ArticleBiochimie2012
Nitroxyl (HNO) acutely activates the glucose uptake activity of GLUT1.
Article in Biochimie, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- The protective role of endothelial GLUT1 in ischemic stroke.Brain and behavior · 2024Review
- The Chemical Biology of NO that Regulates Oncogenic Signaling and Metabolism: NOS2 and Its Role in Inflammatory Disease.Critical reviews in oncogenesis · 2023Review
- Caffeine inhibition of GLUT1 is dependent on the activation state of the transporter.Biochimie · 2017Article
- The chemical biology of HNO signaling.Archives of biochemistry and biophysics · 2017Review
- Thiol-Activated HNO Release from a Ruthenium Antiangiogenesis Complex and HIF-1α Inhibition for Cancer Therapy.ACS chemical biology · 2016Article
- Determination of GLUT1 Oligomerization Parameters using Bioluminescent Förster Resonance Energy Transfer.Scientific reports · 2016Article
- Curcumin directly inhibits the transport activity of GLUT1.Biochimie · 2016Article
- Deletion of thioredoxin-interacting protein improves cardiac inotropic reserve in the streptozotocin-induced diabetic heart.American journal of physiology. Heart and circulatory physiology · 2016Article
- Osthole activates glucose uptake but blocks full activation in L929 fibroblast cells, and inhibits uptake in HCLE cells.Life sciences · 2014Article
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- Differential regulation of GLUT1 activity in human corneal limbal epithelial cells and fibroblasts.Biochimie · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Nitroxyl (HNO) is a molecule of significant interest due to its unique pharmacological properties, particularly within the cardiovascular system. A large portion of HNO biological effects can be attributed to its reactivity with protein thiols, where it can generate disulfide bonds. Evidence from studies in erythrocytes suggests that the activity of GLUT1 is enhanced by the formation of an internal disulfide bond. However, there are no reports that document the effects of HNO on glucose uptake. Therefore, we examined the acute effects of Angeli's salt (AS), a HNO donor, on glucose uptake activity of GLUT1 in L929 fibroblast cells. We report that AS stimulates glucose uptake with a maximum effective concentration of 5.0 mM. An initial 7.2-fold increase occurs within 2 min, which decreases and plateaus to a 4.0-fold activation after 10 min. About 60% of the 4.0-fold activation recovers within 10 min, and 40% remains after an hour. The activation is blocked by the pretreatment of cells with thiol-reactive compounds, iodoacetamide (0.75 mM), cinnamaldehyde (2.0 mM), and phenylarsine oxide (10 μM). The effects of AS are not additive to the stimulatory effects of other acute activators of glucose uptake in L929 cells, such as azide (5 mM), berberine (50 μM), or glucose deprivation. These data suggest that GLUT1 is acutely activated in L929 cells by the formation of a disulfide bond, likely within GLUT1 itself.
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