Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The sodium-independent GLUT1 glucose transporter is expressed in high density in human erythrocytes and in tissues which serve a barrier function. In the polarized endothelial cells of the brain capillaries, which comprise the blood-brain barrier (BBB), GLUT1 is expressed on both apical and basolateral membranes; however, in the epithelium of the choroid plexus, GLUT1 expression is restricted to the basolateral surface. The present study examined whether these differences in subcellular localization of GLUT1 at the BBB and choroid plexus could be correlated with differential N-linked or O-linked glycosylation of the protein. Western blot analysis of solubilized brain capillaries (BC) and choroid plexus (CP) revealed that while the BC GLUT1 had an average molecular mass identical to that of the purified human erythrocyte transporter (54 kDa), the CP GLUT1 was of lower molecular mass (47 kDa). Treatment of brain capillaries and choroid plexus with N-glycanase resulted in a shift in the mobility of the GLUT1 of both samples to a lower molecular mass of 42 kDa; however, in contrast, treatment with O-glycanase produced no change in the mobility patterns of GLUT1, but did result in O-linked deglycosylation of another BBB marker, gamma-glutamyl transpeptidase. In conclusion, BBB and choroid plexus GLUT1 are subject to differential N-linked glycosylation with the protein having an N-linked carbohydrate side chain of higher molecular mass at the BBB in comparison to the choroid plexus.
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PMID:Differential glycosylation of the GLUT1 glucose transporter in brain capillaries and choroid plexus. 803 91

Transforming growth factor-beta 1 (TGF-beta 1) stimulated growth and glucose uptake in Swiss mouse fibroblasts. DNA synthesis was increased 2-3-fold after 48 h incubation of growing 3T3 cells with TGF-beta 1 in calf serum-containing medium. Glucose transport activity in the cells was increased within 3 h after addition of TGF-beta 1 and this stimulation continued during incubation for 48 h. TGF-beta 1 also increased the levels of a brain type-glucose transporter (GLUT1) mRNA and the GLUT1 protein (55 kDa) in the membranes, consistent with the increase in glucose uptake. Furthermore, a longer exposure of TGF-beta 1 for 24-48 h induced a marked increase in the 65 kDa GLUT1 in 3T3 cell membranes. Other growth factors such as epidermal growth factor, fibroblast growth factor, transforming growth factor-alpha, and insulin did not elevate glucose uptake and the levels of 55 and 65 kDa GLUT1 proteins. Adding tunicamycin or deoxymannojirimycin to the TGF-beta 1-treated and untreated cells caused these 55 and 65 kDa glucose transporters to migrate as one band at 40-43 kDa. In addition, treating membrane proteins with glycopeptidase F, which removes N-linked oligosaccharides, also generated a glucose transporter of 40 kDa, suggesting that the 55 and 65 kDa GLUT1 proteins have a similar or identical core polypeptide but with different N-linked oligosaccharides. These results indicate that TGF-beta 1 modulates the synthesis of GLUT1 protein as well as its glycosylation in Swiss 3T3 cells, and that these changes may contribute to the control of cell proliferation by TGF-beta 1.
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PMID:Modulation of the synthesis and glycosylation of the glucose transporter protein by transforming growth factor-beta 1 in Swiss 3T3 fibroblasts. 843 54