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Am J Physiol Lung Cell Mol Physiol (November 30, 2001). doi:10.1152/ajplung.00359.2001
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Articles in PresS, published online ahead of print November 30, 2001
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00359.2001
Submitted on September 7, 2001
Accepted on November 27, 2001

Identification of protein disulfide isomerase as an endothelial hypoxic stress protein

Krista K Graven1*, Christopher Molvar2, Jill S Roncarati2, Brian D Klahn1, Shawna Lowrey1, and Harrison W Farber2

1 Medicine, University of Wisconsin Medical School, Madison, WI, USA
2 Pulmonary Center, Boston University School of Medicine, Boston, MA, USA

* To whom correspondence should be addressed. E-mail: kkg{at}medicine.wisc.edu.

Endothelial cells (EC) exposed to hypoxia upregulate a unique set of five stress proteins. These proteins are upregulated in human and bovine aortic and pulmonary artery EC and are distinct from heat shock or glucose-regulated proteins. We previously identified two of these proteins as the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase and enolase, and postulated that the remaining proteins were also glycolytic enzymes. We report here the identification of the 56 kD protein as protein disulfide isomerase (PDI) using SDS-polyacrylamide gel electrophoresis, tryptic digestion and N-terminal amino acid sequencing. PDI is upregulated by hypoxia at the mRNA level and follows a similar time course to that of the protein, with maximal upregulation detected after exposure to 18 hours of 0%O2. Neither smooth muscle cells or fibroblasts upregulate PDI to the same extent as EC which correlates with their decreased hypoxia tolerance. Upregulation of PDI specifically in EC may contribute to their ability to tolerate hypoxia and may occur through PDI's functions as a prolyl hydroxylase subunit, protein folding catalyst or molecular chaperone.




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