Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2015 (2015), Article ID 274585, 17 pages
http://dx.doi.org/10.1155/2015/274585
Review Article

Obesity and Cancer Progression: Is There a Role of Fatty Acid Metabolism?

1Discipline of Physiology, School of Medical Sciences and Bosch Institute, The University of Sydney, Sydney, NSW 2006, Australia
2Charles Perkins Centre, The University of Sydney, Sydney, NSW 2006, Australia
3Boden Institute of Obesity, Nutrition, Exercise & Eating Disorders, The University of Sydney, Sydney, NSW 2006, Australia

Received 30 July 2014; Accepted 24 November 2014

Academic Editor: James McManaman

Copyright © 2015 Seher Balaban et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. S. M. Grundy, “Obesity, metabolic syndrome, and cardiovascular disease,” Journal of Clinical Endocrinology and Metabolism, vol. 89, no. 6, pp. 2595–2600, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. S. M. Louie, L. S. Roberts, and D. K. Nomura, “Mechanisms linking obesity and cancer,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1831, no. 10, pp. 1499–1508, 2013. View at Publisher · View at Google Scholar · View at Scopus
  3. K. Y. Wolin, K. Carson, and G. A. Colditz, “Obesity and cancer,” Oncologist, vol. 15, no. 6, pp. 556–565, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. G. de Pergola and F. Silvestris, “Obesity as a major risk factor for cancer,” Journal of Obesity, vol. 2013, Article ID 291546, 11 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  5. W. C. Buschemeyer III and S. J. Freedland, “Obesity and prostate cancer: epidemiology and clinical implications,” European Urology, vol. 52, no. 2, pp. 331–343, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. B. Majed, T. Moreau, K. Senouci, R. J. Salmon, A. Fourquet, and B. Asselain, “Is obesity an independent prognosis factor in woman breast cancer?” Breast Cancer Research and Treatment, vol. 111, no. 2, pp. 329–342, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. Y. Zhu, H.-K. Wang, H.-L. Zhang et al., “Visceral obesity and risk of high grade disease in clinical T1a renal cell carcinoma,” The Journal of Urology, vol. 189, no. 2, pp. 447–453, 2013. View at Publisher · View at Google Scholar · View at Scopus
  8. A. Ansary-Moghaddam, R. Huxley, F. Barzi et al., “The effect of modifiable risk factors on pancreatic cancer mortality in populations of the Asia-Pacific region,” Cancer Epidemiology Biomarkers and Prevention, vol. 15, no. 12, pp. 2435–2440, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. C. A. Gilbert and J. M. Slingerland, “Cytokines, obesity, and cancer: new insights on mechanisms linking obesity to cancer risk and progression,” Annual Review of Medicine, vol. 64, pp. 45–57, 2013. View at Publisher · View at Google Scholar · View at Scopus
  10. J. K. Sethi and A. J. Vidal-Puig, “Thematic review series: adipocyte Biology. Adipose tissue function and plasticity orchestrate nutritional adaptation,” Journal of Lipid Research, vol. 48, no. 6, pp. 1253–1262, 2007. View at Publisher · View at Google Scholar · View at Scopus
  11. D. Samocha-Bonet, D. J. Chisholm, K. Tonks, L. V. Campbell, and J. R. Greenfield, “Insulin-sensitive obesity in humans—a “favorable fat” phenotype?” Trends in Endocrinology & Metabolism, vol. 23, no. 3, pp. 116–124, 2012. View at Publisher · View at Google Scholar · View at Scopus
  12. N. Ruderman, D. Chisholm, X. Pi-Sunyer, and S. Schneider, “The metabolically obese, normal-weight individual revisited,” Diabetes, vol. 47, no. 5, pp. 699–713, 1998. View at Publisher · View at Google Scholar · View at Scopus
  13. R. Kelishadi, S. R. Cook, M. E. Motlagh et al., “Metabolically obese normal weight and phenotypically obese metabolically normal youths: the CASPIAN Study,” Journal of the American Dietetic Association, vol. 108, no. 1, pp. 82–90, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. T. Nolis, “Exploring the pathophysiology behind the more common genetic and acquired lipodystrophies,” Journal of Human Genetics, vol. 59, no. 1, pp. 16–23, 2014. View at Publisher · View at Google Scholar · View at Scopus
  15. J. Capeau, J. Magré, M. Caron-Debarle et al., “Human lipodystrophies: genetic and acquired diseases of adipose tissue,” Endocrine Development, vol. 19, pp. 1–20, 2010. View at Publisher · View at Google Scholar · View at Scopus
  16. M. J. Khandekar, P. Cohen, and B. M. Spiegelman, “Molecular mechanisms of cancer development in obesity,” Nature Reviews Cancer, vol. 11, no. 12, pp. 886–895, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Narita, N. Tsuchiya, L. Wang et al., “Association of lipoprotein lipase gene polymorphism with risk of prostate cancer in a Japanese population,” International Journal of Cancer, vol. 112, no. 5, pp. 872–876, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. J. C. Carter and F. C. Church, “Mature breast adipocytes promote breast cancer cell motility,” Experimental and Molecular Pathology, vol. 92, no. 3, pp. 312–317, 2012. View at Publisher · View at Google Scholar · View at Scopus
  19. K. Sakayama, H. Masuno, T. Miyazaki, H. Okumura, T. Shibata, and H. Okuda, “Existence of lipoprotein lipase in human sarcomas and carcinomas,” Japanese Journal of Cancer Research, vol. 85, no. 5, pp. 515–521, 1994. View at Publisher · View at Google Scholar · View at Scopus
  20. D. Cerne, I. P. Zitnik, and M. Sok, “Increased fatty acid synthase activity in non-small cell lung cancer tissue is a weaker predictor of shorter patient survival than increased lipoprotein lipase activity,” Archives of Medical Research, vol. 41, no. 6, pp. 405–409, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. Z. Trost, M. Sok, J. Marc, and D. Cerne, “Increased lipoprotein lipase activity in non-small cell lung cancer tissue predicts shorter patient survival,” Archives of Medical Research, vol. 40, no. 5, pp. 364–368, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. S. M. Rachidi, T. Qin, S. Sun, W. J. Zheng, and Z. Li, “Molecular profiling of multiple human cancers defines an inflammatory cancer-associated molecular pattern and uncovers KPNA2 as a uniform poor prognostic cancer marker,” PLoS ONE, vol. 8, no. 3, Article ID e57911, 2013. View at Publisher · View at Google Scholar · View at Scopus
  23. I. P. Uray, Y. Liang, and S. M. Hyder, “Estradiol down-regulates CD36 expression in human breast cancer cells,” Cancer Letters, vol. 207, no. 1, pp. 101–107, 2004. View at Publisher · View at Google Scholar · View at Scopus
  24. D. E. Blask, L. A. Sauer, R. T. Dauchy, E. W. Holowachuk, M. S. Ruhoff, and H. S. Kopff, “Melatonin inhibition of cancer growth in vivo involves suppression of tumor fatty acid metabolism via melatonin receptor-mediated signal transduction events,” Cancer Research, vol. 59, no. 18, pp. 4693–4701, 1999. View at Google Scholar · View at Scopus
  25. R. Hammamieh, N. Chakraborty, M. Barmada, R. Das, and M. Jett, “Expression patterns of fatty acid binding proteins in breast cancer cells,” Journal of Experimental Therapeutics and Oncology, vol. 5, no. 2, pp. 133–143, 2005. View at Google Scholar · View at Scopus
  26. A. Tölle, S. Suhail, M. Jung, K. Jung, and C. Stephan, “Fatty acid binding proteins (FABPs) in prostate, bladder and kidney cancer cell lines and the use of IL-FABP as survival predictor in patients with renal cell carcinoma,” BMC cancer, vol. 11, article 302, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. J. E. Celis, M. Østergaard, B. Basse et al., “Loss of adipocyte-type fatty acid binding protein and other protein biomarkers is associated with progression of human bladder transitional cell carcinomas,” Cancer Research, vol. 56, no. 20, pp. 4782–4790, 1996. View at Google Scholar · View at Scopus
  28. G. Ohlsson, J. M. A. Moreira, P. Gromov, G. Sauter, and J. E. Celis, “Loss of expression of the adipocyte-type fatty acid-binding protein (A-FABP) is associated with progression of human urothelial carcinomas,” Molecular & Cellular Proteomics, vol. 4, no. 4, pp. 570–581, 2005. View at Publisher · View at Google Scholar · View at Scopus
  29. P. J. Wild, A. Herr, C. Wissmann et al., “Gene expression profiling of progressive papillary noninvasive carcinomas of the urinary bladder,” Clinical Cancer Research, vol. 11, no. 12, pp. 4415–4429, 2005. View at Publisher · View at Google Scholar · View at Scopus
  30. M. K. Herroon, E. Rajagurubandara, A. L. Hardaway et al., “Bone marrow adipocytes promote tumor growth in bone via FABP4-dependent mechanisms,” Oncotarget, vol. 4, no. 11, pp. 2108–2123, 2013. View at Google Scholar · View at Scopus
  31. K. M. Nieman, H. A. Kenny, C. V. Penicka et al., “Adipocytes promote ovarian cancer metastasis and provide energy for rapid tumor growth,” Nature Medicine, vol. 17, no. 11, pp. 1498–1503, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. C. Jing, C. Beesley, C. S. Foster et al., “Identification of the messenger RNA for human cutaneous fatty acid-binding protein as a metastasis inducer,” Cancer Research, vol. 60, no. 9, pp. 2390–2398, 2000. View at Google Scholar · View at Scopus
  33. R.-Z. Liu, K. Graham, D. D. Glubrecht, D. R. Germain, J. R. Mackey, and R. Godbout, “Association of FABP5 expression with poor survival in triple-negative breast cancer: implication for retinoic acid therapy,” The American Journal of Pathology, vol. 178, no. 3, pp. 997–1008, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. Z. Li, C. Huang, S. Bai et al., “Prognostic evaluation of epidermal fatty acid-binding protein and calcyphosine, two proteins implicated in endometrial cancer using a proteomic approach,” International Journal of Cancer, vol. 123, no. 10, pp. 2377–2383, 2008. View at Publisher · View at Google Scholar · View at Scopus
  35. K. Fujii, T. Kondo, H. Yokoo, T. Yamada, K. Iwatsuki, and S. Hirohashi, “Proteomic study of human hepatocellular carcinoma using two-dimensional difference gel electrophoresis with saturation cysteine dye,” Proteomics, vol. 5, no. 5, pp. 1411–1422, 2005. View at Publisher · View at Google Scholar · View at Scopus
  36. P. Sinha, G. Hütter, E. Köttgen, M. Dietel, D. Schadendorf, and H. Lage, “Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-sigma (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas,” Electrophoresis, vol. 20, no. 14, pp. 2952–2960, 1999. View at Google Scholar
  37. Z. Bao, M. I. Malki, S. S. Forootan et al., “A novel cutaneous Fatty Acid-binding protein-related signaling pathway leading to malignant progression in prostate cancer cells,” Genes and Cancer, vol. 4, no. 7-8, pp. 297–314, 2013. View at Publisher · View at Google Scholar · View at Scopus
  38. R. Das, R. Hammamieh, R. Neill, M. Melhem, and M. Jett, “Expression pattern of fatty acid-binding proteins in human normal and cancer prostate cells and tissues,” Clinical Cancer Research, vol. 7, no. 6, pp. 1706–1715, 2001. View at Google Scholar · View at Scopus
  39. 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, vol. 22, no. 18, pp. 2739–2749, 2003. View at Publisher · View at Google Scholar · View at Scopus
  40. X. Y. Tang, S. Umemura, H. Tsukamoto, N. Kumaki, Y. Tokuda, and R. Y. Osamura, “Overexpression of fatty acid binding protein-7 correlates with basal-like subtype of breast cancer,” Pathology Research and Practice, vol. 206, no. 2, pp. 98–101, 2010. View at Publisher · View at Google Scholar · View at Scopus
  41. H. Zhang, E. A. Rakha, G. R. Ball et al., “The proteins FABP7 and OATP2 are associated with the basal phenotype and patient outcome in human breast cancer,” Breast Cancer Research and Treatment, vol. 121, no. 1, pp. 41–51, 2010. View at Publisher · View at Google Scholar · View at Scopus
  42. A. T. Alshareeda, E. A. Rakha, C. C. Nolan, I. O. Ellis, and A. R. Green, “Fatty acid binding protein 7 expression and its sub-cellular localization in breast cancer,” Breast Cancer Research and Treatment, vol. 134, no. 2, pp. 519–529, 2012. View at Publisher · View at Google Scholar · View at Scopus
  43. Y. Goto, K. Koyanagi, N. Narita et al., “Aberrant fatty acid-binding protein-7 gene expression in cutaneous malignant melanoma,” Journal of Investigative Dermatology, vol. 130, no. 1, pp. 221–229, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. C. Tan, T. Takayama, N. Takaoka et al., “Impact of gender in renal cell carcinoma: the relationship of FABP7 and BRN2 expression with overall survival,” Clinical Medicine Insights: Oncology, vol. 8, pp. 21–27, 2014. View at Publisher · View at Google Scholar · View at Scopus
  45. T. Teratani, T. Domoto, K. Kuriki et al., “Detection of transcript for brain-type fatty acid-binding protein in tumor and urine of patients with renal cell carcinoma,” Urology, vol. 69, no. 2, pp. 236–240, 2007. View at Publisher · View at Google Scholar · View at Scopus
  46. Z. Pei, P. Sun, P. Huang, B. Lal, J. Laterra, and P. A. Watkins, “Acyl-CoA synthetase VL3 knockdown inhibits human glioma cell proliferation and tumorigenicity,” Cancer Research, vol. 69, no. 24, pp. 9175–9182, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. Y. Cao, K. B. Dave, T. P. Doan, and S. M. Prescott, “Fatty acid CoA ligase 4 is up-regulated in colon adenocarcinoma,” Cancer Research, vol. 61, no. 23, pp. 8429–8434, 2001. View at Google Scholar · View at Scopus
  48. Y.-C. Liang, C.-H. Wu, J.-S. Chu et al., “Involvement of fatty acid-CoA ligase 4 in hepatocellular carcinoma growth: roles of cyclic AMP and p38 mitogen-activated protein kinase,” World Journal of Gastroenterology, vol. 11, no. 17, pp. 2557–2563, 2005. View at Google Scholar · View at Scopus
  49. C.-S. Yeh, J.-Y. Wang, T.-L. Cheng, C.-H. Juan, C.-H. Wu, and S.-R. Lin, “Fatty acid metabolism pathway play an important role in carcinogenesis of human colorectal cancers by Microarray-Bioinformatics analysis,” Cancer Letters, vol. 233, no. 2, pp. 297–308, 2006. View at Publisher · View at Google Scholar · View at Scopus
  50. C. S. M. Diefenbach, R. A. Soslow, A. Iasonos et al., “Lysophosphatidic acid acyltransferase-β (LPAAT-β) is highly expressed in advanced ovarian cancer and is associated with aggressive histology and poor survival,” Cancer, vol. 107, no. 7, pp. 1511–1519, 2006. View at Publisher · View at Google Scholar · View at Scopus
  51. S. Niesporek, C. Denkert, W. Weichert et al., “Expression of lysophosphatidic acid acyltransferase beta (LPAAT-beta) in ovarian carcinoma: correlation with tumour grading and prognosis,” British Journal of Cancer, vol. 92, no. 9, pp. 1729–1736, 2005. View at Publisher · View at Google Scholar · View at Scopus
  52. G. M. Springett, L. Bonham, A. Hummer et al., “Lysophosphatidic acid acyltransferase-beta is a prognostic marker and therapeutic target in gynecologic malignancies,” Cancer Research, vol. 65, no. 20, pp. 9415–9425, 2005. View at Google Scholar
  53. A. K. Agarwal and A. Garg, “Enzymatic activity of the human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 11: upregulated in breast and cervical cancers,” Journal of Lipid Research, vol. 51, no. 8, pp. 2143–2152, 2010. View at Publisher · View at Google Scholar · View at Scopus
  54. F. Mansilla, K.-A. Da Costa, S. Wang et al., “Lysophosphatidylcholine acyltransferase 1 (LPCAT1) overexpression in human colorectal cancer,” Journal of Molecular Medicine, vol. 87, no. 1, pp. 85–97, 2009. View at Publisher · View at Google Scholar · View at Scopus
  55. T. Agustsson, M. Rydén, J. Hoffstedt et al., “Mechanism of increased lipolysis in cancer cachexia,” Cancer Research, vol. 67, no. 11, pp. 5531–5537, 2007. View at Publisher · View at Google Scholar · View at Scopus
  56. S. K. Das, S. Eder, S. Schauer et al., “Adipose triglyceride lipase contributes to cancer-associated cachexia,” Science, vol. 333, no. 6039, pp. 233–238, 2011. View at Publisher · View at Google Scholar · View at Scopus
  57. M. P. Thompson, S. T. Cooper, B. R. Parry, and J. A. Tuckey, “Increased expression of the mRNA for hormone-sensitive lipase in adipose tissue of cancer patients,” Biochimica et Biophysica Acta, vol. 1180, no. 3, pp. 236–242, 1993. View at Publisher · View at Google Scholar · View at Scopus
  58. L. Ye, B. Zhang, E. G. Seviour et al., “Monoacylglycerol lipase (MAGL) knockdown inhibits tumor cells growth in colorectal cancer,” Cancer Letters, vol. 307, no. 1, pp. 6–17, 2011. View at Publisher · View at Google Scholar · View at Scopus
  59. D. K. Nomura, D. P. Lombardi, J. W. Chang et al., “Monoacylglycerol lipase exerts dual control over endocannabinoid and fatty acid pathways to support prostate cancer,” Chemistry and Biology, vol. 18, no. 7, pp. 846–856, 2011. View at Publisher · View at Google Scholar · View at Scopus
  60. K. Linher-Melville, S. Zantinge, T. Sanli, H. Gerstein, T. Tsakiridis, and G. Singh, “Establishing a relationship between prolactin and altered fatty acid β-oxidation via carnitine palmitoyl transferase 1 in breast cancer cells,” BMC Cancer, vol. 11, article 56, 2011. View at Publisher · View at Google Scholar · View at Scopus
  61. A. Cirillo, A. Di Salle, O. Petillo et al., “High grade glioblastoma is associated with aberrant expression of ZFP57, a protein involved in gene imprinting, and of CPT1A and CPT1C that regulate fatty acid metabolism,” Cancer Biology and Therapy, vol. 15, no. 6, pp. 735–741, 2014. View at Publisher · View at Google Scholar · View at Scopus
  62. K. Zaugg, Y. Yao, P. T. Reilly et al., “Carnitine palmitoyltransferase 1C promotes cell survival and tumor growth under conditions of metabolic stress,” Genes & Development, vol. 25, no. 10, pp. 1041–1051, 2011. View at Publisher · View at Google Scholar · View at Scopus
  63. L. Z. Milgraum, L. A. Witters, G. R. Pasternack, and F. P. Kuhajda, “Enzymes of the fatty acid synthesis pathway are highly expressed in in situ breast carcinoma,” Clinical Cancer Research, vol. 3, no. 11, pp. 2115–2120, 1997. View at Google Scholar · View at Scopus
  64. J. T. Moncur, J. P. Park, V. A. Memoli, T. K. Mohandas, and W. B. Kinlaw, “The “Spot 14” gene resides on the telomeric end of the 11q13 amplicon and is expressed in lipogenic breast cancers: implications for control of tumor metabolism,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 12, pp. 6989–6994, 1998. View at Publisher · View at Google Scholar · View at Scopus
  65. J. V. Swinnen, F. Vanderhoydonc, A. A. Elgamal et al., “Selective activation of the fatty acid synthesis pathway in human prostate cancer,” International Journal of Cancer, vol. 88, no. 2, pp. 176–179, 2000. View at Google Scholar
  66. E. Conde, A. Suarez-Gauthier, E. García-García et al., “Specific pattern of LKB1 and phospho-acetyl-CoA carboxylase protein immunostaining in human normal tissues and lung carcinomas,” Human Pathology, vol. 38, no. 9, pp. 1351–1360, 2007. View at Publisher · View at Google Scholar · View at Scopus
  67. N. Yahagi, H. Shimano, K. Hasegawa et al., “Co-ordinate activation of lipogenic enzymes in hepatocellular carcinoma,” European Journal of Cancer, vol. 41, no. 9, pp. 1316–1322, 2005. View at Publisher · View at Google Scholar · View at Scopus
  68. H. Wong and M. C. Schotz, “The lipase gene family,” Journal of Lipid Research, vol. 43, no. 7, pp. 993–999, 2002. View at Publisher · View at Google Scholar · View at Scopus
  69. H. Podgornik, M. Sok, I. Kern, J. Marc, and D. Cerne, “Lipoprotein lipase in non-small cell lung cancer tissue is highly expressed in a subpopulation of tumor-associated macrophages,” Pathology—Research and Practice, vol. 209, no. 8, pp. 516–520, 2013. View at Publisher · View at Google Scholar · View at Scopus
  70. S. Kersten, “Physiological regulation of lipoprotein lipase,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1841, no. 7, pp. 919–933, 2014. View at Publisher · View at Google Scholar · View at Scopus
  71. J. F. F. Brinkmann, N. A. Abumrad, A. Ibrahimi, G. J. Van der Vusse, and J. F. C. Glatz, “New insights into long-chain fatty acid uptake by heart muscle: a crucial role for fatty acid translocase/CD36,” Biochemical Journal, vol. 367, no. 3, pp. 561–570, 2002. View at Publisher · View at Google Scholar · View at Scopus
  72. A. Bonen, A. Chabowski, J. J. F. P. Luiken, and J. F. C. Glatz, “Is membrane transport of FFA mediated by lipid, protein, or both? Mechanisms and regulation of protein-mediated cellular fatty acid uptake: molecular, biochemical, and physiological evidence,” Physiology, vol. 22, pp. 15–29, 2007. View at Google Scholar · View at Scopus
  73. D. Hirsch, A. Stahl, and H. F. Lodish, “A family of fatty acid transporters conserved from mycobacterium to man,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 15, pp. 8625–8629, 1998. View at Publisher · View at Google Scholar · View at Scopus
  74. J. G. Nickerson, H. Alkhateeb, C. R. Benton et al., “Greater transport efficiencies of the membrane fatty acid transporters FAT/CD36 and FATP4 compared with FABPpm and FATP1 and differential effects on fatty acid esterification and oxidation in rat skeletal muscle,” The Journal of Biological Chemistry, vol. 284, no. 24, pp. 16522–16530, 2009. View at Publisher · View at Google Scholar · View at Scopus
  75. Q. Wu, A. M. Ortegon, B. Tsang, H. Doege, K. R. Feingold, and A. Stahl, “FATP1 is an insulin-sensitive fatty acid transporter involved in diet-induced obesity,” Molecular and Cellular Biology, vol. 26, no. 9, pp. 3455–3467, 2006. View at Publisher · View at Google Scholar · View at Scopus
  76. L. Love-Gregory and N. A. Abumrad, “CD36 genetics and the metabolic complications of obesity,” Current Opinion in Clinical Nutrition and Metabolic Care, vol. 14, no. 6, pp. 527–534, 2011. View at Publisher · View at Google Scholar · View at Scopus
  77. A. S. Asch, J. Barnwell, R. L. Silverstein, and R. L. Nachman, “Isolation of the thrombospondin membrane receptor,” The Journal of Clinical Investigation, vol. 79, no. 4, pp. 1054–1061, 1987. View at Publisher · View at Google Scholar · View at Scopus
  78. N. N. Tandon, U. Kralisz, and G. A. Jamieson, “Identification of glycoprotein IV (CD36) as a primary receptor for platelet-collagen adhesion,” The Journal of Biological Chemistry, vol. 264, no. 13, pp. 7576–7583, 1989. View at Google Scholar · View at Scopus
  79. G. Endemann, L. W. Stanton, K. S. Madden, C. M. Bryant, R. T. White, and A. A. Protter, “CD36 is a receptor for oxidized low density lipoprotein,” The Journal of Biological Chemistry, vol. 268, no. 16, pp. 11811–11816, 1993. View at Google Scholar · View at Scopus
  80. A. G. S. Baillie, C. T. Coburn, and N. A. Abumrad, “Reversible binding of long-chain fatty acids to purified FAT, the adipose CD36 homolog,” The Journal of Membrane Biology, vol. 153, no. 1, pp. 75–81, 1996. View at Publisher · View at Google Scholar · View at Scopus
  81. D. M. Muoio, G. L. Dohm, E. B. Tapscott, and R. A. Coleman, “Leptin opposes insulin's effects on fatty acid partitioning in muscles isolated from obese ob/ob mice,” The American Journal of Physiology—Endocrinology and Metabolism, vol. 276, no. 5, part 1, pp. E913–E921, 1999. View at Google Scholar · View at Scopus
  82. J. F. C. Glatz, A. Bonen, and J. J. F. P. Luiken, “Exercise and insulin increase muscle fatty acid uptake by recruiting putative fatty acid transporters to the sarcolemma,” Current Opinion in Clinical Nutrition and Metabolic Care, vol. 5, no. 4, pp. 365–370, 2002. View at Publisher · View at Google Scholar · View at Scopus
  83. X. Buqué, M. J. Martínez, A. Cano et al., “A subset of dysregulated metabolic and survival genes is associated with severity of hepatic steatosis in obese Zucker rats,” Journal of Lipid Research, vol. 51, no. 3, pp. 500–513, 2010. View at Publisher · View at Google Scholar · View at Scopus
  84. A. Bonen, C. R. Benton, S. E. Campbell et al., “Plasmalemmal fatty acid transport is regulated in heart and skeletal muscle by contraction, insulin and leptin, and in obesity and diabetes,” Acta Physiologica Scandinavica, vol. 178, no. 4, pp. 347–356, 2003. View at Publisher · View at Google Scholar · View at Scopus
  85. J. Smith, X. Su, R. El-Maghrabi, P. D. Stahl, and N. A. Abumrad, “Opposite regulation of CD36 ubiquitination by fatty acids and insulin: effects on fatty acid uptake,” The Journal of Biological Chemistry, vol. 283, no. 20, pp. 13578–13585, 2008. View at Publisher · View at Google Scholar · View at Scopus
  86. Y. Angin, L. K. M. Steinbusch, P. J. Simons et al., “CD36 inhibition prevents lipid accumulation and contractile dysfunction in rat cardiomyocytes,” Biochemical Journal, vol. 448, no. 1, pp. 43–53, 2012. View at Publisher · View at Google Scholar · View at Scopus
  87. A. Chabowski, S. L. M. Coort, J. Calles-Escandon et al., “Insulin stimulates fatty acid transport by regulating expression of FAT/CD36 but not FABPpm,” American Journal of Physiology: Endocrinology and Metabolism, vol. 287, no. 4, pp. E781–E789, 2004. View at Publisher · View at Google Scholar · View at Scopus
  88. N. J. Bryant, R. Govers, and D. E. James, “Regulated transport of the glucose transporter GLUT4,” Nature Reviews Molecular Cell Biology, vol. 3, no. 4, pp. 267–277, 2002. View at Publisher · View at Google Scholar · View at Scopus
  89. J. W. Slot, H. J. Geuze, S. Gigengack, D. E. James, and G. E. Lienhard, “Translocation of the glucose transporter GLUT4 in cardiac myocytes of the rat,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 17, pp. 7815–7819, 1991. View at Publisher · View at Google Scholar · View at Scopus
  90. I. N. Hines, H. J. Hartwell, Y. Feng et al., “Insulin resistance and metabolic hepatocarcinogenesis with parent-of-origin effects in A×B mice,” The American Journal of Pathology, vol. 179, no. 6, pp. 2855–2865, 2011. View at Publisher · View at Google Scholar · View at Scopus
  91. L. P. Bechmann, R. K. Gieseler, J.-P. Sowa et al., “Apoptosis is associated with CD36/fatty acid translocase upregulation in non-alcoholic steatohepatitis,” Liver International, vol. 30, no. 6, pp. 850–859, 2010. View at Publisher · View at Google Scholar · View at Scopus
  92. A. Bonen, N. N. Tandon, J. F. C. Glatz, J. J. F. P. Luiken, and G. J. F. Heigenhauser, “The fatty acid transporter FAT/CD36 is upregulated in subcutaneous and visceral adipose tissues in human obesity and type 2 diabetes,” International Journal of Obesity, vol. 30, no. 6, pp. 877–883, 2006. View at Publisher · View at Google Scholar · View at Scopus
  93. R. A. Memon, J. Fuller, A. H. Moser, P. J. Smith, C. Grunfeld, and K. R. Feingold, “Regulation of putative fatty acid transporters and Acyl-CoA synthetase in liver and adipose tissue in ob/ob mice,” Diabetes, vol. 48, no. 1, pp. 121–127, 1999. View at Google Scholar
  94. A. Taube, S. Lambernd, G. van Echten-Deckert, K. Eckardt, and J. Eckel, “Adipokines promote lipotoxicity in human skeletal muscle cells,” Archives of Physiology and Biochemistry, vol. 118, no. 3, pp. 92–101, 2012. View at Publisher · View at Google Scholar · View at Scopus
  95. S. El Akoum, I. Cloutier, and J.-F. Tanguay, “Vascular smooth muscle cell alterations triggered by mice adipocytes: role of high-fat diet,” Journal of Atherosclerosis and Thrombosis, vol. 19, no. 12, pp. 1128–1141, 2012. View at Publisher · View at Google Scholar · View at Scopus
  96. M. Anan, K. Uchihashi, S. Aoki et al., “A promising culture model for analyzing the interaction between adipose tissue and cardiomyocytes,” Endocrinology, vol. 152, no. 4, pp. 1599–1605, 2011. View at Publisher · View at Google Scholar · View at Scopus
  97. R. Gandhi, M. Takahashi, C. Virtanen, K. Syed, J. R. Davey, and N. N. Mahomed, “Microarray analysis of the infrapatellar fat pad in knee osteoarthritis: relationship with joint inflammation,” Journal of Rheumatology, vol. 38, no. 9, pp. 1966–1972, 2011. View at Publisher · View at Google Scholar · View at Scopus
  98. C. W. Wu, E. S. H. Chu, C. N. Y. Lam et al., “PPARγ is essential for protection against nonalcoholic steatohepatitis,” Gene Therapy, vol. 17, no. 6, pp. 790–798, 2010. View at Publisher · View at Google Scholar · View at Scopus
  99. A. Stahl, “A current review of fatty acid transport proteins (SLC27),” Pflugers Archiv European Journal of Physiology, vol. 447, no. 5, pp. 722–727, 2004. View at Publisher · View at Google Scholar · View at Scopus
  100. J. Pohl, A. Ring, T. Hermann, and W. Stremmel, “Role of FATP in parenchymal cell fatty acid uptake,” Biochimica et Biophysica Acta, vol. 1686, no. 1-2, pp. 1–6, 2004. View at Publisher · View at Google Scholar · View at Scopus
  101. R. E. Gimeno, “Fatty acid transport proteins,” Current Opinion in Lipidology, vol. 18, no. 3, pp. 271–266, 2007. View at Google Scholar
  102. C. M. Anderson and A. Stahl, “SLC27 fatty acid transport proteins,” Molecular Aspects of Medicine, vol. 34, no. 2-3, pp. 516–528, 2013. View at Publisher · View at Google Scholar · View at Scopus
  103. H. Doege and A. Stah, “Protein-mediated fatty acid uptake: novel insights from in vivo models,” Physiology, vol. 21, no. 4, pp. 259–268, 2006. View at Publisher · View at Google Scholar · View at Scopus
  104. H. Schneider, S. Staudacher, M. Poppelreuther, W. Stremmel, R. Ehehalt, and J. Füllekrug, “Protein mediated fatty acid uptake: synergy between CD36/FAT-facilitated transport and acyl-CoA synthetase-driven metabolism,” Archives of Biochemistry and Biophysics, vol. 546, pp. 8–18, 2014. View at Publisher · View at Google Scholar · View at Scopus
  105. J. F. Bower, J. M. Davis, E. Hao, and H. A. Barakat, “Differences in transport of fatty acids and expression of fatty acid transporting proteins in adipose tissue of obese black and white women,” The American Journal of Physiology—Endocrinology and Metabolism, vol. 290, no. 1, pp. E87–E91, 2006. View at Publisher · View at Google Scholar · View at Scopus
  106. K. Gertow, K. H. Pietiläinen, H. Yki-Järvinen et al., “Expression of fatty-acid-handling proteins in human adipose tissue in relation to obesity and insulin resistance,” Diabetologia, vol. 47, no. 6, pp. 1118–1125, 2004. View at Google Scholar · View at Scopus
  107. H.-C. Chiu, A. Kovacs, R. M. Blanton et al., “Transgenic expression of fatty acid transport protein 1 in the heart causes lipotoxic cardiomyopathy,” Circulation Research, vol. 96, no. 2, pp. 225–233, 2005. View at Publisher · View at Google Scholar · View at Scopus
  108. M. Marotta, A. Ferrer-Martínez, J. Parnau, M. Turini, K. MacÉ, and A. M. Gómez Foix, “Fiber type- and fatty acid composition-dependent effects of high-fat diets on rat muscle triacylglyceride and fatty acid transporter protein-1 content,” Metabolism: Clinical and Experimental, vol. 53, no. 8, pp. 1032–1036, 2004. View at Publisher · View at Google Scholar · View at Scopus
  109. P. D. Berk, S.-L. Zhou, C.-L. Kiang, D. Stump, M. Bradbury, and L. M. Isola, “Uptake of long chain free fatty acids is selectively up-regulated in adipocytes of zucker rats with genetic obesity and non-insulin-dependent diabetes mellitus,” The Journal of Biological Chemistry, vol. 272, no. 13, pp. 8830–8835, 1997. View at Publisher · View at Google Scholar · View at Scopus
  110. P. Besnard, I. Niot, H. Poirier, L. Clément, and A. Bernard, “New insights into the fatty acid-binding protein (FABP) family in the small intestine,” Molecular and Cellular Biochemistry, vol. 239, no. 1-2, pp. 139–147, 2002. View at Publisher · View at Google Scholar · View at Scopus
  111. A. Chmurzyńska, “The multigene family of fatty acid-binding proteins (FABPs): function, structure and polymorphism,” Journal of Applied Genetics, vol. 47, no. 1, pp. 39–48, 2006. View at Publisher · View at Google Scholar · View at Scopus
  112. R. M. Kaikaus, N. M. Bass, and R. K. Ockner, “Functions of fatty acid binding proteins,” Experientia, vol. 46, no. 6, pp. 617–630, 1990. View at Publisher · View at Google Scholar · View at Scopus
  113. A. W. Zimmerman and J. H. Veerkamp, “New insights into the structure and function of fatty acid-binding proteins,” Cellular and Molecular Life Sciences, vol. 59, no. 7, pp. 1096–1116, 2002. View at Publisher · View at Google Scholar · View at Scopus
  114. Y. Goto, Y. Matsuzaki, S. Kurihara et al., “A new melanoma antigen fatty acid-binding protein 7, involved in proliferation and invasion, is a potential target for immunotherapy and molecular target therapy,” Cancer Research, vol. 66, no. 8, pp. 4443–4449, 2006. View at Publisher · View at Google Scholar · View at Scopus
  115. C. Wolfrum, C. M. Borrmann, T. Börchers, and F. Spener, “Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors α- and γ-mediated gene expression via liver fatty acid binding protein: a signaling path to the nucleus,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 5, pp. 2323–2328, 2001. View at Publisher · View at Google Scholar · View at Scopus
  116. N. H. Haunerland and F. Spener, “Fatty acid-binding proteins—insights from genetic manipulations,” Progress in Lipid Research, vol. 43, no. 4, pp. 328–349, 2004. View at Publisher · View at Google Scholar · View at Scopus
  117. L. A. Afman and M. Müller, “Human nutrigenomics of gene regulation by dietary fatty acids,” Progress in Lipid Research, vol. 51, no. 1, pp. 63–70, 2012. View at Publisher · View at Google Scholar · View at Scopus
  118. J. Justesen, K. Stenderup, E. N. Ebbesen, L. Mosekilde, T. Steiniche, and M. Kassem, “Adipocyte tissue volume in bone marrow is increased with aging and in patients with osteoporosis,” Biogerontology, vol. 2, no. 3, pp. 165–171, 2001. View at Publisher · View at Google Scholar · View at Scopus
  119. D. G. Mashek, L. O. Li, and R. A. Coleman, “Long-chain acyl-CoA synthetases and fatty acid channeling,” Future Lipidology, vol. 2, no. 4, pp. 465–476, 2007. View at Publisher · View at Google Scholar · View at Scopus
  120. J. A. Kanaley, S. Shadid, M. T. Sheehan, Z. Guo, and M. D. Jensen, “Relationship between plasma free fatty acid, intramyocellular triglycerides and long-chain acylcarnitines in resting humans,” Journal of Physiology, vol. 587, part 24, pp. 5939–5950, 2009. View at Publisher · View at Google Scholar · View at Scopus
  121. S. M. Turpin, A. J. Hoy, R. D. Brown et al., “Adipose triacylglycerol lipase is a major regulator of hepatic lipid metabolism but not insulin sensitivity in mice,” Diabetologia, vol. 54, no. 1, pp. 146–156, 2011. View at Publisher · View at Google Scholar · View at Scopus
  122. R. A. Coleman and D. P. Lee, “Enzymes of triacylglycerol synthesis and their regulation,” Progress in Lipid Research, vol. 43, no. 2, pp. 134–176, 2004. View at Publisher · View at Google Scholar · View at Scopus
  123. M. E. Monaco, C. J. Creighton, P. Lee, X. Zou, M. K. Topham, and D. M. Stafforini, “Expression of long-chain fatty Acyl-CoA synthetase 4 in breast and prostate cancers is associated with sex steroid hormone receptor negativity,” Translational Oncology, vol. 3, no. 2, pp. 91–98, 2010. View at Publisher · View at Google Scholar · View at Scopus
  124. Z. Pei, P. Fraisl, X. Shi et al., “Very long-chain acyl-CoA synthetase 3: overexpression and growth dependence in lung cancer,” PLoS ONE, vol. 8, no. 7, Article ID e69392, 2013. View at Publisher · View at Google Scholar · View at Scopus
  125. K. S. Young, K. P. Mi, H. H. Su et al., “Regulation of cell growth by fatty acid-CoA ligase 4 in human hepatocellular carcinoma cells,” Experimental and Molecular Medicine, vol. 39, no. 4, pp. 477–482, 2007. View at Publisher · View at Google Scholar · View at Scopus
  126. Y. Zhou, P. Abidi, A. Kim et al., “Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin M reduces hypertriglyceridemia through enhanced β-oxidation,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 10, pp. 2198–2205, 2007. View at Publisher · View at Google Scholar · View at Scopus
  127. Y. Cao, A. T. Pearman, G. A. Zimmerman, T. M. McIntyre, and S. M. Prescott, “Intracellular unesterified arachidonic acid signals apoptosis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 21, pp. 11280–11285, 2000. View at Publisher · View at Google Scholar · View at Scopus
  128. T. Mashima, S. Sato, S. Okabe et al., “Acyl-CoA synthetase as a cancer survival factor: its inhibition enhances the efficacy of etoposide,” Cancer Science, vol. 100, no. 8, pp. 1556–1562, 2009. View at Publisher · View at Google Scholar · View at Scopus
  129. I. Shimomura, K. Tokunaga, S. Jiao et al., “Marked enhancement of acyl-CoA synthetase activity and mRNA, paralleled to lipoprotein lipase mRNA, in adipose tissues of Zucker obese rats (fa/fa),” Biochimica et Biophysica Acta, vol. 1124, no. 2, pp. 112–118, 1992. View at Publisher · View at Google Scholar · View at Scopus
  130. B. D. Hegarty, G. J. Cooney, E. W. Kraegen, and S. M. Furler, “Increased efficiency of fatty acid uptake contributes to lipid accumulation in skeletal muscle of high fat-fed insulin-resistant rats,” Diabetes, vol. 51, no. 5, pp. 1477–1484, 2002. View at Publisher · View at Google Scholar · View at Scopus
  131. V. K. Khor, W. J. Shen, and F. B. Kraemer, “Lipid droplet metabolism,” Current Opinion in Clinical Nutrition and Metabolic Care, vol. 16, no. 6, pp. 632–637, 2013. View at Google Scholar
  132. S. Cases, S. J. Smith, Y.-W. Zheng et al., “Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 22, pp. 13018–13023, 1998. View at Publisher · View at Google Scholar · View at Scopus
  133. R. Coleman and R. M. Bell, “Triacylglycerol synthesis in isolated fat cells. Studies on the microsomal diacylglycerol acyltransferase activity using ethanol-dispersed diacylglycerols,” The Journal of Biological Chemistry, vol. 251, no. 15, pp. 4537–4543, 1976. View at Google Scholar · View at Scopus
  134. R. A. Coleman, T. M. Lewin, and D. M. Muoio, “Physiological and nutritional regulation of enzymes of triacylglycerol synthesis,” Annual Review of Nutrition, vol. 20, pp. 77–103, 2000. View at Publisher · View at Google Scholar · View at Scopus
  135. R. Zechner, R. Zimmermann, T. O. Eichmann et al., “FAT SIGNALS—lipases and lipolysis in lipid metabolism and signaling,” Cell Metabolism, vol. 15, no. 3, pp. 279–291, 2012. View at Publisher · View at Google Scholar · View at Scopus
  136. R. E. Gimeno and J. Cao, “Thematic review series: glycerolipids. Mammalian glycerol-3-phosphate acyltransferases: new genes for an old activity,” The Journal of Lipid Research, vol. 49, no. 10, pp. 2079–2088, 2008. View at Publisher · View at Google Scholar · View at Scopus
  137. K. Takeuchi and K. Reue, “Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis,” American Journal of Physiology—Endocrinology and Metabolism, vol. 296, no. 6, pp. E1195–E1209, 2009. View at Publisher · View at Google Scholar · View at Scopus
  138. A. A. Wendel, T. M. Lewin, and R. A. Coleman, “Glycerol-3-phosphate acyltransferases: rate limiting enzymes of triacylglycerol biosynthesis,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1791, no. 6, pp. 501–506, 2009. View at Publisher · View at Google Scholar · View at Scopus
  139. L. S. Csaki and K. Reue, “Lipins: multifunctional lipid metabolism proteins,” Annual Review of Nutrition, vol. 30, pp. 257–272, 2010. View at Publisher · View at Google Scholar · View at Scopus
  140. R. Stienstra and S. Kersten, “Fight fat with DGAT,” Journal of Lipid Research, vol. 52, no. 4, pp. 591–592, 2011. View at Publisher · View at Google Scholar · View at Scopus
  141. E. Currie, A. Schulze, R. Zechner, T. C. Walther, and R. V. Farese Jr., “Cellular fatty acid metabolism and cancer,” Cell Metabolism, vol. 18, no. 2, pp. 153–161, 2013. View at Publisher · View at Google Scholar · View at Scopus
  142. G. P. Holloway, L. A. Snook, R. J. Harris, J. F. C. Glatz, J. J. F. P. Luiken, and A. Bonen, “In obese Zucker rats, lipids accumulate in the heart despite normal mitochondrial content, morphology and long-chain fatty acid oxidation,” The Journal of Physiology, vol. 589, no. 1, pp. 169–180, 2011. View at Publisher · View at Google Scholar · View at Scopus
  143. Z. K. Guo and M. D. Jensen, “Accelerated intramyocellular triglyceride synthesis in skeletal muscle of high-fat-induced obese rats,” International Journal of Obesity, vol. 27, no. 9, pp. 1014–1019, 2003. View at Publisher · View at Google Scholar · View at Scopus
  144. X.-J. Zhang, D. L. Chinkes, Z. Wu, D. N. Herndon, and R. R. Wolfe, “The synthetic rate of muscle triglyceride but not phospholipid is increased in obese rabbits,” Metabolism: Clinical and Experimental, vol. 58, no. 11, pp. 1649–1656, 2009. View at Publisher · View at Google Scholar · View at Scopus
  145. A. Bonen, M. L. Parolin, G. R. Steinberg et al., “Triacylglycerol accumulation in human obesity and type 2 diabetes is associated with increased rates of skeletal muscle fatty acid transport increased sarcolemmal FAT/CD36,” FASEB Journal, vol. 18, no. 10, pp. 1144–1146, 2004. View at Publisher · View at Google Scholar · View at Scopus
  146. L. Vergnes, A. P. Beigneux, R. Davis, S. M. Watkins, S. G. Young, and K. Reue, “Agpat6 deficiency causes subdermal lipodystrophy and resistance to obesity,” Journal of Lipid Research, vol. 47, no. 4, pp. 745–754, 2006. View at Publisher · View at Google Scholar · View at Scopus
  147. S. J. Smith, S. Cases, D. R. Jensen et al., “Obesity resistance and multiple mechanisms of triglyceride synthesis in mice lacking Dgat,” Nature Genetics, vol. 25, no. 1, pp. 87–90, 2000. View at Publisher · View at Google Scholar · View at Scopus
  148. L. S. Csaki, J. R. Dwyer, X. Li et al., “Lipin-1 and lipin-3 together determine adiposity in vivo,” Molecular Metabolism, vol. 3, no. 2, pp. 145–154, 2014. View at Publisher · View at Google Scholar
  149. H. C. Chen and R. V. Farese Jr., “Inhibition of triglyceride synthesis as a treatment strategy for obesity: lessons from DGAT1-deficient mice,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 25, no. 3, pp. 482–486, 2005. View at Publisher · View at Google Scholar · View at Scopus
  150. L. E. Hammond, S. Neschen, A. J. Romanelli et al., “Mitochondrial glycerol-3-phosphate acyltransferase-1 is essential in liver for the metabolism of excess acyl-CoAs,” The Journal of Biological Chemistry, vol. 280, no. 27, pp. 25629–25636, 2005. View at Publisher · View at Google Scholar · View at Scopus
  151. D. Lindén, L. William-Olsson, M. Rhedin, A.-K. Asztély, J. C. Clapham, and S. Schreyer, “Overexpression of mitochondrial GPAT in rat hepatocytes leads to decreased fatty acid oxidation and increased glycerolipid biosynthesis,” The Journal of Lipid Research, vol. 45, no. 7, pp. 1279–1288, 2004. View at Publisher · View at Google Scholar · View at Scopus
  152. C. A. Nagle, L. Vergnes, H. Dejong et al., “Identification of a novel sn-glycerol-3-phosphate acyltransferase isoform, GPAT4, as the enzyme deficient in Agpat6-/- mice,” Journal of Lipid Research, vol. 49, no. 4, pp. 823–831, 2008. View at Publisher · View at Google Scholar · View at Scopus
  153. H. Ruan and H. J. Pownall, “Overexpression of 1-acyl-glycerol-3-phosphate acyltransferase-alpha enhances lipid storage in cellular models of adipose tissue and skeletal muscle,” Diabetes, vol. 50, no. 2, pp. 233–240, 2001. View at Publisher · View at Google Scholar
  154. J. Phan and K. Reue, “Lipin, a lipodystrophy and obesity gene,” Cell Metabolism, vol. 1, no. 1, pp. 73–83, 2005. View at Publisher · View at Google Scholar · View at Scopus
  155. C. Bagnato and R. A. Igal, “Overexpression of diacylglycerol acyltransferase-1 reduces phospholipid synthesis, proliferation, and invasiveness in simian virus 40-transformed human lung fibroblasts,” The Journal of Biological Chemistry, vol. 278, no. 52, pp. 52203–52211, 2003. View at Publisher · View at Google Scholar · View at Scopus
  156. T. C. Walther and R. V. Farese, “Lipid droplets and cellular lipid metabolism,” Annual Review of Biochemistry, vol. 81, pp. 687–714, 2012. View at Publisher · View at Google Scholar · View at Scopus
  157. C. J. Antalis, T. Arnold, T. Rasool, B. Lee, K. K. Buhman, and R. A. Siddiqui, “High ACAT1 expression in estrogen receptor negative basal-like breast cancer cells is associated with LDL-induced proliferation,” Breast Cancer Research and Treatment, vol. 122, no. 3, pp. 661–670, 2010. View at Publisher · View at Google Scholar · View at Scopus
  158. J. V. Swinnen, P. P. van Veldhoven, M. Esquenet, W. Heyns, and G. Verhoeven, “Androgens markedly stimulate the accumulation of neutral lipids in the human prostatic adenocarcinoma cell line LNCaP,” Endocrinology, vol. 137, no. 10, pp. 4468–4474, 1996. View at Publisher · View at Google Scholar · View at Scopus
  159. N. G. Than, B. Sumegi, S. Bellyei et al., “Lipid droplet and milk lipid globule membrane associated placental protein 17b (PP17b) is involved in apoptotic and differentiation processes of human epithelial cervical carcinoma cells,” European Journal of Biochemistry, vol. 270, no. 6, pp. 1176–1188, 2003. View at Publisher · View at Google Scholar · View at Scopus
  160. A. M. Dvorak, P. F. Weller, V. S. Harvey, E. S. Morgan, and H. F. Dvorak, “Ultrastructural localization of prostaglandin endoperoxide synthase (cyclooxygenase) to isolated, purified fractions of guinea pig peritoneal macrophage and line 10 hepatocarcinoma cell lipid bodies,” International Archives of Allergy and Immunology, vol. 101, no. 2, pp. 136–142, 1993. View at Publisher · View at Google Scholar · View at Scopus
  161. M. T. Accioly, P. Pacheco, C. M. Maya-Monteiro et al., “Lipid bodies are reservoirs of cyclooxygenase-2 and sites of prostaglandin-E2 synthesis in colon cancer cells,” Cancer Research, vol. 68, no. 6, pp. 1732–1740, 2008. View at Publisher · View at Google Scholar · View at Scopus
  162. E. Przybytkowski, É. Joly, C. J. Nolan et al., “Upregulation of cellular triacylglycerol—free fatty acid cycling by oleate is associated with long-term serum-free survival of human breast cancer cells,” Biochemistry and Cell Biology, vol. 85, no. 3, pp. 301–310, 2007. View at Publisher · View at Google Scholar · View at Scopus
  163. R. J. DeBerardinis, J. J. Lum, G. Hatzivassiliou, and C. B. Thompson, “The biology of cancer: metabolic reprogramming fuels cell growth and proliferation,” Cell Metabolism, vol. 7, no. 1, pp. 11–20, 2008. View at Publisher · View at Google Scholar · View at Scopus
  164. J. A. Villena, B. Viollet, F. Andreelli, A. Kahn, S. Vaulont, and H. S. Sul, “Induced adiposity and adipocyte hypertrophy in mice lacking the AMP-activated protein kinase-alpha2 subunit,” Diabetes, vol. 53, no. 9, pp. 2242–2249, 2004. View at Publisher · View at Google Scholar · View at Scopus
  165. R. Zimmermann, J. G. Strauss, G. Haemmerle et al., “Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase,” Science, vol. 306, no. 5700, pp. 1383–1386, 2004. View at Publisher · View at Google Scholar · View at Scopus
  166. T. O. Eichmann, M. Kumari, J. T. Haas et al., “Studies on the substrate and stereo/regioselectivity of adipose triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-acyltransferases,” The Journal of Biological Chemistry, vol. 287, no. 49, pp. 41446–41457, 2012. View at Publisher · View at Google Scholar · View at Scopus
  167. G. Haemmerle, R. Zimmermann, M. Hayn et al., “Hormone-sensitive lipase deficiency in mice causes diglyceride accumulation in adipose tissue, muscle, and testis,” Journal of Biological Chemistry, vol. 277, no. 7, pp. 4806–4815, 2002. View at Publisher · View at Google Scholar · View at Scopus
  168. G. Fredrikson, P. Stralfors, N. O. Nilsson, and P. Belfrage, “Hormone-sensitive lipase of rat adipose tissue. Purification and some properties,” The Journal of Biological Chemistry, vol. 256, no. 12, pp. 6311–6320, 1981. View at Google Scholar · View at Scopus
  169. R. Zechner, P. C. Kienesberger, G. Haemmerle, R. Zimmermann, and A. Lass, “Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores,” Journal of Lipid Research, vol. 50, no. 1, pp. 3–21, 2009. View at Publisher · View at Google Scholar · View at Scopus
  170. C. Gercel-Taylor, D. L. Doering, F. B. Kraemer, and D. D. Taylor, “Aberrations in normal systemic lipid metabolism in ovarian cancer patients,” Gynecologic Oncology, vol. 60, no. 1, pp. 35–41, 1996. View at Publisher · View at Google Scholar · View at Scopus
  171. D. K. Nomura, J. Z. Long, S. Niessen, H. S. Hoover, S.-W. Ng, and B. F. Cravatt, “Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis,” Cell, vol. 140, no. 1, pp. 49–61, 2010. View at Publisher · View at Google Scholar · View at Scopus
  172. H. de Naeyer, D. M. Ouwens, Y. van Nieuwenhove et al., “Combined gene and protein expression of hormone-sensitive lipase and adipose triglyceride lipase, mitochondrial content, and adipocyte size in subcutaneous and visceral adipose tissue of morbidly obese men,” Obesity Facts, vol. 4, no. 5, pp. 407–416, 2011. View at Publisher · View at Google Scholar · View at Scopus
  173. D. Langin, A. Dicker, G. Tavernier et al., “Adipocyte lipases and defect of lipolysis in human obesity,” Diabetes, vol. 54, no. 11, pp. 3190–3197, 2005. View at Publisher · View at Google Scholar · View at Scopus
  174. G. R. Steinberg, B. E. Kemp, and M. J. Watt, “Adipocyte triglyceride lipase expression in human obesity,” American Journal of Physiology—Endocrinology and Metabolism, vol. 293, no. 4, pp. E958–E964, 2007. View at Publisher · View at Google Scholar · View at Scopus
  175. J. W. E. Jocken, D. Langin, E. Smit et al., “Adipose triglyceride lipase and hormone-sensitive lipase protein expression is decreased in the obese insulin-resistant state,” The Journal of Clinical Endocrinology and Metabolism, vol. 92, no. 6, pp. 2292–2299, 2007. View at Publisher · View at Google Scholar · View at Scopus
  176. P. Oliver, A. Caimari, R. Díaz-Rúa, and A. Palou, “Diet-induced obesity affects expression of adiponutrin/PNPLA3 and adipose triglyceride lipase, two members of the same family,” International Journal of Obesity, vol. 36, no. 2, pp. 225–232, 2012. View at Publisher · View at Google Scholar · View at Scopus
  177. R. A. Coleman and D. G. Mashek, “Mammalian triacylglycerol metabolism: synthesis, lipolysis, and signaling,” Chemical Reviews, vol. 111, no. 10, pp. 6359–6386, 2011. View at Publisher · View at Google Scholar · View at Scopus
  178. Y. Liu, “Fatty acid oxidation is a dominant bioenergetic pathway in prostate cancer,” Prostate Cancer and Prostatic Diseases, vol. 9, no. 3, pp. 230–234, 2006. View at Publisher · View at Google Scholar · View at Scopus
  179. J. Khasawneh, M. D. Schulz, A. Walch et al., “Inflammation and mitochondrial fatty acid β-oxidation link obesity to early tumor promotion,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 9, pp. 3354–3359, 2009. View at Publisher · View at Google Scholar · View at Scopus
  180. N. Turner, C. R. Bruce, S. M. Beale et al., “Excess lipid availability increases mitochondrial fatty acid oxidative capacity in muscle: evidence against a role for reduced fatty acid oxidation in lipid-induced insulin resistance in rodents,” Diabetes, vol. 56, no. 8, pp. 2085–2092, 2007. View at Publisher · View at Google Scholar · View at Scopus
  181. G. P. Holloway, A. Bonen, and L. L. Spriet, “Regulation of skeletal muscle mitochondrial fatty acid metabolism in lean and obese individuals,” American Journal of Clinical Nutrition, vol. 89, no. 1, pp. 455S–462S, 2009. View at Publisher · View at Google Scholar · View at Scopus
  182. M. W. Hulver, J. R. Berggren, R. N. Cortright et al., “Skeletal muscle lipid metabolism with obesity,” The American Journal of Physiology—Endocrinology and Metabolism, vol. 284, no. 4, pp. E741–E747, 2003. View at Google Scholar
  183. J.-Y. Kim, R. C. Hickner, R. L. Cortright, G. L. Dohm, and J. A. Houmard, “Lipid oxidation is reduced in obese human skeletal muscle,” American Journal of Physiology—Endocrinology and Metabolism, vol. 279, no. 5, pp. E1039–E1044, 2000. View at Google Scholar · View at Scopus
  184. J. D. McGarry and N. F. Brown, “The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis,” European Journal of Biochemistry, vol. 244, no. 1, pp. 1–14, 1997. View at Publisher · View at Google Scholar · View at Scopus
  185. L. Abu-Elheiga, M. M. Matzuk, K. A. H. Abo-Hashema, and S. J. Wakil, “Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2,” Science, vol. 291, no. 5513, pp. 2613–2616, 2001. View at Publisher · View at Google Scholar · View at Scopus
  186. G. Peluso, R. Nicolai, E. Reda, P. Benatti, A. Barbarisi, and M. Calvani, “Cancer and anticancer therapy-induced modifications on metabolism mediated by carnitine system,” Journal of Cellular Physiology, vol. 182, no. 3, pp. 339–350, 2000. View at Google Scholar
  187. N. T. Price, F. R. van der Leij, V. N. Jackson et al., “A novel brain-expressed protein related to carnitine palmitoyltransferase I,” Genomics, vol. 80, no. 4, pp. 433–442, 2002. View at Publisher · View at Google Scholar · View at Scopus
  188. F. R. van der Leij, A. M. Kram, B. Bartelds et al., “Cytological evidence that the C-terminus of carnitine palmitoyltransferase I is on the cytosolic face of the mitochondrial outer membrane,” Biochemical Journal, vol. 341, no. 3, pp. 777–784, 1999. View at Publisher · View at Google Scholar · View at Scopus
  189. P. Mazzarelli, S. Pucci, E. Bonanno, F. Sesti, M. Calvani, and L. G. Spagnoli, “Carnitine palmitoyltransferase I in human carcinomas: a novel role in histone deacetylation?” Cancer Biology and Therapy, vol. 6, no. 10, pp. 1606–1613, 2007. View at Publisher · View at Google Scholar · View at Scopus
  190. P. T. Reilly and T. W. Mak, “Molecular pathways: tumor cells Co-opt the brain-specific metabolism gene CPT1C to promote survival,” Clinical Cancer Research, vol. 18, no. 21, pp. 5850–5855, 2012. View at Publisher · View at Google Scholar · View at Scopus
  191. A. Pacilli, M. Calienni, S. Margarucci et al., “Carnitine-acyltransferase system inhibition, cancer cell death, and prevention of myc-induced lymphomagenesis,” Journal of the National Cancer Institute, vol. 105, no. 7, pp. 489–498, 2013. View at Publisher · View at Google Scholar · View at Scopus
  192. L. S. Pike, A. L. Smift, N. J. Croteau, D. A. Ferrick, and M. Wu, “Inhibition of fatty acid oxidation by etomoxir impairs NADPH production and increases reactive oxygen species resulting in ATP depletion and cell death in human glioblastoma cells,” Biochimica et Biophysica Acta, vol. 1807, no. 6, pp. 726–734, 2011. View at Google Scholar
  193. I. Samudio, R. Harmancey, M. Fiegl et al., “Pharmacologic inhibition of fatty acid oxidation sensitizes human leukemia cells to apoptosis induction,” The Journal of Clinical Investigation, vol. 120, no. 1, pp. 142–156, 2010. View at Publisher · View at Google Scholar · View at Scopus
  194. S. J. Wakil, E. B. Titchener, and D. M. Gibson, “Evidence for the participation of biotin in the enzymic synthesis of fatty acids,” Biochimica et Biophysica Acta, vol. 29, no. 1, pp. 225–226, 1958. View at Publisher · View at Google Scholar · View at Scopus
  195. L. Abu-Elheiga, W. Oh, P. Kordari, and S. J. Wakil, “Acetyl-CoA carboxylase 2 mutant mice are protected against obesity and diabetes induced by high-fat/high-carbohydrate diets,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 18, pp. 10207–10212, 2003. View at Publisher · View at Google Scholar · View at Scopus
  196. A. J. Iverson, A. Bianchi, A.-C. Nordlund, and L. A. Witters, “Immunological analysis of acetyl-CoA carboxylase mass, tissue distribution and subunit composition,” Biochemical Journal, vol. 269, no. 2, pp. 365–371, 1990. View at Google Scholar · View at Scopus
  197. K. G. Thampy, “Formation of malonyl coenzyme A in rat heart. Identification and purification of an isozyme of acetyl coenzyme A carboxylase from rat heart,” The Journal of Biological Chemistry, vol. 264, no. 30, pp. 17631–17634, 1989. View at Google Scholar · View at Scopus
  198. K. G. Thampy and S. J. Wakil, “Regulation of acetyl-coenzyme A carboxylase. I. Purification and properties of two forms of acetyl-coenzyme A carboxylase from rat liver,” The Journal of Biological Chemistry, vol. 263, no. 13, pp. 6447–6453, 1988. View at Google Scholar · View at Scopus
  199. H. J. Harwood Jr., “Treating the meytabolic syndrome: acetyl-CoA carboxylase inhibition,” Expert Opinion on Therapeutic Targets, vol. 9, no. 2, pp. 267–281, 2005. View at Publisher · View at Google Scholar · View at Scopus
  200. L. Tong, “Structure and function of biotin-dependent carboxylases,” Cellular and Molecular Life Sciences, vol. 70, no. 5, pp. 863–891, 2013. View at Publisher · View at Google Scholar · View at Scopus
  201. C. Wang, C. Xu, M. Sun, D. Luo, D.-F. Liao, and D. Cao, “Acetyl-CoA carboxylase-alpha inhibitor TOFA induces human cancer cell apoptosis,” Biochemical and Biophysical Research Communications, vol. 385, no. 3, pp. 302–306, 2009. View at Publisher · View at Google Scholar · View at Scopus
  202. A. Beckers, S. Organe, L. Timmermans et al., “Chemical inhibition of acetyl-CoA carboxylase induces growth arrest and cytotoxicity selectively in cancer cells,” Cancer Research, vol. 67, no. 17, pp. 8180–8187, 2007. View at Publisher · View at Google Scholar · View at Scopus
  203. V. Chajès, M. Cambot, K. Moreau, G. M. Lenoir, and V. Joulin, “Acetyl-CoA carboxylase α is essential to breast cancer cell survival,” Cancer Research, vol. 66, no. 10, pp. 5287–5294, 2006. View at Publisher · View at Google Scholar · View at Scopus
  204. K. Brusselmans, E. de Schrijver, G. Verhoeven, and J. V. Swinnen, “RNA interference—mediated silencing of the acetyl-Coa-carboxylase-α gene induces growth inhibition and apoptosis of prostate cancer cells,” Cancer Research, vol. 65, no. 15, pp. 6719–6725, 2005. View at Publisher · View at Google Scholar · View at Scopus
  205. S.-M. Jeon, N. S. Chandel, and N. Hay, “AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress,” Nature, vol. 485, no. 7400, pp. 661–665, 2012. View at Publisher · View at Google Scholar · View at Scopus
  206. W. Zhou, Y. Tu, P. J. Simpson, and F. P. Kuhajda, “Malonyl-CoA decarboxylase inhibition is selectively cytotoxic to human breast cancer cells,” Oncogene, vol. 28, no. 33, pp. 2979–2987, 2009. View at Publisher · View at Google Scholar · View at Scopus
  207. G. K. Bandyopadhyay, J. G. Yu, J. Ofrecio, and J. M. Olefsky, “Increased malonyl-CoA levels in muscle from obese and type 2 diabetic subjects lead to decreased fatty acid oxidation and increased lipogenesis; thiazolidinedione treatment reverses these defects,” Diabetes, vol. 55, no. 8, pp. 2277–2285, 2006. View at Publisher · View at Google Scholar · View at Scopus
  208. G. R. Steinberg, B. J. Michell, B. J. W. van Denderen et al., “Tumor necrosis factor α-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling,” Cell Metabolism, vol. 4, no. 6, pp. 465–474, 2006. View at Publisher · View at Google Scholar · View at Scopus
  209. M. Yamasaki, S. Hasegawa, T. Kitani, K. Hidai, and T. Fukui, “Differential effects of obesity on acetoacetyl-CoA synthetase gene in rat adipose tissues,” European Journal of Lipid Science and Technology, vol. 109, no. 6, pp. 617–622, 2007. View at Publisher · View at Google Scholar · View at Scopus
  210. A. Janovská, G. Hatzinikolas, V. Staikopoulos, J. McInerney, M. Mano, and G. A. Wittert, “AMPK and ACC phosphorylation: effect of leptin, muscle fibre type and obesity,” Molecular and Cellular Endocrinology, vol. 284, no. 1-2, pp. 1–10, 2008. View at Publisher · View at Google Scholar · View at Scopus
  211. K. L. Mullen, J. Pritchard, I. Ritchie et al., “Adiponectin resistance precedes the accumulation of skeletal muscle lipids and insulin resistance in high-fat-fed rats,” American Journal of Physiology: Regulatory Integrative and Comparative Physiology, vol. 296, no. 2, pp. R243–R251, 2009. View at Publisher · View at Google Scholar · View at Scopus
  212. J. M. Peterson, S. Aja, Z. Wei, and G. W. Wong, “CTRP1 protein enhances fatty acid oxidation via AMP-activated protein kinase (AMPK) activation and acetyl-CoA carboxylase (ACC) inhibition,” Journal of Biological Chemistry, vol. 287, no. 2, pp. 1576–1587, 2012. View at Publisher · View at Google Scholar · View at Scopus
  213. M. D. Fullerton, S. Galic, K. Marcinko et al., “Single phosphorylation sites in Acc1 and Acc2 regulate lipid homeostasis and the insulin-sensitizing effects of metformin,” Nature Medicine, vol. 19, no. 12, pp. 1649–1654, 2013. View at Publisher · View at Google Scholar · View at Scopus