scholarly journals Inhibiting cancer metabolism by aromatic carbohydrate amphiphiles that act as antagonists of the glucose transporter GLUT1

2020 ◽  
Vol 11 (14) ◽  
pp. 3737-3744 ◽  
Author(s):  
Alexandra Brito ◽  
Patrícia M. R. Pereira ◽  
Diana Soares da Costa ◽  
Rui L. Reis ◽  
Rein V. Ulijn ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Self Assembly ◽  
Cancer Metabolism ◽  
Glucose Transporter ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1

We report on aromatic N-glucosides that inhibit selectively the cancer metabolism via two coexistent mechanisms: by deprivation of the glucose uptake through blocking of GLUT1 and by formation of sequestering nanonet through biocatalytic self-assembly.

scholarly journals Rosiglitazone enhances glucose uptake in glomerular podocytes using the glucose transporter GLUT1

Diabetologia ◽  
2009 ◽  
Vol 52 (9) ◽  
pp. 1944-1952 ◽  
Author(s):  
R. Lennon ◽  
G. I. Welsh ◽  
A. Singh ◽  
S. C. Satchell ◽  
R. J. Coward ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Glucose Transporter ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1

scholarly journals DHHC9-mediated GLUT1 S-palmitoylation promotes glioblastoma glycolysis and tumorigenesis

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Zhenxing Zhang ◽  
Xin Li ◽  
Fan Yang ◽  
Chao Chen ◽  
Ping Liu ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Plasma Membrane ◽  
Glucose Uptake ◽  
Posttranslational Modification ◽  
Poor Prognosis ◽  
Glucose Transporter ◽  
Transmembrane Protein ◽  
Glucose Supply ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1

AbstractGlucose transporter GLUT1 is a transmembrane protein responsible for the uptake of glucose into the cells of many tissues through facilitative diffusion. Plasma membrane (PM) localization is essential for glucose uptake by GLUT1. However, the mechanism underlying GLUT1 PM localization remains enigmatic. We find that GLUT1 is palmitoylated at Cys207, and S-palmitoylation is required for maintaining GLUT1 PM localization. Furthermore, we identify DHHC9 as the palmitoyl transferase responsible for this critical posttranslational modification. Knockout of DHHC9 or mutation of GLUT1 Cys207 to serine abrogates palmitoylation and PM distribution of GLUT1, and impairs glycolysis, cell proliferation, and glioblastoma (GBM) tumorigenesis. In addition, DHHC9 expression positively correlates with GLUT1 PM localization in GBM specimens and indicates a poor prognosis in GBM patients. These findings underscore that DHHC9-mediated GLUT1 S-palmitoylation is critical for glucose supply during GBM tumorigenesis.

Polymorphisms of the glucose transporter (GLUT1) gene are associated with diabetic nephropathy

2001 ◽  
Vol 59 (3) ◽  
pp. 985-989 ◽  
Author(s):  
Andrea D. Hodgkinson ◽  
Beverley A. Millward ◽  
Andrew G. Demaine
Keyword(s):  
Diabetic Nephropathy ◽  
Glucose Transporter ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1 ◽  
Glut1 Gene

scholarly journals LncRNA HOTAIR regulates glucose transporter Glut1 expression and glucose uptake in macrophages during inflammation

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Monira Obaid ◽  
S. M. Nashir Udden ◽  
Prasanna Alluri ◽  
Subhrangsu S. Mandal
Keyword(s):  
Immune Response ◽  
Glucose Metabolism ◽  
Glucose Uptake ◽  
Immune Cells ◽  
Glucose Transporter ◽  
Energy Needs ◽  
Glut1 Expression ◽  
Lncrna Hotair ◽  
Upstream Regulators ◽  
Glucose Transporter Glut1

AbstractInflammation plays central roles in the immune response. Inflammatory response normally requires higher energy and therefore is associated with glucose metabolism. Our recent study demonstrates that lncRNA HOTAIR plays key roles in NF-kB activation, cytokine expression, and inflammation. Here, we investigated if HOTAIR plays any role in the regulation of glucose metabolism in immune cells during inflammation. Our results demonstrate that LPS-induced inflammation induces the expression of glucose transporter isoform 1 (Glut1) which controls the glucose uptake in macrophages. LPS-induced Glut1 expression is regulated via NF-kB activation. Importantly, siRNA-mediated knockdown of HOTAIR suppressed the LPS-induced expression of Glut1 suggesting key roles of HOTAIR in LPS-induced Glut1 expression in macrophage. HOTAIR induces NF-kB activation, which in turn increases Glut1 expression in response to LPS. We also found that HOTAIR regulates glucose uptake in macrophages during LPS-induced inflammation and its knockdown decreases LPS-induced increased glucose uptake. HOTAIR also regulates other upstream regulators of glucose metabolism such as PTEN and HIF1α, suggesting its multimodal functions in glucose metabolism. Overall, our study demonstrated that lncRNA HOTAIR plays key roles in LPS-induced Glut1 expression and glucose uptake by activating NF-kB and hence HOTAIR regulates metabolic programming in immune cells potentially to meet the energy needs during the immune response.

scholarly journals Paroxysmal exercise-induced dyskinesia and epilepsy is due to mutations in SLC2A1, encoding the glucose transporter GLUT1

Brain ◽  
2008 ◽  
Vol 131 (7) ◽  
pp. 1831-1844 ◽  
Author(s):  
A. Suls ◽  
P. Dedeken ◽  
K. Goffin ◽  
H. Van Esch ◽  
P. Dupont ◽  
...  
Keyword(s):  
Glucose Transporter ◽  
Exercise Induced ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1

scholarly journals Monosomy-3 Alters the Expression Profile of the Glucose Transporters GLUT1-3 in Uveal Melanoma

2020 ◽  
Vol 21 (24) ◽  
pp. 9345
Author(s):  
Tjorge Maaßen ◽  
Siranush Vardanyan ◽  
Anton Brosig ◽  
Hartmut Merz ◽  
Mahdy Ranjbar ◽  
...  
Keyword(s):  
Uveal Melanoma ◽  
Glucose Transporter ◽  
Glucose Transporters ◽  
Clinical Factors ◽  
Gene Encoding ◽  
Primary Tumors ◽  
High Affinity ◽  
Monosomy 3 ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1

Monosomy-3 in uveal melanoma (UM) cells increases the risk of fatal metastases. The gene encoding the low-affinity glucose transporter GLUT2 resides on chromosome 3q26.2. Here, we analyzed the expression of the glucose transporters GLUT1, GLUT2, and GLUT3 with regard to the histological and clinical factors by performing immunohistochemistry on the primary tumors of n = 33 UM patients. UMs with monosomy-3 exhibited a 57% lower immunoreactivity for GLUT2 and a 1.8×-fold higher ratio of GLUT1 to total GLUT1-3. The combined levels of GLUT1-3 proteins were reduced in the irradiated but not the non-irradiated tumors with monosomy-3. GLUT3 expression was stronger in the irradiated samples with disomy-3 versus monosomy-3, but the ratio of the GLUT3 isoform to total GLUT1-3 did not differ with regard to the monosomy-3 status in the irradiated or non-irradiated subgroups. Systemic metastases were associated with the presence of monosomy-3 in the primary and circulating tumor cells as well as a higher GLUT1 ratio. Upregulation of the high-affinity glucose transporter GLUT1 possibly as a compensation for the low-affinity isoform GLUT2 may be enhancing the basal glucose uptake in the UM cells with monosomy-3. Prevention of hyperglycemia might, therefore, be a valuable approach to delay the lethal UM metastases.

Sign in / Sign up

Export Citation Format

Share Document