Cloning, structure, and expression of a rat binding protein for polychlorinated biphenyls: Homology to the hormonally regulated progesterone-binding protein uteroglobin

Lena Nordlund-Möller, Olof Andersson, Ragnhild Ahlgren, James Schilling, Mikael Gillner, Jan Åke Gustafsson, Johan Lund

    Research output: Contribution to journalArticlepeer-review

    63 Scopus citations

    Abstract

    Certain metabolites of polychlorinated biphenyls (PCBs) are retained in the Clara cells and in the airway lumen of rodent lung due to their interaction with a secretory 13-kDa protein. Here, we report the isolation of a cDNA encoding the rat lung PCB-binding protein. The identity of the PCB-binding protein is supported by expression of the cDNA in Cos-1 cells where the homogenates from transfected cells show specific binding of 4,4′-bis([ 3H]methylsulfonyl)-2,2′,5,5′-tetrachlorobiphenyl, a high affinity ligand for the PCB-binding protein. Also a monospecific antiserum to the PCB-binding protein recognizes a 13-kDa protein in the homogenates of transfected cells but not in the corresponding fraction of mock-transfected cells. Northern blot analysis of total RNA from different rat tissues demonstrates that the cDNA detects a ∼600-base pair mRNA which appears to be solely expressed in lung. Interestingly, DNA sequence analysis and prediction of the amino acid sequence reveals that the PCB-binding protein shares 53% positional amino acid identity with uteroglobin, a progesterone-binding protein found in rabbit uterus and lung. Furthermore, amino acids shown by x-ray crystallography to delineate the central cavity of uteroglobin, which fits progesterone, are highly conserved in the two proteins.

    Original languageEnglish (US)
    Pages (from-to)12690-12693
    Number of pages4
    JournalJournal of Biological Chemistry
    Volume265
    Issue number21
    StatePublished - Jul 25 1990

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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