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(Received for publication, September 13, 1995, and in revised form, September 17, 1996)
From the In the rat, cytochrome P4501A1 gene expression is
thought to be regulated by several trans-acting factors
including the 4 S polycyclic aromatic hydrocarbon (PAH)-binding
protein. Phosphorylation and dephosphorylation have been suggested to
influence the function of many cytosolic receptors and transcription
factors. The ATP level within H4IIE rat hepatoma cells could be
depleted by treatment with sodium azide or 2,4-dinitrophenol;
restoration of the original ATP levels occurred with addition of
glucose to the cell culture. ATP depletion reduced the phosphate
content of the 4 S protein by ~25-30%, which lowered the binding of
benzo[a]pyrene (B[a]P) to the 4 S protein
by >60%. This effect could not be reversed by the addition of ATP to
the binding reaction mixtures. Alkaline phosphatase treatment of the
purified 4 S protein in a cell-free system also reduced the
B[a]P binding to the protein. Cells treated with a
protein phosphatase inhibitor, okadaic acid, and a protein kinase
inhibitor, staurosporin, affected the B[a]P binding of the 4 S protein positively and negatively, respectively,. These data
suggested that phosphorylation is involved in the interaction of the 4 S protein with the PAH. The nuclear translocation of the predominantly
cytosolic binding protein has been investigated after ligand binding.
Western blots with the immunopurified 4 S PAH-binding protein from
cytosolic and nuclear lysates showed significant differences in the
distribution of the 4 S receptor between cytosolic and nuclear
compartments in control and ATP-depleted cells. Ligand binding
stimulated the movement of the receptor into the nucleus, which was
completely blocked by reducing the intracellular ATP
concentration. These findings provide new information on the role of
ATP and phosphorylation on the interaction of B[a]P with
4 S PAH-binding protein and its nuclear translocation.
Volume 271, Number 51,
Issue of December 20, 1996
pp. 32551-32556
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Department of Pharmacology and Molecular
Toxicology, University of Massachusetts Medical Center,
Worcester, Massachusetts 01655, § Department of
Biochemistry, Vanderbilt University School of Medicine,
Nashville, Tennessee 37232, and ¶ Department of Physiology,
Dartmouth Medical School, Hanover, New Hampshire 03756
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