| 150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cells. | |
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MedLine Citation:
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PMID: 10837345 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Y Bando; S Ogawa; A Yamauchi; K Kuwabara; K Ozawa; O Hori; H Yanagi; M Tamatani; M Tohyama |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: American journal of physiology. Cell physiology Volume: 278 ISSN: 0363-6143 ISO Abbreviation: Am. J. Physiol., Cell Physiol. Publication Date: 2000 Jun |
Date Detail:
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Created Date: 2000-07-18 Completed Date: 2000-07-18 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 100901225 Medline TA: Am J Physiol Cell Physiol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: C1172-82 Citation Subset: IM |
Affiliation:
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Department of Anatomy and Neuroscience, Osaka University Graduate School of Medicine, Suita City, Japan. ybando@anat2.med.osaka-u.ac.jp |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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metabolism Animals Cell Hypoxia / physiology* Cell Line Cell Survival Clusterin Dogs Energy Metabolism Glycoproteins / metabolism Humans Kidney Membrane Glycoproteins / metabolism Molecular Chaperones / physiology* Oligodeoxyribonucleotides, Antisense / pharmacology Proteins / genetics, physiology* Receptors, Interleukin-6 Recombinant Proteins / metabolism Transfection |
| Chemical | |
Reg. No./Substance:
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0/CLU protein, human; 0/Clusterin; 0/Glycoproteins; 0/IL6R protein, human; 0/Membrane Glycoproteins; 0/Molecular Chaperones; 0/Oligodeoxyribonucleotides, Antisense; 0/Proteins; 0/Receptors, Interleukin-6; 0/Recombinant Proteins; 0/oxygen-regulated proteins; 56-65-5/Adenosine Triphosphate |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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