Regulation and Function of Aquaporin-1 in Glioma Cells
Glioblastoma multiformes (GBMs) express increased aquaporin (AQP) 1 compared to normal brain. AQPs may contribute to edema, cell motility, shuttling of H2O and H+ from intracellular to extracellular space. We sought to gain insight into AQPs function in GBM. In cultured 9L gliosarcoma cells, AQPs e...
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2007-09-01
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doaj-a2b370578e4444059330ae066ce2bb312020-11-24T22:58:17ZengElsevierNeoplasia: An International Journal for Oncology Research1476-55861522-80022007-09-019977778710.1593/neo.07454Regulation and Function of Aquaporin-1 in Glioma CellsYasuhiko Hayashi0Nancy A. Edwards1Martin A. Proescholdt2Edward H. Oldfield3Marsha J. Merrill4Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USASurgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USADepartment of Neurosurgery, University of Regensburg, Regensburg 93053, GermanySurgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USASurgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA Glioblastoma multiformes (GBMs) express increased aquaporin (AQP) 1 compared to normal brain. AQPs may contribute to edema, cell motility, shuttling of H2O and H+ from intracellular to extracellular space. We sought to gain insight into AQPs function in GBM. In cultured 9L gliosarcoma cells, AQPs expression was induced by dexamethasone, platelet-derived growth factor, NaCl, hypoxia, D-glucose (but not L-glucose), fructose. Induction of AQPs expression correlated with the level of glycolysis, maximized by increasing medium D-glucose or fructose and decreasing O2, was quantified by measuring lactate dehydrogenase (LDH) activity and medium lactate concentration. Upregulation of the protease cathepsin B was also observed in 9L cells cultured under glycolytic conditions. Immunohistochemical staining of human GBM specimens revealed increased coincident expression of AQPs, LDH, cathepsin B in glioma cells associated with blood vessels at the tumor periphery. GBMs are known to exhibit aerobic glycolysis. Increased glucose metabolism at the tumor periphery may provide a scenario by which upregulation of AQPs, LDH, cathepsin B contributes to acidification of the extracellular milieu and to invasive potential of glioma cells in perivascular space. The specific upregulation and metabolic consequences of increased AQPs in gliomas may provide a therapeutic target, both as a cell surface marker and as a functional intervention. http://www.sciencedirect.com/science/article/pii/S1476558607800376Aquaporincathepsin Bgliomaglycolysisinvasion |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yasuhiko Hayashi Nancy A. Edwards Martin A. Proescholdt Edward H. Oldfield Marsha J. Merrill |
spellingShingle |
Yasuhiko Hayashi Nancy A. Edwards Martin A. Proescholdt Edward H. Oldfield Marsha J. Merrill Regulation and Function of Aquaporin-1 in Glioma Cells Neoplasia: An International Journal for Oncology Research Aquaporin cathepsin B glioma glycolysis invasion |
author_facet |
Yasuhiko Hayashi Nancy A. Edwards Martin A. Proescholdt Edward H. Oldfield Marsha J. Merrill |
author_sort |
Yasuhiko Hayashi |
title |
Regulation and Function of Aquaporin-1 in Glioma Cells |
title_short |
Regulation and Function of Aquaporin-1 in Glioma Cells |
title_full |
Regulation and Function of Aquaporin-1 in Glioma Cells |
title_fullStr |
Regulation and Function of Aquaporin-1 in Glioma Cells |
title_full_unstemmed |
Regulation and Function of Aquaporin-1 in Glioma Cells |
title_sort |
regulation and function of aquaporin-1 in glioma cells |
publisher |
Elsevier |
series |
Neoplasia: An International Journal for Oncology Research |
issn |
1476-5586 1522-8002 |
publishDate |
2007-09-01 |
description |
Glioblastoma multiformes (GBMs) express increased aquaporin (AQP) 1 compared to normal brain. AQPs may contribute to edema, cell motility, shuttling of H2O and H+ from intracellular to extracellular space. We sought to gain insight into AQPs function in GBM. In cultured 9L gliosarcoma cells, AQPs expression was induced by dexamethasone, platelet-derived growth factor, NaCl, hypoxia, D-glucose (but not L-glucose), fructose. Induction of AQPs expression correlated with the level of glycolysis, maximized by increasing medium D-glucose or fructose and decreasing O2, was quantified by measuring lactate dehydrogenase (LDH) activity and medium lactate concentration. Upregulation of the protease cathepsin B was also observed in 9L cells cultured under glycolytic conditions. Immunohistochemical staining of human GBM specimens revealed increased coincident expression of AQPs, LDH, cathepsin B in glioma cells associated with blood vessels at the tumor periphery. GBMs are known to exhibit aerobic glycolysis. Increased glucose metabolism at the tumor periphery may provide a scenario by which upregulation of AQPs, LDH, cathepsin B contributes to acidification of the extracellular milieu and to invasive potential of glioma cells in perivascular space. The specific upregulation and metabolic consequences of increased AQPs in gliomas may provide a therapeutic target, both as a cell surface marker and as a functional intervention.
|
topic |
Aquaporin cathepsin B glioma glycolysis invasion |
url |
http://www.sciencedirect.com/science/article/pii/S1476558607800376 |
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