Metabolic enzyme diversity in different human thyroid cell lines and their sensitivity to gravitational forces.

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  • Additional Information
    • Source:
      Publisher: Wiley-VCH Country of Publication: Germany NLM ID: 101092707 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1615-9861 (Electronic) Linking ISSN: 16159853 NLM ISO Abbreviation: Proteomics Subsets: MEDLINE
    • Publication Information:
      Original Publication: Weinheim, Germany : Wiley-VCH,
    • Subject Terms:
      Gravitation*; Enzymes/*metabolism ; Thyroid Gland/*cytology ; Thyroid Gland/*enzymology; Animals ; Blotting, Western ; Cell Line ; Culture Media/chemistry ; Flow Cytometry ; Fluorescent Antibody Technique ; Glycolysis ; Humans ; Mice ; Oxygen/metabolism ; Phosphopyruvate Hydratase/metabolism ; Protein Transport ; Time Factors ; Triose-Phosphate Isomerase/metabolism
    • Abstract:
      Many cancer cells show unique protein expression patterns. We used proteome technology including MS, free flow isoelectric focusing and Western blotting to determine current concentrations of metabolic enzymes in healthy and malignant human thyroid cells. Three different types of human thyroid cells were investigated after they had been cultured under equal conditions. MS revealed high quantities of glycolytic enzymes and moderate quantities of citric acid cycle enzymes in malignant FTC-133 cells with abnormal LDH B-chains, high quantities of glycolytic enzymes and marginal quantities of citric acid cycle enzymes in normal HTU-5 cells, and low quantities of glycolytic enzymes and marginal quantities of citrate cycle enzymes in malignant CGTH-W1 cells with abnormal LDH A-chains. When an alteration of gene expression activity was challenged physically by removing gravity forces, the concentrations of various glycolytic enzymes were changed in normal and malignant thyroid cells. However, the changes varied among the different cell types. Different cellular alignment of the enzymes could be one reason for the cell type-specific behavior as demonstrated by histological analysis of alpha-enolase.
      (© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
    • Accession Number:
      0 (Culture Media)
      0 (Enzymes)
      EC 4.2.1.11 (Phosphopyruvate Hydratase)
      EC 5.3.1.1 (Triose-Phosphate Isomerase)
      S88TT14065 (Oxygen)
    • Publication Date:
      Date Created: 20120619 Date Completed: 20121226 Latest Revision: 20131121
    • Publication Date:
      20231215
    • Accession Number:
      10.1002/pmic.201200070
    • Accession Number:
      22707460