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    Glycine N-methyltransferase is an example of functional diversity. Role as a polycyclic aromatic hydrocarbon-binding receptor

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    Authors
    Bhat, Rashid
    Bresnick, Edward
    UMass Chan Affiliations
    Department of Pharmacology and Molecular Toxicology
    Document Type
    Journal Article
    Publication Date
    1997-08-22
    Keywords
    Animals
    Benzo(a)pyrene
    CHO Cells
    Cricetinae
    Cytochrome P-450 CYP1A1
    DNA-Binding Proteins
    Dimerization
    Enzyme Induction
    Gene Expression Regulation, Enzymologic
    Glycine N-Methyltransferase
    Methyltransferases
    Promoter Regions (Genetics)
    Protein Binding
    RNA, Messenger
    Rats
    Receptors, Aryl Hydrocarbon
    Receptors, Cytoplasmic and Nuclear
    Structure-Activity Relationship
    Tetrachlorodibenzodioxin
    Transcription, Genetic
    Transfection
    Life Sciences
    Medicine and Health Sciences
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    Metadata
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    Link to Full Text
    https://doi.org/10.1074/jbc.272.34.21221
    Abstract
    The cytochrome P-4501A1 (CYP1A1) gene is regulated by several trans-acting factors including the 4 S polycyclic aromatic hydrocarbon (PAH)-binding protein, which has recently been identified as glycine N-methyltransferase (GNMT) (Raha, A., Wagner, C., Macdonald, R. G., and Bresnick, E. (1994) J. Biol. Chem. 269, 5750-5756). The role of GNMT as a 4 S PAH-binding protein in mediating the induction of cytochrome P-4501A1 has been investigated further. GNMT cDNA, which was cloned into a pMAMneo vector containing the Rous sarcoma virus promoter and the neomycin resistance gene, was stably transfected into D422 Chinese hamster ovary (CHO) cells. Several positive clones were selected by reverse transcription-polymerase chain reaction and assayed for the expression of recombinant protein. Western blot analysis indicated the expression of significant levels of the 4 S protein in the stably transfected CHO cells (CHO-GNMT). Cytosolic preparations from the CHO-GNMT showed high benzo[a]pyrene (B[a]P) binding but no 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) binding activity when compared with clones transfected with the pMAMneo vector alone (CHO-neo) or the parental CHO cells. Challanging the CHO-GNMT cells with 4 microM B[a]P resulted in elevated levels of CYP1A1 mRNA. Equally effective in inducing CYP1A1 mRNA were benzo[e]pyrene and 3-methylcholanthrene. On the other hand, TCDD did not induce CYP1A1 gene expression in these cells. B[a]P-treated CHO-GNMT, expressing the 4 S protein, also showed CYP1A1 protein by Western blotting and exhibited ethoxyresorufin-O-deethylase activity; neither the CHO-neo or parental CHO cells were positive for any of these measures. No Ah receptor message or protein was detectable in the parental CHO, CHO-neo, or CHO-GNMT cells. Furthermore, no XRE binding activity was observed in TCDD-treated cytosolic preparations or nuclear extracts from CHO-GNMT cells that were treated with TCDD. These studies unequivocally establish that GNMT is a PAH-binding protein that can mediate the induction of CYP1A1 by PAHs such as B[a]P through an Ah receptor-independent pathway.
    Source

    J Biol Chem. 1997 Aug 22;272(34):21221-6.

    DOI
    10.1074/jbc.272.34.21221
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/42438
    PubMed ID
    9261130
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.272.34.21221
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