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© 1990 Oxford University Press

other

The 4S polycyclic aromatic hydrocarbon-binding protein: immunohistochemical localization in mice

P. Gek Forkert 1 3, Hugh A. Barton 2 4, Maria G. Costantini 2 5 and Michael A. Marletta 2

1Department of Anatomy and Medicine, Queen'd University Kingston, Ontario, Canada K7L 3N6
2College of Pharmacy and Department of Biological Chemistry, School of Medicine, University of Michigan Ann Arbor, MI 48109-1065, USA

3To whom correspondence should be addressed at the Department of Anatomy

4Present address: ENSR Consulting and Engineering, 35 Nagog Park, Acton, MA 01720, USA

5Present address: Health Effects Institute, 215 First Street, Cambridge, MA 02142, USA

The 4S polycyclic aromatic hydrocarbon (PAH)-binding protein (PBP) is a cytoplasmic protein that binds PAHs with specificity and high affinity. We have used antisera for the PBP and unlabeled peroxidase anti-peroxidase immunohistochemistry to demonstrate its possible localization in cell types known to have xenobiotic metabolizing capabilities. Cellular sites of the PBP in liver, lung and kidney of C57BL/6 and DBA/2 mice were probed. The PBP was visualized in hepatocytes throughout the liver lobule and was not preferentially located in either centrilobular or periportal areas. However, cellular heterogeneity with respect to PBP content was clearly evident in the hepatocyte population. The positive reactivity correlated with substantial levels of benzo[a]pyrene (B[a]P) binding in liver cytosol. In the lung, the PBP was found in the bronchiolar epithelium and the alveolar septa, and was localized in ciliated and non-ciliated Clara and alveolar type II cells as well as in alveolar macrophages. In the kidney, the glomeruli and epithelia of proximal and distal convoluted tubules and collecting ducts were labeled. Staining for the PBP was greatest in the apical region of the pyramid and was localized in the epithelial lining of the collecting ducts. Relatively lower levels of the PBP were detected in the lung and kidney than in the liver. Staining was localized in the cytoplasmic compartment of cells in all tissues examined. Similar immunoreactivities were exhibited in the tissues of both C57BL/6 and DBA/2 mice. Treatment with ß-naphthoflavone ßNF) altered neither the intensity nor pattern of immuno-staining. Furthermore, treatment with ßNF or isosafrole has no effect on the Kd and Bmax of B[a]P binding to liver cytosolic PBP. The results of our experiments demonstrate localization of the PBP to sites of active physiological response to PAH exposure.


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