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Volume 271, Number 44, Issue of November 1, 1996 pp. 27292-27298
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Biochemical Effects of Retinoic Acid on GTP-binding Protein/Transglutaminases in HeLa Cells
STIMULATION OF GTP-BINDING AND TRANSGLUTAMINASE ACTIVITY, MEMBRANE ASSOCIATION, AND PHOSPHATIDYLINOSITOL LIPID TURNOVER

(Received for publication, June 28, 1996)

From the Department of Pharmacology, Veterinary Medical Center, Cornell University, Ithaca, New York 14853

Treatment of HeLa cells with retinoic acid (RA) gives rise to a marked stimulation in the incorporation of [-³²P]GTP into an ~87-kDa cytosolic protein that cross-reacts with a monoclonal antibody raised against tissue transglutaminases. In the absence of RA treatment, the transglutaminase immunoreactivity elutes from a gel filtration column with an apparent size of ~600 kDa (designated TGa), whereas following RA treatment, a second peak of transglutaminase immunoreactivity (designated TGb) is detected with an apparent size of ~150 kDa. The TGa fractions show little or no GTP-binding or GTP hydrolytic activity and very little transglutaminase activity. However, the TGb fractions show all three activities. Retinoic acid treatment also promotes the association of the GTP-binding protein/transglutaminase with membrane fractions, as detected by Western blotting and photoaffinity cross-linking with [-³²P]GTP. In addition, the TGb fraction shows a markedly enhanced ability (relative to TGa) to associate with membranes from control (non-RA-treated) cells. The ability of the GTP-binding protein/transglutaminase to bind to membranes is correlated with the stimulation of a membrane-associated phospholipase C activity. Thus, these findings indicate that RA treatment results in a number of changes in the biochemical properties of a GTP-binding protein/transglutaminase which strongly enhance its ability to bind GTP, associate with plasma membranes, and stimulate phosphoinositide lipid turnover.

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