The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells.

Abstract

Chronic hypoxia increases the expression of a set of stress proteins (oxygen regulated proteins or ORPs) which is implicated in the development of drug resistance and radiation sensitivity in tumour cells. Five major ORPs have been documented, and two, ORP 80 and ORP 100, are considered to be identical to the glucose regulated stress proteins GRP78 and GRP94, respectively. We report here that ORP 33 is a form of the heme catabolic enzyme, heme oxygenase, using evidence obtained from northern blotting, two-dimensional polyacrylamide gel electrophoresis and western analysis. Heme oxygenase is believed to be an important component of the cellular response to oxidative stress. The significance of heme oxygenase as a hypoxia-induced stress protein is discussed.

• Authors: B J Murphy, K R Laderoute, S M Short, R M Sutherland
• Journal: British journal of cancer (Br J Cancer) Vol. 64 Issue 1 Pg. 69-73 (Jul 1991) ISSN: 0007-0920 [Print] England
• PMID: 1854629 (Publication Type: Journal Article)

Chemical References

• Endoplasmic Reticulum Chaperone BiP
• HSPA5 protein, human
• RNA, Messenger
• Heme Oxygenase (Decyclizing)

Topics

• Aerobiosis
• Animals
• Base Sequence
• Blotting, Northern
• Blotting, Western
• Cell Line
• Cricetinae
• Cricetulus
• Electrophoresis, Gel, Two-Dimensional
• Endoplasmic Reticulum Chaperone BiP
• Female
• Heme Oxygenase (Decyclizing) (biosynthesis, genetics, isolation & purification)
• Humans
• Hypoxia
• Molecular Sequence Data
• Ovary
• RNA, Messenger (analysis, genetics)