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

• Published in: British journal of cancer Vol. 64; no. 1; pp. 69 - 73
• Main Authors: MURPHY, B. J, LADEROUTE, K. R, SHORT, S. M, SUTHERLAND, R. M
• Format: Journal Article
• Language: English
• Published: Basingstoke Nature Publishing Group 01.07.1991
• Subjects: Aerobiosis; Animals; Base Sequence; Biological and medical sciences; Blotting, Northern; Blotting, Western; Cell Line; Cell physiology; Cricetinae; Cricetulus; Effects of physical and chemical agents; Electrophoresis, Gel, Two-Dimensional; Female; Fundamental and applied biological sciences. Psychology; Heme Oxygenase (Decyclizing) - biosynthesis; Heme Oxygenase (Decyclizing) - genetics; Heme Oxygenase (Decyclizing) - isolation & purification; Humans; Hypoxia; Molecular and cellular biology; Molecular Sequence Data; Ovary; RNA, Messenger - analysis; RNA, Messenger - genetics; Oxygenase; Proteins; Vertebrata; Mammalia; Enzyme; Animal; Rodentia; Heme; Hypoxia; Hamster; CHO cell line; Stress
• ISSN: 0007-0920; 1532-1827
• DOI: 10.1038/bjc.1991.241

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.