Cited by 1,002Cancer, Lipids, and MetabolismLipid metabolism and biosynthesisSphingolipid Metabolism and Signaling

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Monoacylglycerol Lipase Regulates a Fatty Acid Network that Promotes Cancer Pathogenesis

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Nomura, Daniel K., Long, Jonathan Z., Niessen, Sherry, Hoover, Heather S., Ng, Shu-Wing, Cravatt, Benjamin F.·2010·Cell

DOI 10.1016/j.cell.2009.11.027PMC PMC2885975

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Abstract

Tumor cells display progressive changes in metabolism that correlate with malignancy, including development of a lipogenic phenotype. How stored fats are liberated and remodeled to support cancer pathogenesis, however, remains unknown. Here, we show that the enzyme monoacylglycerol lipase (MAGL) is highly expressed in aggressive human cancer cells and primary tumors, where it regulates a fatty acid network enriched in oncogenic signaling lipids that promotes migration, invasion, survival, and in vivo tumor growth. Overexpression of MAGL in nonaggressive cancer cells recapitulates this fatty acid network and increases their pathogenicity-phenotypes that are reversed by an MAGL inhibitor. Impairments in MAGL-dependent tumor growth are rescued by a high-fat diet, indicating that exogenous sources of fatty acids can contribute to malignancy in cancers lacking MAGL activity. Together, these findings reveal how cancer cells can co-opt a lipolytic enzyme to translate their lipogenic state into an array of protumorigenic signals. PAPERFLICK:

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Overweight, obesity, and mortality from cancer in a prospectively studied cohort of U.S. Adults
Calle, E. E., Rodriguez, C., Walker-Thurmond, K., & Thun, M. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa021423 · Cited by 7,696
An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
Eng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484
XCMS: Processing Mass Spectrometry Data for Metabolite Profiling Using Nonlinear Peak Alignment, Matching, and Identification
Smith, C. A., Want, E. J., O’Maille, G., Abagyan, R. A., & Siuzdak, G. E. (2006) · Analytical Chemistry · doi:10.1021/ac051437y · Cited by 5,296
Why Do Cancers Have High Aerobic Glycolysis?
Gatenby, R. A., & Gillies, R. J. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1478 · Cited by 4,784
The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation
DeBerardinis, R. J., Lum, J. J., Hatzivassiliou, G., & Thompson, C. B. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.002 · Cited by 4,088
Overweight, obesity and cancer: epidemiological evidence and proposed mechanisms
Calle, E. E., & Kaaks, R. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1408 · Cited by 3,613
Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
Menendez, J. A., & Lupu, R. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2222 · Cited by 2,941
The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820
Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis
DeBerardinis, R. J., Mancuso, A., Daikhin, E., Nissim, I., Yudkoff, M., Wehrli, S., & Thompson, C. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709747104 · Cited by 2,622
A Model for Random Sampling and Estimation of Relative Protein Abundance in Shotgun Proteomics
Liu, H., Sadygov, R. G., & Yates, J. R. (2004) · Analytical Chemistry · doi:10.1021/ac0498563 · Cited by 2,534

Flagged first, then by citations

Show all 69 references

Research works printed but not linked: 6

Cociorva, D., and Yates, J.R. (2006). DTASelect 2.0: improving the confidence of peptide and protein identifications. Proceedings of the 54th Annual ASMS Meeting, American Society for Mass Spectrometry, Sante Fe, New Mexico.
Jessani, N., Liu, Y., Humphrey, M., and Cravatt, B.F. (2002). Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness. Proc. Natl. Acad. Sci. USA 99, 10335-10340. · DOI
Jessani, N., Humphrey, M., McDonald, W.H., Niessen, S., Masuda, K., Gangadharan, B., Yates, J.R., 3rd, Mueller, B.M., and Cravatt, B.F. (2004). Carcinoma and stromal enzyme activity profiles associated with breast tumor growth in vivo. Proc. Natl. Acad. Sci. USA 101, 13756-13761. · DOI
Jessani, N., Niessen, S., Wei, B.Q., Nicolau, M., Humphrey, M., Ji, Y., Han, W., Noh, D.Y., Yates, J.R., 3rd, Jeffrey, S.S., et al. (2005). A streamlined platform for high-content functional proteomics of primary human specimens. Nat. Methods 2, 691-697. · DOI
Liu, H., Sadygov, R.G., and Yates, J.R., III. (2004). A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201. · DOI
Seftor, E.A., Meltzer, P.S., Kirschmann, D.A., Pe'er, J., Maniotis, A.J., Trent, J.M., Folberg, R., and Hendrix, M.J. (2002). Molecular determinants of human uveal melanoma invasion and metastasis. Clin. Exp. Metastasis 19, 233-246. · DOI

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Authors: Nomura, D. K., Long, J. Z., Niessen, S., Hoover, H. S., Ng, S.-W., & Cravatt, B. F.
Affiliations: Scripps Research Institute (US)
Brigham and Women's Hospital (US)
Corresponding author: Cravatt, Benjamin F.
ORCID: Nomura, Daniel K.
Long, Jonathan Z.
Hoover, Heather S.
Ng, Shu-Wing
Cravatt, Benjamin F.
Venue: Cell
Publisher: Elsevier BV
Published: 2010-01
Volume: 140
Issue: 1
Pages: 49-61
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2009.11.027
PMC: PMC2885975
OpenAlex: W2127624416
Cited by: 1,002
References: 69
Citations by year: 2026: 40 · 2025: 41 · 2024: 55 · 2023: 46 · 2022: 59 · 2021: 78 · 2020: 69 · 2019: 67 · 2018: 69 · 2017: 60 · 2016: 75 · 2015: 72 · 2014: 70 · 2013: 61 · 2012: 47
FWCI: 15.66
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1293 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Cancer Institute (R01CA132630, CA-087660, R37CA087660, R01CA087660, CA132630)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Keywords: monoacylglycerol lipase, fatty acid metabolism, lipolysis, tumor cell migration and invasion, tumor growth, MAGL inhibitors, high-fat diet, cancer metabolism
MeSH terms: Animals, Cell Line, Fatty Acids, Female, Humans, Monoacylglycerol Lipases, Neoplasm Transplantation, Ovarian Neoplasms, Transplantation, Heterologous, Tumor Cells, Cultured, Monoglycerides, Mice

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Monoacylglycerol Lipase Regulates a Fatty Acid Network that Promotes Cancer Pathogenesis

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