The ubiquitous glucose transporter GLUT-1 belongs to the glucose-regulated protein family of stress-inducible proteins.
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- E Wertheimer
- Department of Endocrinology and Metabolism, Hebrew University-Hadassah Medical Center, Jerusalem, Israel.
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- S Sasson
- Department of Endocrinology and Metabolism, Hebrew University-Hadassah Medical Center, Jerusalem, Israel.
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- E Cerasi
- Department of Endocrinology and Metabolism, Hebrew University-Hadassah Medical Center, Jerusalem, Israel.
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- Y Ben-Neriah
- Department of Endocrinology and Metabolism, Hebrew University-Hadassah Medical Center, Jerusalem, Israel.
書誌事項
- 公開日
- 1991-03-15
- DOI
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- 10.1073/pnas.88.6.2525
- 公開者
- Proceedings of the National Academy of Sciences
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説明
<jats:p>In mammals, glucose transport is mediated by five structurally related glucose transporters that show a characteristic cell-specific expression. However, the rat brain/HepG2/erythrocyte-type glucose transporter GLUT-1 is expressed at low levels in most cells. The reason for this coexpression is not clear. GLUT-1 is negatively regulated by glucose. Another family of proteins, glucose-regulated proteins (GRPs), is also ubiquitously expressed and stimulated by glucose deprivation and other cellular stresses. We therefore hypothesized that GLUT-1 may be a glucose-regulated stress protein. This was tested by subjecting L8 myocytes and NIH 3T3 fibroblasts to glucose starvation or exposure to the calcium ionophore A23187, 2-mercaptoethanol, or tunicamycin, all known to increase GRP levels. The mRNA for GLUT-1 was augmented by 50-300% in a time-dependent manner, similarly to the changes in GRP-78 mRNA. Ex vivo incubation of rat soleus muscles induced a marked and concomitant rise in the mRNA levels of GLUT-1 and GRP-78. Finally, calcium ionophore A23187 and 2-mercaptoethanol induced a 2- to 3-fold increase in the levels of the GLUT-1 protein and hexose uptake. In all instances in which GRP-78 and GLUT-1 responded to stress, the transcription of the cell-specific muscle/adipocyte-type insulin-responsive glucose transporter (GLUT-4) did not change. Thus, despite the lack of structural similarity, GLUT-1 and GRP-78 expression is regulated similarly, whereas the regulation of GLUT-4, which is structurally related to GLUT-1, is different. We propose that GLUT-1 belongs to the GRP family of stress proteins and that its ubiquitous expression may serve a specific purpose during cellular stress.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 88 (6), 2525-2529, 1991-03-15
Proceedings of the National Academy of Sciences
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詳細情報 詳細情報について
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- CRID
- 1361699995176702208
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- NII論文ID
- 30016291194
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- NII書誌ID
- AA10808769
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- ISSN
- 10916490
- 00278424
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