A2 research: from cells to animals in humans. Prog Lipid Res. 2011; 50:152-92. [Google Scholar][Crossref]
  23. Jaburek M, Pruchova P, Holendova B, Galkin A, Jezek P. Antioxidant Synergy of Mitochondrial phospholipase PNPLA8/ iPLA2γ with fatty acid-conducting SLC25 gene family transporters. Antioxidants. 2021; 10:678. [Google Scholar][Crossref]
  24. Van Tienhoven M, Atkins J, Li Y, Glynn P. Human neuropathy target esterase catalyzes hydrolysis of membrane lipids. J Biol Chem. 2002; 277:20942-948. [Google Scholar][Crossref]
  25. Jenkins CM, Marcuso DJ, Yan W, Sims HF, Gibson B, Gross RW. Identification, cloning, expression, and purification of novel human Calcium independent phospholipase A2 family members possessingtriacyl glycerol lipase and acyl glycerol Trans acyl lipase activities. J Biol Chem 2004; 279:48968-48975. [Google Scholar][Crossref]
  26. Mancuso DJ, Jenkins CM, Sims HF, Cohen JM, Yang J, Gross RW. Complex transcriptional and translational regulation of iPLA2γ resulting in multiple gene products containing dual competing sites for Mitochondrial or peroxisomal localization. Eur J Biochem. 2004; 271:4709-4724. [Google Scholar][Crossref]
  27. Song H, Bao S, Lei X, Jin C, Zhang S, Turk J, et al. Evidence for proteolytic processing and stimulated organelle redistribution. Biochim Biophys Acta Mol Cell Biol Lipids. 2010; 1801:547-58. [Google Scholar][Crossref]
  28. Zhao Z, Zhang X, Zhao C, Choi J, Shi J, Song KJ, et al. Protection of pancreatic β cells by group VIA phospholipase A2-Mediated repair of Mitochondrial membrane peroxidation. Endocrinology. 2010; 151:3038-3048. [Google Scholar][Crossref]
  29. Moon SH, Liu X, Cedars AM, Yang K, Kiebish MA, Joseph SM, et al. Heart failure induced activation of phospholipase A2 iPLA2γ generates hydroxyl-eicosatetraenoic acids opening the Mitochondrial permeability transition pore. J Biol Chem. 2018; 293:115-29. [Google Scholar][Crossref]
  30. Lio YC, Dennis EA. Interfascial activation lyso phospholipase and transacy lase activity of Group VI Ca 2+ independent phospholipase A2. Biochim Biophys Acta Mol Cell Biol Lipids. 1998; 1392:320-32. [Google Scholar][Crossref]
  31. Jenkins CM, Yan W, Mancuso DJ, Gross RW. Highly selective hydrolysis of fatty acyl CoAs by Calcium independent phospholipase A2β: enzyme auto acylation and acyl CoA-mediated reversal of calmodulin inhibition of phospholipase A2 activity. J Biol Chem. 2006; 281:15615-15624. [Google Scholar][Crossref]
  32. Ma Z, Ramanadham S, Kempe K, Chi XS, Ladenson J, Turk J. Pancreatic islets express a Ca 2+ independent phospholipase A2 enzyme that contains a repeated structural motif homologous to the integral membrane protein binding domain of ankyrin. J Biol Chem. 1997; 272:11118-11127. [Google Scholar][Crossref]
  33. Malley KR, Koroleva O, Miller I, Sanishvili R, Jenkins CM, Gross RW, Korolev S. The structure of iPLA2β reverts dimeric active sites and suggests mechanisms of regulation and localization. Nat Commun. 2018; 9:765. [Google Scholar][Crossref]
  34. Bucher D, Hsui YH, Mouchis VD, Dennis EA, McCammon JA. Insertion of Ca 2+ independent phospholipase A2 into a phospho lipid bilayer via coarse grained and atomistic molecular dynamics simulations. PLoS Comput Biol. 2013; 9:e1003156. [Google Scholar][Crossref]
  35. Yan W, Jenkins CM, HanX, Mancuso DJ, Sims HF, Yang K, Gross RW. The highly selective production of 2arachidonoyl lysophosphatidyl choline catalyzed by Calcium independent phospholipase A2γ: Identification of a novel enzymatic mediator of the generation of a key branch point intermediate in eicosanoid signaling. J Biol. Chem. 2005; 280:266669-6679. [Google Scholar][Crossref]
  36. Mancuso DJ, Han X, Jenkins CM, Lehman JJ, Sambandam N, Sims HF, et al. Dramatic accumulation of triglycerides and precipitation of cardiac haemodynamic dysfunction during brief caloric restriction in transgenic myocardium expressing human Calcium independent phospholipase Aγ. J Biol Chem. 2007; 282:9216-227. [Google Scholar][Crossref]
  37. Mancuso DJ, Jenkins CM, Gross RW. The genomic organization, complete m RNA sequence, cloning, and expression of a novel human intracellular membrane -associated Calcium independent phospholipase A(2). J Biol Chem. 2000; 275:9937-945. [Google Scholar][Crossref]
  38. Tanaka H, Takeya R, Sumimoto H. A novel intracellular membrane-bound Calcium independent phospholipase A2. Biochem Biophys Res Commun. 2000; 272:320-26. [Google Scholar][Crossref]
  39. Liu X, Sims HF, Jenkins CM, Guan S, Dilthey BG, Gross RW. 12-LOX catalyzes the oxidation of 2-2arachidonoyl lysolipids in platelets generating eicosanoids- lysolipids that are attenuated by iPLA2γ knockout.J Biol Chem 2020; 295:5307-320. International Journal of Medical and all body Health Research www.allmedicaljournal.com 13 [Google Scholar][Crossref]
  40. Jaburek M, Holendova B,Pruchova P, Jezek P.Cardiolipin hydroperoxides are both substrates and redox activators of iPLA2γ.Free Radic Biol Med 2018;120:S65. [Google Scholar][Crossref]
  41. Kuhlbrandt W. Structure and function of mitochondrial membrane protein complexes. BMC Biol. 2015; 13:89. [Google Scholar][Crossref]
  42. Dlaskova A, Spacek T, Engstova H, Spackova J, Schrofel A, Holendova B, et al. Mitochondrial cristae narrowing upon higher 2-oxoglutarate load. Biochim Biophys Acta Bioenerg. 2019; 1860:659-78. [Google Scholar][Crossref]
  43. Tanaka H, Minakami R, Kanaya A, Sumimoto H. Catalytic residues of VIB Calcium independent phospholipase A2. Biochim Biophys Res Commun. 2004; 320:1284-290. [Google Scholar][Crossref]
  44. Liu GYY, Moon SH, Jenkins CM, Li M, Sims HF, Guan S, et al. The phospholipase iPLA2is a major mediator releasing Oxidized aliphatic chains from cardiolipin, integrating mitochondrial bioenergetics and signaling. J Biol Chem. 2017; 292:10672-10684. [Google Scholar][Crossref]
  45. Yoda E, Hachisu K, Taketomi Y, Yoshida K, Nakamura M, Ikeda K, et al. Mitochondrial dysfunction and reduced prostaglandin synthesis in skeletal muscle of Group VIB Ca 2+ independent phospholipase A2gamma deficient mice. J Lipid Res. 2010; 51:10672-10684. [Google Scholar][Crossref]
  46. Moon SH, Dilthey BG, Liu X, Guan S, Sims HF, Gross RW. High fat diet activates liver iPLA2γ generating eicosanoids that mediate metabolic stress. J Lipid Res. 2021; 62:100052. [Google Scholar][Crossref]
  47. Jaburek M, Garlid KD. Reconstitution of recombinant uncoupling proteins UCP1,2 and -3have similar affinities for ATP and were unaffected by coenzyme Q10. J Biol Chem. 2003; 278:25825-5831. [Google Scholar][Crossref]
  48. Jaburek M, Miyamoto S, DiMascio P, Garlid KD, Jezek P. Hydroperoxide fatty acids cycling mediated by mitochondria uncoupling proteins2 and 3.J Biol Chem. 2004; 279:53097-53102. [Google Scholar][Crossref]
  49. Bertholet AM, Kazak L, Chouchani ET, Bogaczzynska MG, ParanipeI, Wainwright GL, et al. Mitochondrial patch clamp of beige adipocytesreveals UCP1positive and UCP1 negative cells both exhibiting futile creating cycling. Cell Metab. 2017;25:811-22e4. [Google Scholar][Crossref]
  50. Wojtczak L, Wieckowski MR. The Schonfeld P. Protonophoric activity of fatty acid- analogues and derivatives in the inner mitochondrial membrane: a further argument for fatty acid cycling model.Arch Biochim Biophys. 1998; 357:76-84. [Google Scholar][Crossref]
  51. Capaldi RA. Arrangement of proteins in the mitochondrial inner membrane. BBA Rev Biomembr. 1982; 694:291-306. [Google Scholar][Crossref]
  52. Elimam H, Papillon J, Guillemette J, Navarro-Betancourt JR, Cybulsky AV. Genetic ablation of Calcium independent phospholipase A2γ exacerbates glomerular injury in adriamycin nephrosis in mice. Sci Rep. 2019; 9:16229. [Google Scholar][Crossref]
  53. Peterson B, Knotts T, Cummings BS. Involvement of Ca 2+ independent phospholipase A2 isoforms in oxidant induced cell death.neural cell death. Neurotoxicology. 2007; 28:150-60. [Google Scholar][Crossref]
  54. Rauckhorst AJ, Pfeiffer DR, Brokemeir KM. The iPLA2γ is identified as the membrane potential sensitive phospholipase A2 in liver mitochondria. FEBS Lett. 2015; 589:2367-371. [Google Scholar][Crossref]
  55. ,Garlid KD, Jaburek M, Jezek P. Mechanism of uncoupling protein action. Biochem Soc Trans. 2001; 29:803-806. [Google Scholar][Crossref]
  56. Skulachev VP. Membrane linked systems preventing Superoxide formation. Biosci Rep. 1997; 17:347-66. [Google Scholar][Crossref]
  57. Jastroch M, Divakurani AS, Mookherjee S, Treberg JR, Brand MD. Mitochondrial proton and electron leaks. Essays Biochem. 2010; 47:53-67. [Google Scholar][Crossref]
  58. Jezek P, Zackova M, Ruzicka M, Skobisova E, Jaburek M. Mitochondrial uncoupling protein-Facts and fantasies. Physiol Res. 2004; 53:S199-S211. [Google Scholar][Crossref]
  59. Jaburek M, Varecha M, Jezek P, Garlid KD. Alkylsulfonates as probes of uncoupling protein transport mechanism. Ion pair transport demonstrates that direct H + translocation by UCP1 is not necessary for uncoupling. J Biol Chem. 2001; 276:31897-1905. [Google Scholar][Crossref]
  60. Brand MD. Mitochondrial generation of superoxide and hydroperoxide as the source of mitochondrial redox signaling. Free Radic Biol Med. 2016; 100:14-31. [Google Scholar][Crossref]
  61. Vyssokikh MY, Holtze S, Averina OA, Lyamzev KG, Panteleeva AA, Marey MV, et al. Mild depolarization of the inner mitochondrial membrane is a crucial concept of an antiaging program. Proc Natl Acad Sci USA. 2020; 117:6491-501. [Google Scholar][Crossref]
  62. Rupprecht A, Sokolenko EA, Beck V, Ninemann O, Jaburek M, Trimbuch T, et al. Role of the trans membrane potential in the membrane proton leak. Biophys J. 2010; 98:1503-511. [Google Scholar][Crossref]
  63. Yin Z, Burger N, Kula-Alwar D, Aksentijevic D, Bridges HR, Prag HA, et al. Structural basis for a complex I mutation that blocks pathological ROS production. Nat Commun. 2021; 12:707. [Google Scholar][Crossref]
  64. Kukat A, Dogan SA, Edgar D, Mourier A, Jacoby C, Maiti P, et al. Loss of UCP2attenuates Mitochondrial dysfunction without altering ROS production and uncoupling activity. PLOs Genet. 2014; 10:e1004385. [Google Scholar][Crossref]
  65. Andreyev AY, Bondareva TO, Dedukhova VI, Mokhova EN, Skulachev VP. Tsofina LM, et al. The ATP/AD Pantiporter is involved in the uncoupling effect of fatty acids in Mitochondria. Eur J Biochem. 1989; 182:585-92. [Google Scholar][Crossref]
  66. Smartsev VN, Mokhova EA, Skulachev VP. The pH – dependent reciprocal changes in contributions of ATP/ADPantiporter and aspartate/glutamate antiporter to the fatty acids induced uncoupling. FEBS Lett. 1997; 412:179-82. [Google Scholar][Crossref]
  67. Khailova LS, Prikhodko EA, Dedukhova VI, Mokhova EN, Skulachev VP. Participation of ATP/ADPantiporter in oleate and Hydroperoxide - induced uncoupling suppressed by GDP and carboxyactractyloside. Biochim Biophys Acta Bioenerg. 2006; 1757:1324-329. [Google Scholar][Crossref]
  68. Korshunov SS, Korkina OV, Ruuge EK, Skulachev VP. Starkov AA. Fatty acids as natural uncouplers preventing generation of O (-)2 andH2O2 by Mitochondria in resting state. FEBS Lett. 1998; 435:215-18. [Google Scholar][Crossref]
  69. Shabalina IG, Kramarova TV, Nedergaard J, Cannon B. Carboxyactractyloside effect on brown fat Mitochondria imply that adeninenucleotide translocator isoforms ANT1 and ANT2may be responsible for basal and fatty acids induced uncoupling respectively. Biochem. J2006; 399:405-14. [Google Scholar][Crossref]
  70. Kreiter J, Rupprecht A, Skulj S, Brkljaca Z, Zuna K, Knyazev DG, et al. Ant1 activationand inhibition patterns support the fatty acids cycling mechanism for proton transport. Int J Mol Sci. 2021; 22:2490. [Google Scholar][Crossref]
  71. Nordmann C, Strokin M, Schonfeld P, Reiser G. Putative International Journal of Medical and all body Health Research www.allmedicaljournal.com 14 roles of Ca 2+ independent phospholipase A2 in respiratory chain associated ROS production in brain Mitochondria: influence of docosahexaenoic acid and bromenol lactate. J Neurochem. 2014; 131:e163-76. [Google Scholar][Crossref]
  72. Pruchova P, Leguina-Ruzzi A, Galkin A, Jezek P, Jaburek M. Anti-oxidant activity of Calcium independent phospholipase A2γ in brain Mitochondria. Free Radic Biol Med, 2018, 128:S86. [Google Scholar][Crossref]
  73. Winterbourn CC. Are free radicles involved in thiol based redox signaling. Free Radic Biol Med. 2015; 80:164-70. [Google Scholar][Crossref]
  74. Requejo R, Hurd TR, Costa NJ, Murphy MP. Cysteine residues exposed on protein surfaces are the dominant Intra Mitochondrial thiols and may protect against oxidative damage. FEBSJ. 2010; 277:1465-480. [Google Scholar][Crossref]
  75. Nietzel T, Mostertz J, Hochgrafe F, Schwarzlander M. Redox regulation of Mitochondrial protein and proteomes by thiol switches. Mitochondrion. 2017; 33:72-83. [Google Scholar][Crossref]
  76. Rhee SG, WooHA, Kang D. The role of peroxidiredoxins in the Transduction of the H2O2 Signals. Antioxidant Redox Signal. 2018; 28:537-557. [Google Scholar][Crossref]
  77. Codreanu SG, Lieber DC. Novel approaches to identify protein adducts provided by lipid peroxidation. Free Radic Res. 2015; 49:881-7. [Google Scholar][Crossref]
  78. Xiao H, Jedrichowski MP, Schweppe DK, Huttlin EL, Yu Q, Heppner DE, et al. A quantitative tissue specificlandscape of protein Redox regulation during aging. Cell. 2020; 180:968-93. [Google Scholar][Crossref]
  79. Elimam H, Papillon J, Takano T, Cybulsky AV. Complement-mediated activation of Calcium independent phospholipase A2γ: role of protein kinases and phosphorylation. J Biol Chem. 2013; 288:3871-885. [Google Scholar][Crossref]
  80. Sadzak A, Mravljak J, Maltar-Strmecki N, Arsov Z, Baranovic G, Erceg I, et al. The structural integrity of the model lipid membraneduring induced lipid peroxidation: The role of flavonols in the inhibition of lipid peroxidation. Antioxidants. 2020; 9:430. [Google Scholar][Crossref]
  81. Tsubone TM, Junqueira HC, Baptista MS, Itri R. Contrasting roles of oxidized lipids in modulating membrane microdomains. Biochim Biophys Acta Biomembr. 2019; 1861:660-69. [Google Scholar][Crossref]
  82. Sevanian A, Wratten M, Mcleod LL, Kim E. Lipid peroxidation and phospholipase A2activity in liposomes composed of unsaturated phospholipids:a structural basis for enzyme activation. Biochim Biophys Acta. 1988; 961:316-27. [Google Scholar][Crossref]
  83. McLean LR, Hagaman KA, Davidson WS. Role of lipid structure in the activation of phospholipids. Lipids. 1993; 28:505-509. [Google Scholar][Crossref]
  84. Niki E, Yoshida Y, Saito Y, Noguchi N. Lipid peroxidation: Mechanisms, inhibition, and biological effects. Biochim Biophys Res Commun. 2005; 338:668-76. [Google Scholar][Crossref]
  85. Pennington ER, Funai K, Brown DA, Shaikh SR. The role of cardiolipin concentration and acyl chain composition on, mitochondrial inner membrane molecular organization and function. Biochim Biophys Acta Mol Cell Biol Lipids. 2019; 1864:1039-52. [Google Scholar][Crossref]
  86. Tatsuta T, Langer T. Intra mitochondrial phospholipid trafficking. Biochim Biophys Acta Mol Cell Biol Lipids. 2017; 1862:81-89. [Google Scholar][Crossref]
  87. Kiebish MA, Yang K, Liu X, Mancuso DJ, Guan S, Zhao Z, 1. Dysfunctional cardiac mitochondrial bioenergetic, lipidomic and signaling in a murine model of Barth syndrome. J Lipid Res. 2013; 54:1312-325. [Google Scholar][Crossref]
  88. Casares D, Escriba PV, Rossello CA. Membrane Lipidcomposition: effect on membrane and organelle structure, function and compartmentalization and therapeutic avenues. Int J Mol Sci. 2019; 20:2167. [Google Scholar][Crossref]
  89. Valianpour F, Wanders RJA, Barth PG, Overmars H, Van Gennip AH. Quantitative and compositional study of cardiolipin in platelets by electrospray ionization mass spectrometry: application for the identification of Barth syndrome patients. Clin Chem. 2002; 48:1390-397. [Google Scholar][Crossref]
  90. Kiebish MA, Han X, Cheng H, Chuang JH, Seyfried TN. Cardiolipin and electron transport chain abnormalities in mouse brain tumour mitochondria: lipidomic evidence supporting the Warburg theory of cancer. J Lipid Res. 2008; 49:2545-556. [Google Scholar][Crossref]
  91. Tyurina YY, Shrivastava I, Tyurin VA, Mao G, Dar HH, Watkins S, et al. Only a life lived for others is worth living: redox signaling by oxygenated phospholipids in cell fate decisions. Antioxidant Redox Signal. 2018; 29:1333-358. [Google Scholar][Crossref]
  92. Ikon N, Ryan RO. Cardiolipin and mitochon drial cristae organization. Biochim Biophys Acta Biomembr. 2017; 1859:1156-63. [Google Scholar][Crossref]
  93. Ban T, Heymann JAW, Song Z, Hinshaw JE, Chan DC. OPA1diseasealleles causing dominant optical atrophy have defects in cardiolipin- stimulated GT Phydrolysis and membrane tabulation. Hum Mol Genet. 2010; 19:2113-122. [Google Scholar][Crossref]
  94. Jussupow A, Di Luca A, Kalia VRI. How cardiolipin modulates the dynamics of respiratory complex I. Sci Adv. 2019; 5:1850. [Google Scholar][Crossref]
  95. Malkamaki A, Sharma V. Atomistic insights into cardiolipin binding sites of cytochrome c oxidase. Biochim Biophys Acta Bioenerg. 2019; 1860:224-32. MICOS [Google Scholar][Crossref]
  96. Duncan AL, Rupprecht JJ, Kunji ERS, Robinson AJ. Cardiolipin dynamics and binding to conserved residues in the mitochondrial ADP/ATP carrier.Biochim Biophys Acta Biomembr. 2018; 1860:1035-45. [Google Scholar][Crossref]
  97. Gasanov SE, Kim AA, Yaguzhinsky LS, Dagda RK. Non bilayer structuresin mitochondrial membrane regulates ATP- synthase activity. Biochim Biophys Acta Biomembr. 2018; 1860:586-99.1035-63. [Google Scholar][Crossref]
  98. Khosravi S, Harner ME. The MICOS complex, a structural element of mitochondria with versatile functions. Biol Chem. 2020; 401:765-778. [Google Scholar][Crossref]
  99. Hsu YH, Dumlao DS, Cao J, Dennis EA. Assessing phospholipase A2 activity toward cardiolipin by mass spectrometry. PLoS One. 2013; 8:e59267. [Google Scholar][Crossref]
  100. Gonzalez Bro MR, Coleman RA. Mitochondrial acyltranferases and glycerophospholipids metabolism. Biochim Biophys Acta Mol Cell Biol Lipids. 2017; 1862:49-55. [Google Scholar][Crossref]
  101. Cipolat S, Rudka T, Hartmann D, Costa V, Serneels L, Craessaerts K, et al. Mitochondrial rhomboid PARL regulates Cytochrome c releas e during apoptosis via OPA1- dependent cristae remodeling. Cell. 2006; 126:163-75. [Google Scholar][Crossref]
  102. Lopaschuk GD, Usher JR, Folmes CDL, Jaswal JS, Stanley WC. Myocardial fatty acids metabolism in health and disease. Physiol Rev. 2010; 90:207-58. [Google Scholar][Crossref]
  103. Ford DA, Hazan SL, Saffitz JE, Gross RW. The rapid andreversible activation of a Calcium independent International Journal of Medical and all body Health Research www.allmedicaljournal.com 15 plasmalogen selective phospholipase A2during myocardial ischaemia. J ClinInvest. 1991; 88:331-35. [Google Scholar][Crossref]
  104. Williams SD, Gottlieb RA. Inhibition of Calcium independent phospholipase A2 (iPLA2) attenuates phospholipid loss and is cardioprotective. Biochem. J2002; 362:23-32. [Google Scholar][Crossref]
  105. Moon SH, Mancuso DJ, Sims HF, Liu X, Nguyen al, Yang K, et al. Cardiac myocyte specific knockout of Calcium independent phospholipase A2 (iPLA2) decreases oxidized fatty acids during ischaemia /reperfusion and reduces infarct size. J Biol Chem. 2016; 291:19687-9700. [Google Scholar][Crossref]
  106. Garlid AO, Jaburek M Jacobs P, Garlid KD. Myocardial Reactive oxygen species: Which ROS signals cardio protection? AJP Heart Circ Physiol. 2013; 305:H960-H968. [Google Scholar][Crossref]
  107. Wolf MJ, Izumi Y, Zorumski CF, Gross RW. Long term potentiation requires activation of Calcium independent phospholipase A2. FEBS Lett. 1995; 377:358-62. [Google Scholar][Crossref]
  108. Adibhatla RM, Hatcher JF. Phospholipase A2, Reactive oxygen species,and lipid peroxidation in CNS pathologies. J Biochem Mol Biol. 2008; 41:560-67. [Google Scholar][Crossref]
  109. Mancuso DJ, Kotzbauer P, Woznac DF, Sims HF, Jenkins CM, Guan S, et al. Genetic ablation of Calcium independent phospholipase A2γ leads to alterations in hippocampal cardiolipin content and molecular species distribution, mitochondrial degeneration, autophagy and cognitive dysfunction. J Biol Chem. 2009; 284:35632-5644 [Google Scholar][Crossref]
  110. Chao H, Liu Y, Fu X, Xu X, Bao Z, Lin C, et al. Lowered iPLA2γ activity causes increased mitochondrial lipid peroxidation and mitochondrial dysfunction in a rotenone induced model of parkinson’s disease. Exp Neurol. 2016; 300:74-86. [Google Scholar][Crossref]
  111. Chao H, Anthonymuthu TS, Kenny EM, Amoscato AA, Cole LK, Hatch GM, et al. Disentangling oxidization /hydrolysis reactions of brain mitochondrial cardiolipins in pathogenesis of traumatic injury. JCI Insight. 2018; 3:e97677. [Google Scholar][Crossref]
  112. Jaburek M, Jezek P, Porter RK. Uncoupling mechanism and redox regulation of mitochondrial uncoupling protein1 (UCP1).Elsevier BV. 2019; 1860:259-69. [Google Scholar][Crossref]
  113. Mancuso DJ, Sims HF, Han X, Jenkins CM, Shao PG, Yang K, et al. Genetic ablation of Calcium independent phospholipase A2γ leads to alterations in mitochondrial lipid Metabolism. J Biol Chem. 2007; 282:34611-4622. [Google Scholar][Crossref]
  114. Schweizer S, Leibisch G, Oeckl J, Hoering M, Seeliger C, Klingenspor M, et al. The lipiodome of primary murine White, brite and brown adipocytes-impact of betaadrenergic stimulation. PLoS Biol. 2019; 17:e3000412. [Google Scholar][Crossref]
  115. Chouchani ET, Kazak L, Jedrichowski MP, Lu GZ, Erickson BK, Szpyt J, et al. Mitochondrial ROS regulate thermogenic energy expenditure and sulfenylation of UCP1.Nature. 2016; 532:112-16. [Google Scholar][Crossref]

How to Cite

Kaur, K. K., Allahbadia, G., & Singh, M. (2020). Synergistic anti-oxidant Actions of Mitochondrial Palatin-like PhosphoLipaseA2Domain-Containing Protein-8(PNPLA8/ iPLA2γ) with the Fatty Acids (FA)-Translocating-SLC-25 Gene Family Transporters with their Sequelae-A Review. International Journal of Medical and All Body Health Research, 1(4), 01-15.

Kaur, Kulvinder Kochar, et al. "Synergistic anti-oxidant Actions of Mitochondrial Palatin-like PhosphoLipaseA2Domain-Containing Protein-8(PNPLA8/ iPLA2γ) with the Fatty Acids (FA)-Translocating-SLC-25 Gene Family Transporters with their Sequelae-A Review." International Journal of Medical and All Body Health Research, vol. 1, no. 4, 2020, pp. 01-15.

Kaur, K. K., Allahbadia, G. and Singh, M. (2020) 'Synergistic anti-oxidant Actions of Mitochondrial Palatin-like PhosphoLipaseA2Domain-Containing Protein-8(PNPLA8/ iPLA2γ) with the Fatty Acids (FA)-Translocating-SLC-25 Gene Family Transporters with their Sequelae-A Review', International Journal of Medical and All Body Health Research, 1(4), pp. 01-15.

Kaur KK, Allahbadia G, Singh M. Synergistic anti-oxidant Actions of Mitochondrial Palatin-like PhosphoLipaseA2Domain-Containing Protein-8(PNPLA8/ iPLA2γ) with the Fatty Acids (FA)-Translocating-SLC-25 Gene Family Transporters with their Sequelae-A Review. International Journal of Medical and All Body Health Research. 2020;1(4):01-15.

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