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J Biol Chem, Vol. 273, Issue 31, 19834-19839, July 31, 1998
From the Department of Cellular and Molecular Physiology,
University of Cincinnati College of Medicine,
Cincinnati, Ohio 45267-0576
To investigate signaling mechanisms by which
hypoxia regulates gene expression, we examined the effect of hypoxia on
the cyclic AMP response element-binding protein (CREB) in PC12 cells.
Exposure to physiological levels of hypoxia (5% O2,
~50 mm Hg) rapidly induced a persistent phosphorylation of CREB on
Ser133, an event that is required for CREB-mediated
transcriptional activation. Hypoxia-induced phosphorylation of CREB was
more robust than that induced by any other stimulus tested, including
forskolin, depolarization, and osmotic stress. Furthermore, this effect
was not mediated by any of the previously known signaling pathways that
lead to phosphorylation of CREB, including protein kinase A,
calcium/calmodulin-dependent protein kinase, protein kinase C,
ribosomal S6 kinase-2, and mitogen-activated protein kinase-activated protein kinase-2. Hypoxic activation of a CRE-containing reporter (derived from the 5'-flanking region of the tyrosine hydroxylase gene)
was attenuated markedly by mutation of the CRE. Thus, a physiological
reduction in O2 levels induces a functional phosphorylation of CREB at Ser133 via a novel signaling pathway.
Hypoxia Induces Phosphorylation of the Cyclic AMP Response
Element-binding Protein by a Novel Signaling Mechanism
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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