Hypoxia and CYP1A1 induction-dependent regulation of proteins involved in glucose utilization in Caco-2 cells.

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  • Additional Information
    • Source:
      Publisher: American Physiological Society Country of Publication: United States NLM ID: 0370511 Publication Model: Print Cited Medium: Print ISSN: 0002-9513 (Print) Linking ISSN: 00029513 NLM ISO Abbreviation: Am J Physiol Subsets: MEDLINE
    • Publication Information:
      Publication: Bethesda, MD : American Physiological Society
      Original Publication: Washington [etc.] American Physiological Society.
    • Subject Terms:
      Cell Hypoxia* ; Gene Expression Regulation*; Caco-2 Cells/*metabolism ; Cytochrome P-450 CYP1A1/*biosynthesis ; Glucose/*metabolism; Cobalt/pharmacology ; Cytochrome P-450 CYP1A1/genetics ; Enzyme Induction ; Glucose Transporter Type 1 ; Glycogen/metabolism ; Humans ; Lactic Acid/metabolism ; Monosaccharide Transport Proteins/genetics ; Monosaccharide Transport Proteins/metabolism ; RNA, Messenger/biosynthesis ; Signal Transduction ; Sucrase-Isomaltase Complex/genetics ; Sucrase-Isomaltase Complex/metabolism ; beta-Naphthoflavone/pharmacology
    • Abstract:
      Although induction of cytochrome P-450 1A1 (CYP1A1) in the Caco-2 clone TC7 alters glucose utilization and modifies the expression of sucrase-isomaltase (SI) and hexose transporters, nothing is known of the events that control these effects. In this study, we analyzed the effects of beta-naphthoflavone (beta-NF) and hypoxia on these parameters and expression of key enzymes of glucose metabolism. Both beta-NF and hypoxia induce similar changes: 1) induction of CYP1A1 mRNA; 2) increased glucose consumption and lactic acid production and lower glycogen content; 3) downregulation of SI and upregulation of GLUT1 mRNAs; 4) downregulation of fructose-1,6-bisphosphatase and pyruvate kinase mRNAs and upregulation of phosphoenolpyruvate carboxykinase, pyruvate dehydrogenase, lactate dehydrogenase, and phosphofructokinase mRNAs; and 5) upregulation of c-fos and c-jun mRNAs. Although addition of inhibitors of CYP1A1 catalytic activity to beta-NF-treated cells totally inhibits the enzyme activity, it does not modify CYP1A1 mRNA response and associated effects, thus excluding a direct role for the enzyme per se. These results point to a possible physiological implication of the signal-transduction pathway responsible for CYP1A1 induction.
    • Accession Number:
      0 (Glucose Transporter Type 1)
      0 (Monosaccharide Transport Proteins)
      0 (RNA, Messenger)
      0 (SLC2A1 protein, human)
      33X04XA5AT (Lactic Acid)
      3G0H8C9362 (Cobalt)
      6051-87-2 (beta-Naphthoflavone)
      9005-79-2 (Glycogen)
      EC 1.14.14.1 (Cytochrome P-450 CYP1A1)
      EC 3.2.1.- (Sucrase-Isomaltase Complex)
      EVS87XF13W (cobaltous chloride)
      IY9XDZ35W2 (Glucose)
    • Publication Date:
      Date Created: 19980808 Date Completed: 19980806 Latest Revision: 20190312
    • Publication Date:
      20240829
    • Accession Number:
      10.1152/ajpgi.1998.274.6.G1101
    • Accession Number:
      9696711