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. 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. 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. Ex vivo incubation of rat soleus muscles induced a marked and concomitant rise in the mRNA levels of GLUT-1 and GRP-78. transmembrane helices 3 and 4 and transmembrane helices 6. The mRNA for GLUT-1 was augmented by 50-300% in a time-dependent manner, similarly to the changes in GRP-78 mRNA. GLUT1 2 is present in red blood cells and epithelial cells, for example, in the bloodbrain. 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. We therefore hypothesized that GLUT-1 may be a glucose-regulated stress protein. Results: The transcription level of GLUT1 was significantly higher in the BC samples than in the normal tissues, whereas the levels of GLUT3 and GLUT4 were. Another family of proteins, glucose-regulated proteins (GRPs), is also ubiquitously expressed and stimulated by glucose deprivation and other cellular stresses. GLUT-1 is negatively regulated by glucose. On the other hand, GLUT2 has a low affinity for glucose with its Km of about 1520 mM glucose. Consequently, the functions of these transporters align with the physiological concentration of glucose of about 5 mM. The test should be performed in the post-absorptive state 4-6 hours after eating. GLUTs 1, 3, and 4 are transporters that have high affinity for glucose ranging in Km of 25 mM glucose. More than 100 different types of mutations and. Glut1 is the principal transporter of glucose, the primary source of energy, across the blood-brain barrier. It is caused by a mutation in the SLC2A1 gene, which regulates the glucose transporter protein type 1 (Glut1). Bei der Regulation der Glucoseaufnahme sowie der Expression von GLUT-1 ist offensichtlich GSK-3 involviert, via Modulation durch TSC2 und mTOR. GLUT-1 wird in mehreren Krebszelllinien überexprimiert. The reason for this coexpression is not clear. De Vivo Disease glucose transporter protein syndrome Glut1 deficiency. Glut1 Deficiency is a rare genetic condition that impairs brain metabolism. Results: GLUT1 was variably expressed in 38 of hepatic EHE (3/8) and 50 of hepatic angiosarcoma cases (2/4), but in none of the cavernous hemangioma. Varianten von GLUT-1 sind assoziiert mit diabetischer Nephropathie bei Diabetes mellitus. However, the rat brain/HepG2/erythrocyte-type glucose transporter GLUT-1 is expressed at low levels in most cells. In mammals, glucose transport is mediated by five structurally related glucose transporters that show a characteristic cell-specific expression.
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