Prostaglandins, Leukotrienes and Essential Fatty Acids
Volume 82, Issue 4 , Pages 165-172 , April 2010

Phosphatidylserine-dependent neuroprotective signaling promoted by docosahexaenoic acid

References 

  1. Salem N. Omega-3 Fatty Acids: Molecular and Biochemical Aspects. New York: Alan R. Liss; 1989;pp 109–228
  2. Kim HY. Novel metabolism of docosahexaenoic acid in neural cell. J. Biol. Chem. 2007;282:18661–18665
  3. Willatts P, Forsyth JS, Di Modugno MK, Varma S, Colvin M. Effect of long-chain polyunsaturated fatty acids in infant formula on problem solving at 10 months of age. Lancet. 1998;352:688–691
  4. Birch EE, Garfield S, Hoffman DR, Uauy RD, Birch DG. A randomized controlled trial of early dietary supply of long-chain polyunsaturated fatty acids and mental development in term infants. Dev. Med. Child Neurol. 2000;42:174–181
  5. Gamoh S, Hashimoto M, Sugioka K, Shahdat Hossain M, Hata N, Misawa Y, et al. Chronic administration of docosahexaenoic acid improves reference memory-related learning ability in young rats. Neuroscience. 1999;93:237–241
  6. Moriguchi T, Greiner RS, Salem N. Behavioral deficits associated with dietary induction of decreased brain docosahexaenoic acid concentration. J Neurochem. 2000;75:2563–2573
  7. Catalan J, Moriguchi T, Slotnick B, Murthy M, Greiner RS, Salem N. Cognitive deficits in docosahexaenoic acid-deficient rats. Behav. Neurosci. 2002;116:1022–1031
  8. McNamara RK, Hahn CG, Jandacek R, Rider T, Tso P, Stanford SK. Selective deficits in the omega-3 fatty acid docosahexaenoic acid in the postmortem orbitofrontal cortex of patients with major depressive disorder. Biol. Psychiatry. 2007;62:17–24
  9. Martinez M. Severe deficiency of docosahexaenoic acid in peroxisomal dis ordersa defect of delta 4 desaturation?. Neurology. 1990;40:1292–1298
  10. Soderberg M, Edlund C, Kristensson K, Dallner G. Fatty acid composition of brain phospholipids in aging and in Alzheimer’s disease. Lipids. 1991;26:421–425
  11. Martinez M, Vazquez E, Garcia-Silva MT, Manzanares J, Bertran JM, Castello F, et al. Therapeutic effects of docosahexaenoic acid ethylester in patients with generalized peroxisomal disorders. Am. J. Clin. Nutr. 2000;71:376S
  12. Freeman MP, Hibbeln JR, Wisner KL, Davis JM, Mischoulon D, Peet M, et al. Omega-3 fatty acids: evidence basis for treatment and future research in psychiatry. J. Clin. Psychiatry. 2006;67:1954–1967
  13. Calon F, Lim GP, Yang F, Morihara T, Teter B, Obeda O, et al. Docosahexaenoic acid protects from dendritic pathology in an Alzheimer’s disease mouse model. Neuron. 2004;43:633–645
  14. Okada M, Amamoto T, Tomonaga M, Kawachi A, Yazawa K, Mine K, et al. The chronic administration of docosahexaenoic acid reduces the spatial cognitive deficit following transient forebrain ischemia in rats. Neuroscience. 1996;71:17–25
  15. Kim HY, Akbar M, Lau A, Edsall L. Inhibition of neuronal apoptosis by docosahexaenoic acid (22:6n-3): role of phosphatidylserine in anti-apoptotic effect. J. Biol. Chem. 2000;275:35215–35223
  16. Akbar M, Kim HY. Protective effects of docosahexaenoic acid (DHA) in staurosporine-induced apoptosis: involvement of wortmanin-sensitive path-way. J. Neurochem. 2002;82:655–665
  17. Akbar M, Calderon F, Wen Z, Kim HY. Docosahexaenoic acid: a positive modulator of Akt signaling in neuronal survival. Proc Natl. Acad. Sci. USA. 2005;102:10858–10863
  18. Kawakita E, Hashimoto M, Shido O. Docosahexaenoic acid promotes neurogenesis in vitro and in vivo. Neuroscience. 2006;139:991–997
  19. Calderon F, Kim HK. Docosahexaenoic acid promotes neurite growth in hippocampal neurons. J. Neurochem. 2004;90:979–988
  20. Cao D, Kevala K, Kim J, Moon HS, Jun SB, Lovinger D, et al. Docosahexaenoic acid promotes hippocampal neuronal development and synaptic function. J. Neurochem. 2009;111:510–521
  21. Yavin E, Himovichi E, Eilam R. Delayed cell migration in the developing rat brain following maternal Omega 3 alpha linolenic acid dietary deficiency. Neuroscience. 2009;162:1011–1022
  22. Kanfer. JN. The base exchange enzymes and phospholipase D of mammalian tissue. Can. J. Biochem. 1980;5:81370–81380
  23. Vance JE, Steenbergen R. Metabolism and functions of phosphatidylserine. Prog. Lipid Res. 2005;44:207–234
  24. Kuge O, Nishijima M. Phosphatidylserine synthase I and II of mammalian cells. Biochim. Biophys. Acta. 1997;1348:151–156
  25. Kuge O, Saito K, Nishijima M. Cloning of a Chinese hamster ovary (CHO) cDNA encoding phosphatidylserine synthase (PSS) II, overexpression of which suppresses the phosphatidylserine biosynthetic defect of a PSS I-lacking mutant of CHO-K1 cells. J. Biol. Chem. 1997;272:19133–19139
  26. Stone J, Cui Z, Vance JE. Cloning and expression of mouse liver phosphatidylserine synthase-1 cDNA. Overexpression in rat hepatoma cells inhibits the CDP–ethanolamine pathway for phosphatidylethanolamine biosynthesis. J. Biol. Chem. 1998;273:7293–7302
  27. Voelker DR. Phosphatidylserine decarboxylase. Biochim. Biophys. Acta. 1997;1348:236–244
  28. Kim HY, Bigelow J, Kevala JH. Substrate preference in phosphatidylserine biosynthesis for docosahexanoic acid containing species. Biochemistry. 2004;43:1030–1036
  29. Hamilton J, Greiner R, Salem. N, Kim HY. N-3 fatty acid deficiency decrease phosphatidylserine accumulation selectively in neuronal tissues. Lipids. 2000;35:863–869
  30. Murthy M, Hamilton J, Greiner RS, Moriguchi T, Salem N, Kim HY. Differential effects of n-3 fatty acid deficiency on phospholipids molecular species composition in the rat hippocampus. J. Lipid Res. 2002;43:611–617
  31. Kim HY, Akbar M, Lau A. Effects of docosapentaenoic acid on neuronal apoptosis. Lipids. 2003;38:453–457
  32. Galli C, Trzeciak. HI, Paoletti R. Effects of dietary fatty acids on the fatty acid composition of brain ethanolamine phosphoglyceride: Reciprocal replacement of n-6 and n-3 polyunsaturated fatty acids. Biochim. Biophys. Acta (BBA)—Lipids Lipid Metab. 1971;248:449–454
  33. Guo M, Stockert L, Akbar M, Kim HY. Neuronal specific increase of phosphatidylserine by docosahexaenoic acid. J. Mol. Neurosci. 2007;33:67–73
  34. Bourre JM, Faivre A, Dumont O, Nouvelot A, Loudes C, Puymirat J, et al. Effect of polyunsaturated fatty acids on fetal mouse brain cells in culture in a chemically defined medium. J. Neurochem. 1983;41:1234–1242
  35. Contestabile A. Cerebellar granule cells as a model to study mechanisms of neuronal apoptosis or survival in vivo and in vitro. Cerebellum. 2002;1:41–55
  36. Boni. LT, Rando RR. The nature of protein kinase C activation by physically defined phospholipid vesicles and diacylglycerols. J. Biol. Chem. 1985;260:10819–10825
  37. Newton AC, Keranen LM. Phophatidyl-l-serine is necessary for protein kinase C’s high-affinity interaction with diacylglycerol-containing membranes. Biochemistry. 1994;33:6651–6658
  38. Verdaguer N, Corbalan-Garcia S, Ochoa WF, Fita I, Gomez-Fernandez. JC. Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calphα directly to phosphatidylserine. EMBO J. 1999;18:6329–6338
  39. Improta-Brears T, Ghosh S, Bell RM. Mutational analysis of Raf-1 cysteine rich domain: requirement for a cluster of basic aminoacids for interaction with phosphatidylserine. Mol. Cell Biochem. 1999;198:171–178
  40. Ghosh S, Strum JC, Sciorra VA, Daniel L, Bell RM. R. Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells. J. Biol. Chem. 1996;271:8472–8480
  41. Brazil DP, Hemmings BA. Ten years of protein kinase B signalling: a hard Akt to Follow. Trends Biochem. Sci. 2001;26:657–664
  42. Alessi DR, Cohen P. Mechanism of activation and function of protein kinase B. Curr. Opin. Genet. Dev. 1998;8:55–62
  43. Downward J. Mechanisms and consequences of activation of protein kinase B/Akt. Curr. Opin. Cell Biol. 1998;10:262–267
  44. Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. Phosphorylation and regulation of Akt/PKB by the rictor-mTor complex. Science. 2005;307:1098–1101
  45. Thiel G, Ekici M, Rossler OG. Regulation of cellular proliferation,differentiation and cell death by activated Raf. Cell Commun. Signal. 2009;7:8
  46. Wellbock C, Karasarides M, Marais R. The Raf proteins take centre stage. Nat. Rev. Mol. Cell Biol. 2004;5:875–885
  47. D. Stokoe, S.G. Macdonald, K. Cadwallader, M. Symons, J.F. Hancock. Activation of Raf as a result of recruitment to the plasma membrane. Science 264 (1994) 1463–1467; Correction, Science 266 (1994) 1792–1793.
  48. Leevers SJ, Paterson HF, Marshall CJ. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature. 1994;369:411–414
  49. King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia S, et al. The protein kinase Pak3 positively regulates Raf-1 through phosphorylation of serine 338. Nature. 1998;396:180–183
  50. Ballif BA, Blenis J. Molecular mechanisms mediating mammalian mitogen-activated protein kinase (MAPK) kinase (MEK)-MAPK cell survival signals. Cell Growth Differ. 2001;12:397–408
  51. Huser M, Luckett J, Chiloeches A, Mercer K, Iwobi M, Giblett S, et al. MEK kinase activity is not necessary for Raf-1 function. EMBO J. 2001;20:1940–1951
  52. Liu L, Xie LY, Lou L. PI3K is required for insulin-stimulated but not EGF-stimulated ERK1/2 activation. Eur. J. Cell Biol. 2006;85:367–374
  53. Nishizuka Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 1995;9:484–496
  54. Goodnight JA, Mischak H, Kolch W, Mushinski JF. Immunocytochemical localization of eight protein kinase C isozymes overexpressed in NIN 3T3 fibroblasts: isoform-specific association with microfilaments, Golgi, endoplasmic reticulum, and nuclear and cell membranes. J. Biol. Chem. 1995;270:9991–10001
  55. Gutcher I, Webb PR, Anderson NG. The isoform specific regulation of apoptosis by protein kinase C. Cell. Mol. Life Sci. 2003;60:1061–1070
  56. Goodnight JA, Mischak H, Mushinski JF. Selective involvement of protein kinase C isozymes in differentiation and neoplastic transformation. Adv. Cancer Res. 1994;64:159–209
  57. Papp H, Czifra G, Bodó E, Lázár J, Kovács I, Aleksza M, et al. Opposite roles of protein kinase C isoforms in proliferation, differentiation, apoptosis, and tumorigenicity of human HaCaT keratinocytes. Cell. Mol. Life Sci. 2004;61:1095–1105
  58. Newton AC. Lipid activation of protein kinases. J. Lipid. Res. 2009;50:S266–S271
  59. Mosior M, Newton AC. Mechanism of apparent cooperativity in the interaction of protein kinase C with phosphatidylserine. Biochemistry. 1998;37:17271–17279
  60. Verdaguer N, Corbalan-Garcia1 S, Ochoa WF, Fita I, Gomez-Fernandez JC. Ca2+ bridges the C2 membrane-binding domain of protein kinase Cα directly to phosphatidylserine. EMBO J. 1999;18:6329–6338
  61. Johnson JE, Giorgione J, Newton AC. The C1 and C2 domains of protein kinase C are independent membrane targeting modules, with specificity for phosphatidylserine conferred by the C1 domain. Biochemistry. 2000;39:11360–11369
  62. Moelling K, Schad K, Bosse M, Zimmermann S, Schweneker M. Regulation of Raf-Akt Cross-talk. J Biol. Chem. 2002;277:31099–31106
  63. Zimmermann S, Moelling K. Phosphorylation and regulation of Raf by Akt (protein kinase B). Science. 1999;286:1741–1744
  64. Rommel C, Clarke BA, Zimmerman S, Nunez L, Rossman R, Reid K, et al. Differentiation stage specific inhibition of the Raf–MEK–ERK pathway by Akt. Science. 1999;286:1738–1741
  65. Corbit KC, Trakul N, Eves EM, Diaz B, Marshall M, Rosner MR. Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J. Biol. Chem. 2003;278:13061–13068
  66. Weyrich P, Neuscheler D, Melzer M, Hennige AM, Häring HU, Lammers R. The Par6alpha/αPKC complex regulates Akt1 activity by phosphorylating Thr34 in the PH-domain. Mol. Cell Endocrinol. 2007;268:30–36

PII: S0952-3278(10)00069-4

doi: 10.1016/j.plefa.2010.02.025

Prostaglandins, Leukotrienes and Essential Fatty Acids
Volume 82, Issue 4 , Pages 165-172 , April 2010