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Am J Physiol Cell Physiol 278: C1172-C1182, 2000;
0363-6143/00 $5.00
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Vol. 278, Issue 6, C1172-C1182, June 2000

150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cells

Yoshio Bando1,2, Satoshi Ogawa1,2, Atsushi Yamauchi3, Keisuke Kuwabara4, Kentaro Ozawa1,2, Osamu Hori1,2, Hideki Yanagi5, Michio Tamatani1,2, and Masaya Tohyama1,2

1 Department of Anatomy and Neuroscience and 4 First Department of Medicine, Osaka University Graduate School of Medicine, Suita City 565-0871; 3 Division of Nephrology, Department of Medicine, Osaka Rosai Hospital, Sakai, Osaka 591-8025; 5 HSP Research Institute, Kyoto Research Park, Shimogyo-Ku, Kyoto 600-8813; and 2 Core Research for Evolutional Science and Technology, Japan Science and Technology, Kawaguchi City 332-0012, Japan

To assess the participation of the 150-kDa oxygen-regulated protein (ORP150) in protein transport, its function in Madin-Darby canine kidney (MDCK) cells was studied. Exposure of MDCK cells to hypoxia resulted in an increase of ORP150 antigen and increased binding of ORP150 to GP80/clusterin (80-kDa glycoprotein), a natural secretory protein in this cell line. In ORP150 antisense transformant MDCK cells, GP80 was retained within the endoplasmic reticulum after exposure to hypoxia. Metabolic labeling showed the delay of GP80 maturation in antisense transformants in hypoxia, whereas its matured form was detected in wild-type cells, indicating a role of ORP150 in protein transport, especially in hypoxia. The affinity chromatographic analysis of ORP150 suggested its ability to bind to ATP-agarose. Furthermore, the ATP hydrolysis analysis showed that ORP150 can release GP80 at a lower ATP concentration. These data indicate that ORP150 may function as a unique molecular chaperone in renal epithelial cells by facilitating protein transport/maturation in an environment where less ATP is accessible.

hypoxia; energy metabolism; renal epithelium; ischemia; adenosine 5'-triphosphate kinetics


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