Hepatocyte Growth Factor Liver Regeneration Cancer Cachexia Carnitine Palmitoyltransferase Liver Fatty Acid Binding Protein 
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4.6. References

  1. 1.
    W. Kidwell, M. Monaco, M. Wicha, and G. Smith, Unsaturated fatty acid requirements for growth and survival of a rat mammary tumor cell line, Cancer Res 38:4091–4100 (1978).PubMedGoogle Scholar
  2. 2.
    M. Wicha, L. Liotta, and W. Kidwell, Effects of free fatty acids on the growth of normal and neoplastic rat mammary epithelial cells, Cancer Res 39:426–435 (1979).PubMedGoogle Scholar
  3. 3.
    S. Abraham, and L. Hillyard, Effect of dietary 18-carbon fatty acids on growth of transplantable mammary adenocarcinomas in mice., J Natl Cancer Inst 71:601–605 (1983).PubMedGoogle Scholar
  4. 4.
    C. Maziere, M.-A. Conte, J. Degonville, D. Ali, and J.-C. Maziere, Cellular enrichment with polyunsaturated fatty acids induces an oxidative stress and activates the transcription factors AP1 and NF-kappaB, Biochem Biophys Res Comm 265:116–122 (1999).CrossRefPubMedGoogle Scholar
  5. 5.
    I. Rusyn, C. Bradham, L. Cohn, et al., Corn oil rapidly activates nuclear factor-kappaB in hepatic Kupffer cells by oxidant-dependent mechanisms, Carcinogenesis 20:2095–2100 (1999).CrossRefPubMedGoogle Scholar
  6. 6.
    I. Rusyn, H. Tsukamoto, and R. Thurman, WY-14 643 rapidly activates nuclear factor kappaB in Kupffer cells before hepatocytes, Carcinogenesis 19:1217–1222 (1998).CrossRefPubMedGoogle Scholar
  7. 7.
    L. Sauer, and R. Dauchy, Blood nutrient relationships during the onset of an acute fast nt concentrations and tumor growth in vivo in rats:, Cancer Res 47:1065–1068 (1987A).PubMedGoogle Scholar
  8. 8.
    L. Sauer, and R. Dauchy, Stimulation of tumor growth in adult rats in vivo during acute streptozotocin-induced diabetes, Cancer Res 47:1756–1761 (1987B).PubMedGoogle Scholar
  9. 9.
    S. Beck, and M. Tisdale, Effect of insulin on weight loss and tumour growth in a cachexia model., Br J Cancer 59:677–681 (1989).PubMedGoogle Scholar
  10. 10.
    W. Zhang, S. Churchill, R. Lindahl, and P. Churchill, Regulation of D-beta-hydroxybutyrate dehydrogenase in rat hepatoma cell lines, Cancer Res 49:2433–2437 (1989).PubMedGoogle Scholar
  11. 11.
    L. Sauer, and R. Dauchy, Identification of linoleic and arachidonic acids as the factors in hyperlipemic blood that increase [3H]thymidine incorporation in hepatoma 7288CTC perfused in situ, Cancer Res 48:3106–3111 (1988).PubMedGoogle Scholar
  12. 12.
    L. Sauer, and R. Dauchy, Uptake of plasma lipids by tissue-isolated hepatomas 7288CTC and 7777 in vivo, Br J Cancer 66:290–296 (1992A).PubMedGoogle Scholar
  13. 13.
    R. Daoust, The passage of G2 hepatocytes into mitosis during fasting., Chem Biol Interact 62:99–103 (1987).PubMedGoogle Scholar
  14. 14.
    R. Daoust, Stimulation of G2-arrested rat liver and pancreas cells by fasting., Gastroenterology 97:219–221 (1989).PubMedGoogle Scholar
  15. 15.
    J. Bassuk, P. Tsichlis, and S. Sorof, Liver fatty acid binding protein is the mitosis-associated polypeptide target of a carcinogen in rat hepatocytes., Proc Natl Acad Sci USA 84:7547–7551 (1987).PubMedGoogle Scholar
  16. 16.
    S. Sorof, Modulation of mitogenesis by liver fatty acid binding protein, Cancer Metast Rev 13:317–336 (1994).CrossRefGoogle Scholar
  17. 17.
    H. Mulligan, and M. Tisdale, Lipogenesis in tumour and host tissues in mice bearing colonic adenocarcinomas, Br J Cancer 63:719–722 (1991A).PubMedGoogle Scholar
  18. 18.
    H. Mulligan, and M. Tisdale, Metabolic substrate utilization by tumour and host tissues in cancer cachexia, Biochem J 277:321–326 (1991B).PubMedGoogle Scholar
  19. 19.
    H. Mulligan, S. Beck, and M. Tisdale, Lipid metabolism in cancer cachexia, Br J Cancer 66:57–61 (1992).PubMedGoogle Scholar
  20. 20.
    C. Bing, M. Brown, P. King, P. Collins, M. J. Tisdale, and G. Williams, Increased gene expression of brown fat uncoupling protein (UCP)1 and skeletal muscle UCP2 and UCP3 in MAC16-induced cancer cachexia, Cancer Res 60:2405–10 (2000).PubMedGoogle Scholar
  21. 21.
    H. Mulligan, and M. Tisdale, Effect of the lipid-lowering agent bezafibrate on tumour growth rate in vivo, Br J Cancer 64:1035–1038 (1991C).PubMedGoogle Scholar
  22. 22.
    M. Tisdale, R. Brennan, and K. Fearon, Reduction of weight loss and tumour size in a cachexia model by a high fat diet, Br J Cancer 56:39–43 (1987).PubMedGoogle Scholar
  23. 23.
    A. Moir, B. Park, and V. Zammit, Quantification in vivo of the effects of different types of dietary fat on the loci of control involved in hepatic triacylglycerol secretion, Biochem J 308:537–542 (1995).PubMedGoogle Scholar
  24. 24.
    S. Wong, P. Nestel, R. Trimble, G. Storer, R. Illman, and D. Topping, The adaptive effects of dietary fish and safflower oil on lipid and lipoprotein metabolism in perfused rat liver, Biochim Biophys Acta 792:103–109 (1984).PubMedGoogle Scholar
  25. 25.
    D. Topping, R. Trimble, and G. Storer, Failure of insulin to stimulate lipogenesis and triacylglycerol secretion in perfused livers from rats adapted to dietary fish oil, Biochim Biophys Acta 927:423–428 (1987).PubMedGoogle Scholar
  26. 26.
    T. Ide, M. Murata, and M. Sugano, Stimulation of the activities of hepatic fatty acid oxidation enzymes by dietary fat rich in a-linolenic acid in rats, J Lipid Res 37:448–463 (1996).PubMedGoogle Scholar
  27. 27.
    A. Demoz, D. Asiedu, O. Lie, and R. Berge, Modulation of plasma and hepatic oxidative status and changes in plasma lipid profile by n-3 (EPA and DHA), n-6 (corn oil) and a 3-thia fatty acid in rats., Biochim Biophys Acta 1199:238–244 (1994).PubMedGoogle Scholar
  28. 28.
    J. Dallongeville, E. Baugé, A. Tailleux, et al., Peroxisome proliferator-activated receptor alpha is not rate-limiting for the lipoprotein-lowering action of fish oil., J Biol Chem 16 276:4634–4639 (2001).Google Scholar
  29. 29.
    L. Madsen, L. Frøyland, E. Dyrøy, K. Helland, and R. Berge, Docosahexaenoic and eicosapentaenoic acids are differently metabolized in rat liver during mitochondria and peroxisome proliferation, J Lipid Res 39:583–593 (1998).PubMedGoogle Scholar
  30. 30.
    J. McGarry, Banting lecture, 2001: dysregulation of fatty acid metabolism in the etiology of type 2 diabetes, Diabetes 51:7–18 (2002).PubMedGoogle Scholar
  31. 31.
    D. Rolfe, A. Hulbert, and M. Brand, Characteristics of mitochondrial proton leak and control of oxidative phosphorylation in the major oxygen-consuming tissues of the rat, Biochim Biophys Acta 1188:405–416 (1994).PubMedGoogle Scholar
  32. 32.
    I. Reynolds, and T. Hastings, Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation, J Neurosci 15:3318–3327 (1995).PubMedGoogle Scholar
  33. 33.
    V. Skulachev, Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants, Quart Rev Biophys 29:169–202 (1996).Google Scholar
  34. 34.
    A. Nègre-Salvayre, C. Hirtz, G. Carrera, et al., A role for uncoupling protein-2 as a regulator of mitochondrial hydrogen peroxide generation, FASEB J 11:809–815 (1997).PubMedGoogle Scholar
  35. 35.
    A. Stout, H. Raphael, B. Kanterewicz, E. Klann, and I. Reynolds, Glutamate-induced neuron death requires mitochondrial calcium uptake, Nature Neurosci 1:366–373 (1998).PubMedGoogle Scholar
  36. 36.
    S. Korshunov, O. Kokina, E. Ruuge, V. Skulachev, and A. Starkov, Fatty acids as natural uncouplers preventing generation of O2 and H2O2 by mitochondria in the resting state, FEBS Letts 435:215–218 (1998).CrossRefGoogle Scholar
  37. 37.
    S. Bechoua, M. Dubois, Z. Dominguez, et al., Protective effect of docosahexaenoic acid against hydrogen peroxide-induced oxidative stress in human lymphocytes., Biochem Pharmacol 57:1021–1030 (1999).CrossRefPubMedGoogle Scholar
  38. 38.
    B. A. Narayanan, N. K. Narayanan, B. Simi, and B. S. Reddy, Modulation of inducible nitric oxide synthase and related proinflammatory genes by the omega-3 fatty acid docosahexaenoic acid in human colon cancer cells, Cancer Res 63:972–9 (2003).PubMedGoogle Scholar
  39. 39.
    E. Miles, F. Wallace, and P. Calder, Dietary fish oil reduces intercellular adhesion molecule 1 and scavenger receptor expression on murine macrophages, Athersclerosis 152:43–50 (2000).Google Scholar
  40. 40.
    T. N. Tran, and B. O. Christophersen, Partitioning of polyunsaturated fatty acid oxidation between mitochondria and peroxisomes in isolated rat hepatocytes studied by HPLC separation of oxidation products, Biochim Biophys Acta 1583:195–204 (2002).PubMedGoogle Scholar
  41. 41.
    M. Surette, J. Whelan, K. Broughton, and J. Kinsella, Evidence for mechanisms of the hypotriglyceridemic effect of n-3 polyunsaturated fatty acids, Biochim Biophys Acta 1126:199–205 (1992).PubMedGoogle Scholar
  42. 42.
    H. Wang, X. Chen, and E. Fisher, N-3 fatty acids stimulate intracellular degradation of apoprotein B in rat hepatocytes, J Clin Invest 91:1380–1389 (1993).PubMedGoogle Scholar
  43. 43.
    C. Van Noorden, Effects of n-3 and n-6 polyunsaturated fatty acid-enriched diets on lipid metabolism in periportal and pericentral compartments of female rat liver lobules and the consequences for cell proliferation after partial hepatectomy, J Lipid Res 36:1708–1720 (1995).PubMedGoogle Scholar
  44. 44.
    P. Tollet, M. Stromstedt, L. Froyland, R. Berge, and J. Gustafsson, Pretranslational regulation lf cytochrome P4504A1 by free fatty acids in primary cultures of rat hepatocytes, J Lipid Res 35:248–254 (1994).PubMedGoogle Scholar
  45. 45.
    N. Willumsen, S. Hexeberg, J. Skorve, M. Lundquist, and R. Berge, Docosahexaenoic acid shows no triglyceride-lowering effects but increases the peroxisomal fatty acid oxidation in liver of rats, J Lipid Res 34:13–22 (1993).PubMedGoogle Scholar
  46. 46.
    L. Frøyland, L. Madsen, H. Vaagenes, et al., Mitochondrion is the principal target for nutritional and pharmacological control of triglyceride metabolism., J Lipid Res 38:1851–1858 (1997).PubMedGoogle Scholar
  47. 47.
    A. Rustan, B. Hustvedt, and C. Drevon, Postprandial decrease in plasma unesterified fatty acids during n-3 fatty acid feeding is not caused by accumulation of fatty acids in adipose tissue, Biochim Biophys Acta 1390:245–257 (1998).PubMedGoogle Scholar
  48. 48.
    A. Dannenberg, and M. Reidenberg, Dietary fatty acids are also drugs., Clin Pharmacol Ther 55: 5–9 (1994).PubMedGoogle Scholar
  49. 49.
    D. Rose, and J. Connolly, Effects of fatty acids and inhibitors of eicosanoid synthesis on the growth of a human breast cancer cell line in culture, Cancer Res 50:7139–7144 (1990).PubMedGoogle Scholar
  50. 50.
    D. Rose, J. Connolly, and X. Liu, Effects of linoleic acid and gamma-linolenic acid on the growth and metastasis of a human breast cancer cell line in nude mice and on its growth and invasive capacity in vitro, Nutr Cancer 24:33–45 (1995).PubMedGoogle Scholar
  51. 51.
    V. Chajes, W. Sattler, A. Stranzl, and G. Kostner, Influence of n-3 fatty acids on the growth of human breast cancer cells in vitro: relationship to peroxides and vitamin-E., Breast Cancer Res Treat 34:199–212 (1995).PubMedGoogle Scholar
  52. 52.
    L. Maehle, E. Eilertsen, S. Mollerup, S. Schonberg, H. Krokan, and A. Haugen, Effects of n-3 fatty acids during neoplastic progression and comparison of in vitro and in vivo sensitivity of two human tumour cell lines, Br J Cancer 71:691–696 (1995).PubMedGoogle Scholar
  53. 53.
    P. Lai, J. Ross, K. Fearon, J. Anderson, and D. Carter, Cell cycle arrest and indection of apoptosis in pancreatic cancer cells exposed to eicosapentaenoic acid in vitro, Br J Cancer 74:1375–1383 (1996).PubMedGoogle Scholar
  54. 54.
    H. Finstad, M. Myhrstad, H. Heimli, et al., Multiplication and death-type of leukemia cell lines exposed to very long-chain polyunsaturated fatty acids., Leukemia 12:921–929 (1998).CrossRefPubMedGoogle Scholar
  55. 55.
    H. Bartram, A. Gostner, W. Scheppach, et al., Effects of fish oil on rectal cell proliferation, mucosal fatty acids, and prostaglandin E2 release in healthy subjects., Gastroenterology 105:1317–1322 (1993).PubMedGoogle Scholar
  56. 56.
    M. Anti, F. Armelao, G. Marra, et al., Effects of different doses of fish oil on rectal cell proliferation in patients with sporadic colonic adenomas., Gastroenterology 107:1709–1718 (1994).PubMedGoogle Scholar
  57. 57.
    Y.-C. Huang, J. Jessup, R. Forse, et al., n-3 Fatty acids decrease colonic epithelial cell proliferation in high-risk bowel mucosa, Lipids 31:S313–S317 (1996).PubMedGoogle Scholar
  58. 58.
    S. Endres, S. Meydani, R. Ghorbani, R. Schindler, and C. Dinarello, Dietary supplementation with n-3 fatty acids suppresses interleukin-2 production and mononuclear cell proliferation., J Leukocyte Biol 54:599–603 (1993).PubMedGoogle Scholar
  59. 59.
    G. Johanning, and T. Lin, Unsaturated fatty acid effects on human breast cancer cell adhesion, Nutr Cancer 24:57–66 (1995).PubMedGoogle Scholar
  60. 60.
    J. Gore, P. Besson, C. Hoinard, and P. Bougnoux, Na+-H+ antiporter activity in relation to membrane fatty acid composition and cell proliferation, Am J Physiol 266:C110–C120 (1994).PubMedGoogle Scholar
  61. 61.
    H. Obermeier, N. Hrboticky, and A. Sellmayer, Differential effects of polyunsaturated fatty acids on cell growth and differentiation of premonocytic U937 cells, Biochim Biophys Acta 1266:179–185 (1995).PubMedGoogle Scholar
  62. 62.
    H. Gabor, L. Hillyard, and S. Abraham, Effect of dietary fat on growth kinetics of transplantable mammary carcinoma in BALB/c mice., J Natl Cancer Inst 74:1299–1305 (1985).PubMedGoogle Scholar
  63. 63.
    H. Gabor, and S. Abraham, Effect of dietary menhaden oil on tumour cell loss and the accumulation of mass of a transplantable mammary adenocarcinoma in BALB/c mice., J Natl Cancer Inst 76:1223–1229 (1986).PubMedGoogle Scholar
  64. 64.
    L. Sauer, and R. Dauchy, The effect of omega-6 and omega-3 fatty acids on 3Hthymidine incorporation in hepatoma 7288CTC perfused in situ, Br J Cancer 66:297–303 (1992B).PubMedGoogle Scholar
  65. 65.
    S. Price, and M. Tisdale, Mechanism of inhibition of a tumor lipid-mobilizing factor by eicosapentaenoic acid, Cancer Res 58:4827–4831 (1998).PubMedGoogle Scholar
  66. 66.
    H. Hussey, and M. Tisdale, Effect of a cachectic factor on carbohydrate metabolism and attenuation by eicosapentaenoic acid, Br J Cancer 80:1231–1235 (1999).CrossRefPubMedGoogle Scholar
  67. 67.
    P. Todorov, T. Mcdevitt, D. Meyer, H. Ueyama, I. Ohkubo, and M. Tisdale, Purification and characterization of a tumor lipid-mobilizing factor, Cancer Res 58:2353–2358 (1998).PubMedGoogle Scholar
  68. 68.
    K. Hirai, H. Hussey, M. Barber, S. Price, and M. Tisdale, Biological evaluation of a lipid-mobilizing factor isolated from the urine of cancer patients, Cancer Res 58:2359–2365 (1998).PubMedGoogle Scholar
  69. 69.
    J. Pell, J. Brown, and I. Johnson, Polyunsaturated fatty acids of the n–3 series influence intestinal crypt cell production in rats, Carcinogenesis 15:1115–1119 (1994).PubMedGoogle Scholar
  70. 70.
    G. Calviello, P. Palozza, E. Piccioni, et al., Dietary supplementation with eicosapentaenoic and docosahexaenoic acid inhibits growth of Morris hepatocarcinoma 3924A in rats: effects on proliferation and apoptosis., IntI J Cancer 75:699–705 (1998).Google Scholar
  71. 71.
    G. Calviello, L. Tessitore, E. Piccioni, P. Palozza, P. Franceschelli, and G. Bartoli, EPA inhibits the development of focal proliferative lesions during hepatocarcinogenesis in rat., Gastroenterology 110:A1162 (1996).Google Scholar
  72. 72.
    N. Murray, L. Davidson, R. Chapkin, W. Gustafson, D. Shattenberg, and A. Fields, Overexpression of protein kinase C betaII induces colonic hyperproliferation and increased sensitivity to colon carcinogenesis, J Cell Biol 145:699–711 (1999).CrossRefPubMedGoogle Scholar
  73. 73.
    N. R. Murray, C. Weems, L. Chen, et al., Protein kinase C betaII and TGFbetaRII in omega-3 fatty acid-mediated inhibition of colon carcinogenesis, J Cell Biol 157:915–20 (2002).CrossRefPubMedGoogle Scholar
  74. 74.
    Y. Lin, M. Smit, R. Havinga, H. Verkade, R. Vonk, and F. Kuipers, Differential effects of eicosapentaenoic acid on glycerolipid and apolipoprotein B metabolism in primary human hepatocytes compared to HepG2 cells and primary rat hepatocytes, Biochim Biophys Acta 1256:88–96 (1995).PubMedGoogle Scholar
  75. 75.
    P. Needleman, A. Raz, M. Minkes, J. Ferrendelli, and H. Sprecher, Triene prostaglandins: prostacyclin and thromboxane biosynthesis and unique biological properties, Proc Natl Acad Sci USA 76:944–948 (1979).PubMedGoogle Scholar
  76. 76.
    W. Lands, Biochemistry and physiology of n-3 fatty acids, FASEB J 6:2530–2536 (1992).PubMedGoogle Scholar
  77. 77.
    L. Sauer, R. Dauchy, and D. Blask, Mechanism for the antitumor and anticachectic effects of n-3 fatty acids, Cancer Res 60:5289–5295 (2000).PubMedGoogle Scholar
  78. 78.
    E. Pizer, S. Lax, F. Kuhajda, G. Pasternack, and R. Kurman, Fatty acid synthase correlation with cell proliferation and hormone receptors expression in endometrial carcinoma:, Cancer 83:528–537 (1998).CrossRefPubMedGoogle Scholar
  79. 79.
    J. Swinnen, F. Vanderhoydonc, A. Elgammal, et al., Selective activation of the fatty acid synthesis pathway in human prostate cancer, Intl J Cancer 88:176–179 (2000B).Google Scholar
  80. 80.
    Y. A. Yang, W. F. Han, P. J. Morin, F. J. Chrest, and E. S. Pizer, Activation of fatty acid synthesis during neoplastic transformation: role of mitogen-activated protein kinase and phosphatidylinositol 3-kinase, Exp Cell Res 279:80–90 (2002).CrossRefPubMedGoogle Scholar
  81. 81.
    J. Adamson, E. A. Morgan, C. Beesley, et al., High-level expression of cutaneous fatty acid-binding protein in prostatic carcinomas and its effect on tumorigenicity, Oncogene 22:2739–49 (2003).CrossRefPubMedGoogle Scholar
  82. 82.
    G. Velasco, D. Gómez, Pulgar, T, D. Carlin, and M. Guzmán, Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase I by phosphorylating cytoskeletal components, FEBS Lett 439:317–320 (1998A).CrossRefPubMedGoogle Scholar
  83. 83.
    G. Velasco, M. Geelen, T. Gomez del Pulgar, and M. Guzmán, Malonyl-CoAindependent acute control of hepatic carnitine palmitoyltransferase I activity: Role of Ca2+/calmodulin-dependent protein kinase II and cytoskeletal components, J Biol Chem 273:21497–21504 (1998B).CrossRefPubMedGoogle Scholar
  84. 84.
    J. Sleboda, K. Risan, O. Spydevold, and J. Bremer, Short-term regulation of carnitine palmitoyltransferase I in cultured rat hepatocytes: spontaneous inactivation and reactivation by fatty acids, Biochim Biophys Acta 1436:541–549 (1999).PubMedGoogle Scholar
  85. 85.
    M. Joaquin, J. Rosa, C. Salvado, et al., Hepatocyte growth factor and transforming growth factor beta regulate 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene expression in rat hepatocyte primary cultures, Biochem J 314:235–240 (1996).PubMedGoogle Scholar
  86. 86.
    Q. Shao, N. Arakaki, T. Ohnishi, O. Nakamura, and Y. Daikuhara, Effect of hepatocyte growth factor/scatter factor on lipogenesis in adult rat hepatocytes in primary culture, J Biochem 119:940–946 (1996).PubMedGoogle Scholar
  87. 87.
    M. Kaibori, A. Kwon, M. Oda, Y. Kamiyama, N. Kitamura, and T. Okumura, Hepatocyte growth factor stimulates synthesis of lipids and secretion of lipoproteins in rat hepatocytes, Hepatology 27:1354–1561 (1998).CrossRefPubMedGoogle Scholar
  88. 88.
    S. Presnell, M. Hooth, K. Borchert, W. Coleman, J. Grisham, and G. Smith, Establishment of a functional HGF/C-MET autocrine loop in spontaneous transformants of WB-F344 rat liver stem-like cells, Hepatology 28:1253–1259 (1998).CrossRefPubMedGoogle Scholar
  89. 89.
    M. Kaibori, A. Kwon, M. Nakagawa, et al., Stimulation of liver regeneration and function after partial hepatectomy in cirrhotic rats by continuous infusion of recombinant human hepatocyte growth factor, J Hepatol 27:381–390 (1997).CrossRefPubMedGoogle Scholar
  90. 90.
    K. Feingold, I. Staprans, R. Memon, et al., Endotoxin rapidly induces changes in lipid metabolism that produce hypertriglyceridemia: low doses stimulate hepatic triglyceride production while high doses inhibit clearance., J Lipid Res 33:1765–1776 (1992).PubMedGoogle Scholar
  91. 91.
    M. Navasa, K. Feingold, and C. Grunfeld, Effects of endotoxin and cytokines on hepatic lipid metabolism, Prog Liver Dis 15:147–170 (1997).Google Scholar
  92. 92.
    C. Magnard, R. Bachelier, A. Vincent, et al., BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains, Oncogene 21:6729–39 (2002).CrossRefPubMedGoogle Scholar
  93. 93.
    R. Chakrabarti, and E. Engleman, Interrelationships between mevalonate metabolism and the mitogenic signaling pathway in T lymphocyte proliferation., J Biol Chem 266:12216–12222 (1991).PubMedGoogle Scholar
  94. 94.
    O. Larsson, and H. Blegen, Regulatory role of mevalonate in the growth of normal and neoplastic human mammary epithelial cells, Anticancer Res 13:1075–1079 (1993).PubMedGoogle Scholar
  95. 95.
    B. Agarwal, C. Rao, S. Bhendwal, et al., Lovastatin augments sulindac-induced apoptosis in colon cancer cells and potentiates chemopreventive effects of sulindac., Gastroenterology 117:838–847 (1999).CrossRefPubMedGoogle Scholar
  96. 96.
    S. Jackowski, Coordination of membrane phospholipid synthesis with the cell cycle, J Biol Chem 269:3858–3867 (1994).PubMedGoogle Scholar
  97. 97.
    D. Hardie, D. Carting, and M. Carlson, The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell?, Annu Rev Biochem 67:821–855 (1998).CrossRefPubMedGoogle Scholar
  98. 98.
    K. Tobin, H. Steineger, S. Alberti, et al., Cross-talk between fatty acid and cholesterol metabolism mediated by liver X receptor-a, Molec Endocrinol 14:741–752 (2000).Google Scholar
  99. 99.
    J. D. Horton, J. L. Goldstein, and M. S. Brown, SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver, J Clin Invest 109:1125–31 (2002).CrossRefPubMedGoogle Scholar
  100. 100.
    S. B. Joseph, B. A. Laffitte, P. H. Patel, et al., Direct and indirect mechanisms for regulation of fatty acid synthase gene expression by liver X receptors, J Biol Chem 277:11019–25 (2002A).PubMedGoogle Scholar
  101. 101.
    M. Foretz, C. Pacot, I. Dugail, et al., ADD1/SREBP-1c is required in the activation of hepatic lipogenic gene expression by glucose, Mol Cell Biol 19:3760–8 (1999A).PubMedGoogle Scholar
  102. 102.
    M. Foretz, C. Guichard, P. Ferré, and F. Foufelle, Sterol regulatory element binding protein-1c is a major mediator of insulin action on the hepatic expression of glucokinase and lipogenesis-related genes., Proc Natl Acad Sci USA 96:12737–12742 (1999B).CrossRefPubMedGoogle Scholar
  103. 103.
    I. Shimomura, Y. Bashmakov, S. Ikemoto, J. D. Horton, M. S. Brown, and J. L. Goldstein, Insulin selectively increases SREBP-1c mRNA in the livers of rats with streptozotocin-induced diabetes, Proc Natl Acad Sci U S A 96:13656–61 (1999).CrossRefPubMedGoogle Scholar
  104. 104.
    X. Deng, L. M. Cagen, H. G. Wilcox, E. A. Park, R. Raghow, and M. B. Elam, Regulation of the rat SREBP-1c promoter in primary rat hepatocytes, Biochem Biophys Res Commun 290:256–62 (2002).CrossRefPubMedGoogle Scholar
  105. 105.
    Y. A. Yang, P. J. Morin, W. F. Han, et al., Regulation of fatty acid synthase expression in breast cancer by sterol regulatory element binding protein-1c, Exp Cell Res 282:132–7 (2003).CrossRefPubMedGoogle Scholar
  106. 106.
    J. Ou, H. Tu, B. Shan, et al., Unsaturated fatty acids inhibit transcription of the sterol regulatory element-binding protein-1c (SREBP-1c) gene by antagonizing ligand-dependent activation of the LXR, Proc Natl Acad Sci USA 98:6027–6032 (2001).CrossRefPubMedGoogle Scholar
  107. 107.
    A. Pawar, D. Botolin, D. J. Mangelsdorf, and D. B. Jump, The role of liver X receptor-alpha in the fatty acid regulation of hepatic gene expression., J Biol Chem 278:40736–40743 (2003).PubMedGoogle Scholar
  108. 108.
    A. R. Miserez, P. Y. Muller, and V. Spaniol, Indinavir inhibits sterol-regulatory element-binding protein-1c-dependent lipoprotein lipase and fatty acid synthase gene activations, Aids 16:1587–94 (2002).CrossRefPubMedGoogle Scholar
  109. 109.
    Y. Pak, M. Kanuck, D. Berrios, M. Briggs, A. Cooper, and J. Ellsworth, Activation of LDL receptor gene expression in HepG2 cells by hepatocyte growth factor, J Lipid Res 37:985–998 (1996).PubMedGoogle Scholar
  110. 110.
    G. Skouteris, and E. Georgakopoulos, Hepatocyte growth factor-induced proliferation of primary hepatocytes is mediated by activation of phosphatidylinositol 3-kinase, Biochem Biophys Res Commun 218:229–233 (1996).CrossRefPubMedGoogle Scholar
  111. 111.
    J. Papkoff, and M. Aikawa, WNT-1 and HGF regulate GSK3-beta activity and betacatenin signaling in mammary epithelial cells, Biochem Biophys Res Comm 247:851–858 (1998).CrossRefPubMedGoogle Scholar
  112. 112.
    J. Swinnen, H. Heemers, L. Deboel, F. Foufelle, W. Heyns, and G. Verhoeven, Stimulation of tumor-associated fatty acid synthase expression by growth factor activation of the sterol regulatory element-binding protein pathway, Oncogene 19:5173–5181 (2000A).CrossRefPubMedGoogle Scholar
  113. 113.
    J. Li, M. Mahmoud, W. Han, M. Ripple, and E. Pizer, Sterol regulatory elementbinding protein-1 participates in the regulation of fatty acid synthase expression in colorectal neoplasia, Exp Cell Res 261:159–165 (2000).CrossRefPubMedGoogle Scholar
  114. 114.
    B. A. Laffitte, L. C. Chao, J. Li, et al., Activation of liver X receptor improves glucose tolerance through coordinate regulation of glucose metabolism in liver and adipose tissue, Proc Natl Acad Sci U S A 100:5419–24 (2003).CrossRefPubMedGoogle Scholar
  115. 115.
    T. Ide, H. Shimano, T. Yoshikawa, et al., Cross-talk between peroxisome proliferator-activated receptor (PPAR) alpha and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. II. LXRs suppress lipid degradation gene promoters through inhibition of PPAR signaling, Mol Endocrinol 17:1255–67 (2003).CrossRefPubMedGoogle Scholar
  116. 116.
    S. Hooks, W. Santos, D. Im, C. Heise, T. Macdonald, and K. Lynch, Lysophosphatidic acid-induced mitogenesis is regulated by lipid phosphate phosphatases and is Edg-receptor independent, J Biol Chem 276:4611–4621 (2001).CrossRefPubMedGoogle Scholar
  117. 117.
    J. Chappell, J. Leitner, S. Solomon, I. Golovchenko, M. Goalstone, and B. Draznin, Effect of insulin on cell cycle progression in mcf-7 breast cancer cells. Direct and potentiating influence., J Biol Chem 276:38023–38028 (2001).CrossRefPubMedGoogle Scholar
  118. 118.
    Y. Sautin, J. Crawford, and S. Svetlov, Enhancement of survival by LPA via Erk1/Erk2 and PI 3-kinase/Akt pathways in a murine hepatocyte cell line, Am J Physiol Cell Physiol 281:C2010–C2019 (2001).PubMedGoogle Scholar
  119. 119.
    S. Ghosh, S. J, and B. R, Lipid biochemistry: functions of glycerolipids and sphingolipids in cellular signaling, FASEB J 11: 45–50 (1997).PubMedGoogle Scholar
  120. 120.
    G. A. Rutter, G. da Silva Xavier, and I. Leclercq, Roles of 5’-AMP-activated protein kinase (AMPK) in mammalian glucose homeostasis, Biochem J 375:1–16 (2003).CrossRefPubMedGoogle Scholar
  121. 121.
    H. Park, V. K. Kaushik, S. Constant, et al., Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise, J Biol Chem 277:32571–7 (2002).PubMedGoogle Scholar
  122. 122.
    T. Kawaguchi, K. Osatomi, H. Yamashita, T. Kabashima, and K. Uyeda, Mechanism for fatty acid “sparing” effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase, J Biol Chem 277:3829–3835 (2002).PubMedGoogle Scholar
  123. 123.
    J. J. Luiken, S. L. Coort, J. Willems, et al., Contraction-induced fatty acid translocase/CD36 translocation in rat cardiac myocytes is mediated through AMP-activated protein kinase signaling, Diabetes 52:1627–34 (2003).PubMedGoogle Scholar
  124. 124.
    R. Ockner, Apoptosis and liver diseases: Recent concepts of mechanisms and significance, J Gastroenterol Hepatol 16:248–260 (2001).CrossRefPubMedGoogle Scholar
  125. 125.
    Z. Dagher, N. Ruderman, K. Tornheim, and Y. Ido, Acute regulation of fatty acid oxidation and AMP-activated protein kinase in human umbilical vein endothelial cells., Circ Res 88:1276–82 (2001).PubMedGoogle Scholar
  126. 126.
    G. Steinberg, A. Bonen, and D. Dyck, Fatty acid oxidation and triacylglycerol hydrolysis are enhanced after chronic leptin treatment in rats, AJP — Endocrinol Metab 282:E593–E600 (2002).Google Scholar
  127. 127.
    Y. Minokoshi, Y. Kim, O. Peroni, et al., Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase, Nature 415:339–343 (2002).CrossRefPubMedGoogle Scholar
  128. 128.
    C. Beauloye, A. S. Marsin, L. Bertrand, et al., Insulin antagonizes AMP-activated protein kinase activation by ischemia or anoxia in rat hearts, without affecting total adenine nucleotides, FEBS Lett 505:348–52 (2001).CrossRefPubMedGoogle Scholar
  129. 129.
    L. Stryer, Biochemistry, W.H. Freeman and Co, New York (1995).Google Scholar
  130. 130.
    V. Skulachev, Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation, FEBS Lett 294:158–162 (1991).CrossRefPubMedGoogle Scholar
  131. 131.
    L. Wojtczak, and P. Schönfeld, Effect of fatty acids on energy coupling processes in mitochondria, Biochim Biophys Acta 1183:41–57 (1993).PubMedGoogle Scholar
  132. 132.
    L. Wojtczak, and M. Wieckowski, The mechanisms of fatty acid-induced proton permeability of the inner mitochondrial membrane, J Bioenerg Biomembranes 31:447–455 (1999A).Google Scholar
  133. 133.
    P. Schönfeld, M. Wiêckowski, and L. Wojtczak, Thyroid hormone-induced expression of the ADP/ATP carrier and its effect on fatty acid-induced uncoupling of oxidative phosphorylation, FEBS Lett 416:19–22 (1997A).CrossRefPubMedGoogle Scholar
  134. 134.
    P. Schönfeld, and R. Bohnensack, Fatty acid-promoted mitochondrial permeability transition by membrane depolarization and binding to the ADP/ATP carrier, FEBS Lett 420:167–170 (1997B).CrossRefPubMedGoogle Scholar
  135. 135.
    S. Mills, D. Foster, and J. Mcgarry, Interaction of malonyl-CoA and related compounds with mitochondria from different rat tissues: Relationship between ligand binding and inhibition of carnitine palmitoyltransferase I, Biochem J 214:83–91 (1983).PubMedGoogle Scholar
  136. 136.
    L. Drynan, P. Quant, and V. Zammit, Flux control exerted by mitochondrial outer membrane carnitine palmitoyltransferase over beta-oxidation, ketogenesis and tricarboxylic acid cycle activity in hepatocytes isolated from rats in different metabolic states., Biochem J 317:791–795 (1996A).PubMedGoogle Scholar
  137. 137.
    L. Drynan, P. Quant, and V. Zammit, The role of changes in the sensitivity of hepatic mitochondrial overt carnitine palmitoyltransferase in determining the onset of the ketosis of starvation in the rat., Biochem J 318:767–770 (1996B).PubMedGoogle Scholar
  138. 138.
    J. McGarry, and N. Brown, Reconstitution of purified, active and malonyl-CoAsensitive rat liver carnitine palmitoyltransferase I: relationship between membrane environment and malonyl-CoA sensitivity, Biochem J 349:179–187 (2000).CrossRefPubMedGoogle Scholar
  139. 139.
    M. Young, G. Goodwin, J. Ying, et al., Regulation of cardiac and skeletal muscle malonyl-CoA decarboxylase by fatty acids, Am J Physiol Endocrinol Metab 280:E471–E479 (2001 A).PubMedGoogle Scholar
  140. 140.
    M. L. Casanova, C. Blazquez, J. Martinez-Palacio, et al., Inhibition of skin tumor growth and angiogenesis in vivo by activation of cannabinoid receptors, J Clin Invest 111:43–50 (2003).CrossRefPubMedGoogle Scholar
  141. 141.
    G. Beutner, A. Ruck, B. Riede, and D. Brdiczka, Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore: Implication for regulation of permeability transition by the kinases., Biochim Biophys Acta 1368:7–18 (1998).PubMedGoogle Scholar
  142. 142.
    N. Zamzami, C. Brenner, I. Marzo, S. Susin, and G. Kroemer, Subcellular and submitochondrial mode of action of Bcl-2-like oncoproteins, Oncogene 16:2265–2282 (1998).PubMedGoogle Scholar
  143. 143.
    I. Marzo, C. Brenner, N. Zamzami, et al., The permeability transition pore complex: a target for apoptosis regulation by caspases and bcl-2-related proteins, J Exper Med 187:1261–1271 (1998).CrossRefGoogle Scholar
  144. 144.
    F. Fraser, R. Padovese, and V. Zammit, Distinct kinetics of carnitine palmitoyltransferase I in contact sites and outer membranes of rat liver mitochondria., J Biol Chem 276:20182–20185 (2001).PubMedGoogle Scholar
  145. 145.
    F. Fraser, C. Corstorphine, and V. Zammit, Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane., Biochem J 323:711–718 (1997).PubMedGoogle Scholar
  146. 146.
    J. Pastorino, N. Shulga, and J. Hoek, Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis, J Biol Chem 277:7610–7618 (2002).CrossRefPubMedGoogle Scholar
  147. 147.
    M. Y. Vyssokikh, and D. Brdiczka, The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis, Acta Biochim Pol 50:389–404 (2003).PubMedGoogle Scholar
  148. 148.
    G. Klug, J. Krause, A. Ostlund, G. Knoll, and D. Brdiczka, Alterations in liver mitochondrial function as a result of fasting and exhaustive exercise, Biochim Biophys Acta 764:272–282 (1984).PubMedGoogle Scholar
  149. 149.
    M. Diaz-Guerra, M. Junco, and L. Bosca, Oleic acid promotes changes in the subcellular distribution of protein kinase C in isolated hepatocytes., J Biol Chem 266:23568–23576 (1991).PubMedGoogle Scholar
  150. 150.
    Y. Nishizuka, Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C, Science 258:607–614 (1992).PubMedGoogle Scholar
  151. 151.
    E. Dempsey, A. Newton, D. Mochly-Rosen, et al., Protein kinase C isozymes and the regulation of diverse cell responses., Am J Physiol Lung Cell Mol Physiol 279:L429–L438 (2000).PubMedGoogle Scholar
  152. 152.
    L. Braun, J. Mead, M. Panzica, R. Mikumo, G. Bell, and N. Fausto, Transforming growth factor beta mRNA increases during liver regeneration: a possible paracrine mechanism of growth regulation., Proc Natl Acad Sci USA 85:1539–1543 (1988).PubMedGoogle Scholar
  153. 153.
    D. Bissell, S. Wang, W. Jarnagin, and F. Roll, Cell-specific expression of transforming growth factor-beta in rat liver: Evidence for autocrine regulation of hepatocyte proliferation., J Clin Invest 96:447–455 (1995).PubMedGoogle Scholar
  154. 154.
    M. Macias-Silva, W. Li, J. I. Leu, M. A. Crissey, and R. Taub, Up-regulated transcriptional repressors SnoN and Ski bind Smad proteins to antagonize transforming growth factor-beta signals during liver regeneration, J Biol Chem 277:28483–90 (2002).CrossRefPubMedGoogle Scholar
  155. 155.
    T. Fynan, and M. Reiss, Resistance to inhibition of cell growth by transforming growth factor-beta and its role in oncogenesis., Crit Rev Oncog 4:493–540 (1993).PubMedGoogle Scholar
  156. 156.
    H. Tsushima, S. Kawata, S. Tamura, et al., High levels of transforming growth factor beta1 in patients with colorectal cancer: Association with disease progression, Gastroenterology 110:375–382 (1996).CrossRefPubMedGoogle Scholar
  157. 157.
    J. McCormack, and R. Denton, The role of intramitochondrial Ca2+ in the regulation of oxidative phosphorylation in mammalian tissues, Biochem Soc Trans 21:793–799 (1993).PubMedGoogle Scholar
  158. 158.
    D. Toomey, H. Redmond, and D. Bouchier-Hayes, Mechanisms mediating cancer cachexia, Cancer 76:2418–2426 (1995).PubMedGoogle Scholar
  159. 159.
    D. Gough, S. Heys, and O. Eremin, Cancer cachexiaa; pathophysiological mechanisms, Eur J Surg Oncol 22:192–196 (1996).PubMedGoogle Scholar
  160. 160.
    J. Argilés, and F. López-Soriano, Cancer cachexia. A key role for TNF? (Review), Intl J Oncol 10:565–572 (1997).Google Scholar
  161. 161.
    M. J. Tisdale, Wasting in cancer, J Nutr 129:243S–246S (1999).PubMedGoogle Scholar
  162. 162.
    L. Sánchez, A. Chirino, and P. Bjorkman, Crystal structure of human ZAG, a fatdepleting factor related to MHC molecules, Science 283:1914–1919 (1999).PubMedGoogle Scholar
  163. 163.
    S. Wigmore, P. Todorov, M. Barber, J. Ross, M. Tisdale, and K. Fearon, Characteristics of patients with pancreatic cancer expressing a novel cancer cachectic factor, Br J Surg 87:53–58 (2000).CrossRefPubMedGoogle Scholar
  164. 164.
    H. Smith, and M. Tisdale, Induction of apoptosis by a cachectic-factor in murine myotubes and inhibition by eicosapentaenoic acid., Apoptosis 8:161–169 (2003).CrossRefPubMedGoogle Scholar
  165. 165.
    K. Fearon, M. von Meyenfeldt, A. Moses, et al., Effect of a protein and energy dense n-3 fatty acid enriched oral supplement on loss of weight and lean tissue in cancer cachexia: a randomised double blind trial., Gut 52:1479–1486 (2003).CrossRefPubMedGoogle Scholar
  166. 166.
    L. Levin, and W. Gevers, Metabolic alterations in cancer. Part I: Carbohydrate metabolism, S Afr Med J 59:518–521 (1981A).PubMedGoogle Scholar
  167. 167.
    L. Levin, and W. Gevers, Metabolic alterations in cancer, Part II: Protein and fat metabolism, S Afr Med J 59:553–556 (1981B).PubMedGoogle Scholar
  168. 168.
    K. Bennegard, F. Lundgren, and K. Lundholm, Mechanisms of insulin resistance in cancer associated malnutrition., Clin Physiol 6:539–547 (1986).PubMedGoogle Scholar
  169. 169.
    J. Tayek, A review of cancer cachexia and abnormal glucose metabolism in humans with cancer, J Am Coll Nutr 4:445–456 (1992).Google Scholar
  170. 170.
    A. Rofe, C. Bourgeois, P. Coyle, A. Taylor, and E. Abdi, Altered insulin response to glucose in weight-losing cancer patients, Anticancer Res 14:647–650 (1994).PubMedGoogle Scholar
  171. 171.
    K. Smith, and M. Tisdale, Increased protein degradation and decreased protein synthesis in skeletal muscle during cancer cachexia, Br J Cancer 67:680–685 (1993).PubMedGoogle Scholar
  172. 172.
    K. Lundholm, S. Edstrom, I. Karlberg, L. Ekman, and T. Schersten, Glucose turnover, gluconeogenesis from glycerol, and estimation of net glucose cycling in cancer patients, Cancer 50:1142–1150 (1982).PubMedGoogle Scholar
  173. 173.
    G. Hotamisligil, Mechanisms of TNF-alpha-induced insulin resistance, Exp Clin Endocrinol Diabetes 107:119–125 (1999).PubMedGoogle Scholar
  174. 174.
    X. Chen, N. Iqbal, and G. Boden, The effects of free fatty acids on gluconeogenesis and glycogenolysis in normal subjects., J Clin Invest 103:365–372 (1999).PubMedGoogle Scholar
  175. 175.
    A. Dresner, D. Laurent, M. Marcucci, et al., Effects of free fatty acids on glucose transport and IRS-1-associated phosphatidylinositol 3-kinase activity., J Clin Invest 103:253–259 (1999).PubMedGoogle Scholar
  176. 176.
    M. E. Griffin, M. J. Marcucci, G. W. Cline, et al., Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade, Diabetes 48:1270–4 (1999).PubMedGoogle Scholar
  177. 177.
    P. Arner, Insulin resistance in type 2 diabetes: role of fatty acids, Diabetes Metab Res Rev 18Suppl 2:S5–9 (2002).PubMedGoogle Scholar
  178. 178.
    G. Boden, and G. I. Shulman, Free fatty acids in obesity and type 2 diabetes: defining their role in the development of insulin resistance and beta-cell dysfunction, Eur J Clin Invest 32Suppl 3:14–23 (2002).PubMedGoogle Scholar
  179. 179.
    T. K. Lam, H. Yoshii, C. A. Haber, et al., Free fatty acid-induced hepatic insulin resistance: a potential role for protein kinase C-delta, Am J Physiol Endocrinol Metab 283:E682–91 (2002).PubMedGoogle Scholar
  180. 180.
    C. L. Soltys, L. Buchholz, M. Gandhi, A. S. Clanachan, K. Walsh, and J. R. Dyck, Phosphorylation of cardiac protein kinase B is regulated by palmitate, Am J Physiol Heart Circ Physiol 283:H1056–64 (2002).PubMedGoogle Scholar
  181. 181.
    C. Yu, Y. Chen, G. W. Cline, et al., Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activity in muscle, J Biol Chem 277:50230–50236 (2002).PubMedGoogle Scholar
  182. 182.
    R. Eastman, R. Carson, D. Orloff, et al., Glucose utilization in a patient with hepatoma and hypoglycemia: Assessment by a positron emission tomography., J Clin Invest 89:1958–1963 (1992).PubMedGoogle Scholar
  183. 183.
    D. Le Roith, Insulin-like growth factors, New Engl J Med 336:663–640 (1997).Google Scholar
  184. 184.
    R. Behal, D. Buxton, J. Robertson, and M. Olson, Regulation of the pyruvate dehydrogenase multienzyme complex., Annu Rev Nutr 13:497–520 (1993).CrossRefPubMedGoogle Scholar
  185. 185.
    R. Scholz, M. Olson, A. Schwab, U. Schwabe, C. Noell, and W. Braun, The effect of fatty acids on the regulation of pyruvate dehydrogenase in perfused rat liver, Eur J Biochem 86:519–530 (1978).CrossRefPubMedGoogle Scholar
  186. 186.
    K. Cusi, K. Maezono, A. Osman, et al., Insulin resistance differentially affects the PI 3-kinase-and MAP kinase-mediated signaling in human muscle., J Clin Invest 105:311–320 (2000).PubMedGoogle Scholar
  187. 187.
    Y. Kruszynska, D. Worrall, J. Ofrecio, J. Frias, G. Macaraeg, and J. Olefsky, Fatty acid-induced insulin resistance: decreased muscle PI3K activation but unchanged Akt phosphorylation, J Clin Endocrinol Metab 87:226–234 (2002).CrossRefPubMedGoogle Scholar
  188. 188.
    M. Brauer, R. Inculet, G. Bhatnagar, G. Marsh, A. Driedger, and R. Thompson, Insulin protects against hepatic bioenergetic deterioration induced by cancer cachexia: an in vivo 31P magnetic resonance spectroscopy study., Cancer Res 54:6383–6386 (1994).PubMedGoogle Scholar
  189. 189.
    A. Tsuburaya, D. Blumberg, M. Burt, and M. Brennan, Energy depletion in the liver and in isolated hepatocytes of tumor-bearing animals, J Surg Res 59:421–427 (1995).CrossRefPubMedGoogle Scholar

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