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An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling

Academic Article
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Overview

related to degree

  • Niessen, Sherry, Ph.D. in Chemistry, Scripps Research 2004 - 2008
  • Chiang, Kyle Ping, Ph.D. in Macromolecular and Cellular Structure and Chemistry, Scripps Research 2001 - 2006

authors

  • Chiang, Kyle Ping
  • Niessen, Sherry
  • Saghatelian, Alan
  • Cravatt, Benjamin

publication date

  • October 2006

journal

  • Chemistry & Biology  Journal

abstract

  • Hundreds, if not thousands, of uncharacterized enzymes currently populate the human proteome. Assembly of these proteins into the metabolic and signaling pathways that govern cell physiology and pathology constitutes a grand experimental challenge. Here, we address this problem by using a multidimensional profiling strategy that combines activity-based proteomics and metabolomics. This approach determined that KIAA1363, an uncharacterized enzyme highly elevated in aggressive cancer cells, serves as a central node in an ether lipid signaling network that bridges platelet-activating factor and lysophosphatidic acid. Biochemical studies confirmed that KIAA1363 regulates this pathway by hydrolyzing the metabolic intermediate 2-acetyl monoalkylglycerol. Inactivation of KIAA1363 disrupted ether lipid metabolism in cancer cells and impaired cell migration and tumor growth in vivo. The integrated molecular profiling method described herein should facilitate the functional annotation of metabolic enzymes in any living system.

subject areas

  • Carbamates
  • Carboxylic Ester Hydrolases
  • Cell Line, Tumor
  • Chromatography, High Pressure Liquid
  • Enzyme Activation
  • Enzyme Inhibitors
  • Female
  • Humans
  • Ketones
  • Lysophospholipids
  • Ovarian Neoplasms
  • Phospholipid Ethers
  • Platelet Activating Factor
  • RNA Interference
  • Sensitivity and Specificity
  • Signal Transduction
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Identity

International Standard Serial Number (ISSN)

  • 1074-5521

Digital Object Identifier (DOI)

  • 10.1016/j.chembiol.2006.08.008

PubMed ID

  • 17052608
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Additional Document Info

start page

  • 1041

end page

  • 1050

volume

  • 13

issue

  • 10

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