Low-Affinity glucose carrier geneLGT1 ofSaccharomyces cerevisiae, a homologue of theKluyveromyces lactis RAG1 gene

Yeast ◽  
1993 ◽  
Vol 9 (12) ◽  
pp. 1373-1377 ◽  
Author(s):  
C. Prior ◽  
H. Fukuhara ◽  
J. Blaisonneau ◽  
M. Wesolowski-Louvel
Keyword(s):  
Rag1 Gene ◽  
Glucose Carrier

Unique cytochalasin B binding characteristics of the hepatic glucose carrier

Biochemistry ◽  
1983 ◽  
Vol 22 (9) ◽  
pp. 2222-2227 ◽  
Author(s):  
Jeffrey D. Axelrod ◽  
Paul F. Pilch
Keyword(s):  
Cytochalasin B ◽  
Binding Characteristics ◽  
Hepatic Glucose ◽  
Glucose Carrier

Transport of 2-deoxy-D-glucose by isolated protoplasts of the yeast, Kluyveromyces lactis

1982 ◽  
Vol 28 (7) ◽  
pp. 901-906 ◽  
Author(s):  
Paulette W. Royt ◽  
Averett S. Tombes
Keyword(s):  
Glucose Utilization ◽  
Kluyveromyces Lactis ◽  
Isolated Protoplasts ◽  
Osmotic Stabilizer ◽  
Glucose Carrier

Protoplasts of succinate- and glucose-grown Kluyveromyces lactis were generated by incubating cells with β-mercaptoethanol and β-glucuronidase in the presence of MgSO4 as osmotic stabilizer. Transport of 2-deoxyglucose by the protoplasts was comparable with that of the walled cells. Only protoplasts of succinate-grown cells exhibited a lag in glucose utilization. Removal of the wall by this technique does not result in loss of the inducible component of the glucose carrier via degradation or release.

Inositol Transport by Hepatopancreatic Brush-Border Membrane Vesicles of the Lobster Homarus Americanus

1988 ◽  
Vol 140 (1) ◽  
pp. 107-121
Author(s):  
TEVA SIU ◽  
GREGORY A. AHEARN
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Homarus Americanus ◽  
Brush Border Membrane Vesicles ◽  
Carrier Mechanism ◽  
Apparent Diffusion ◽  
Noncompetitive Inhibitor ◽  
Inositol Uptake ◽  
Glucose Carrier

The mechanism of [3H]myo-inositol transport by the lobster hepatopancreas was examined using purified brush-border membrane vesicles. Transport was stimulated by a 100 mmoll−1 inward Na+ gradient, but other cation gradients were ineffective, suggesting a Na+-dependent transfer mechanism. The transport system was most efficient at pH7.0 (both sides), rather than in the presence of a pH gradient (pHin = 7.0; pHout = 5.5) or at bilaterally low pH (pHin = pHout = 5.5). The system was shown to be electrogenic in two different ways. First, myo-inositol uptake was stimulated by anions of increasing permeability (SCN− > Cl− > gluconate). Second, an outwardly directed, valinomycin-induced K+ diffusion potential (inside negative) enhanced uptake in comparison with vesicles lacking the ionophore. Myo-inositol was transported by a carrier mechanism with an apparent Kt of 0.79mmoll−1, a Jmax of 6.3pmolmg protein−1 s−1, and by apparent diffusion with a permeability coefficient of 5.92 pmolmg protein−1s−1 (mmolT1)−1. D-Glucose was a noncompetitive inhibitor of myo-inositol uptake, but myo-inositol did not significantly reduce the transport of D-[3H]glucose. Vesicles preloaded with myo-inositol trans-stimulated [3H]myo-inositol uptake, whereas those preloaded with D-glucose did not, suggesting that the inositol carrier did not transport D-glucose. It is proposed that myo-inositol does not share the glucose carrier, and that D-glucose may modulateinositol influx by binding to a ‘regulator’ site on the inositol carrier.

scholarly journals The interaction of 3-deoxy-3-fluoro-d-glucose with the hexose-transport system of the human erythrocyte

1973 ◽  
Vol 135 (4) ◽  
pp. 773-777 ◽  
Author(s):  
G. J. Riley ◽  
N. F. Taylor
Keyword(s):  
Kinetic Parameters ◽  
Erythrocyte Membrane ◽  
Transport System ◽  
Dissociation Energy ◽  
Human Erythrocyte ◽  
Optical Method ◽  
Hexose Transport ◽  
Human Erythrocyte Membrane ◽  
Significant Release ◽  
Glucose Carrier

1. By using an optical method the kinetic parameters of hexose transport across the human erythrocyte membrane were determined for several sugars. The series of half-saturated constants is as follows: 3-deoxy-3-fluoro-d-glucose = 3-O-methyl-d-glucose <d-glucose<d-mannose <3-deoxy-d-glucose<d-galactose<l-arabinose. 2. Estimations of the dissociation energy of the 3-deoxy-3-fluoro-d-glucose–carrier and d-glucose–carrier complexes suggest that the binding of the two sugars to the transport system is equivalent. 3. Incubation of the erythrocytes with 3-deoxy-3-fluoro-d-glucose results in a small but significant release of F−anion. Cells treated in this way lose their ability to transport glucose.

scholarly journals N-terminal truncated human RAG1 proteins can direct T-cell receptor but not immunoglobulin gene rearrangements

Blood ◽  
2000 ◽  
Vol 96 (1) ◽  
pp. 203-209 ◽  
Author(s):  
Jeroen G. Noordzij ◽  
Nicole S. Verkaik ◽  
Nico G. Hartwig ◽  
Ronald de Groot ◽  
Dik C. van Gent ◽  
...  
Keyword(s):  
T Cell ◽  
Gene Mutation ◽  
T Cell Receptor ◽  
Severe Combined Immunodeficiency ◽  
Premature Stop Codon ◽  
Cell Receptor ◽  
Gene Rearrangements ◽  
Immunoglobulin Gene ◽  
Rag1 Gene ◽  
Immunoglobulin Gene Rearrangements

The proteins encoded by RAG1 and RAG2 can initiate gene recombination by site-specific cleavage of DNA in immunoglobulin and T-cell receptor (TCR) loci. We identified a new homozygous RAG1 gene mutation (631delT) that leads to a premature stop codon in the 5′ part of the RAG1 gene. The patient carrying this 631delT RAG1 gene mutation died at the age of 5 weeks from an Omenn syndrome-like T+/B−severe combined immunodeficiency disease. The high number of blood T-lymphocytes (55 × 106/mL) showed an almost polyclonal TCR gene rearrangement repertoire not of maternal origin. In contrast, B-lymphocytes and immunoglobulin gene rearrangements were hardly detectable. We showed that the 631delT RAG1 gene can give rise to an N-terminal truncated RAG1 protein, using an internal AUG codon as the translation start site. Consistent with the V(D)J recombination in T cells, this N-terminal truncated RAG1 protein was active in a plasmid V(D)J recombination assay. Apparently, the N-terminal truncated RAG1 protein can recombine TCR genes but not immunoglobulin genes. We conclude that the N-terminus of the RAG1 protein is specifically involved in immunoglobulin gene rearrangements.

scholarly journals Agronomic and Seed Traits of Soybean Lines with the Rag1 gene for Aphid Resistance

Crop Science ◽  
2010 ◽  
Vol 50 (5) ◽  
pp. 1891-1895 ◽  
Author(s):  
Justin L. Mardorf ◽  
Walter R. Fehr ◽  
Matthew E. O'Neal
Keyword(s):  
Aphid Resistance ◽  
Seed Traits ◽  
Rag1 Gene

Use of 3-O-methyI-D-glucose and phloretin to estimate the intracellular water space of mouse peritoneal macrophage monolayers

1982 ◽  
Vol 60 (1) ◽  
pp. 76-79
Author(s):  
Douglas B. Lowrie
Keyword(s):  
Glucose Uptake ◽  
Peritoneal Macrophage ◽  
Intracellular Water ◽  
Mouse Peritoneal Macrophage ◽  
Facilitated Diffusion ◽  
Water Space ◽  
Glucose Carrier

Macrophages took up 3-O-methyl-D-glucose rapidly by facilitated diffusion using the glucose carrier and slowly by carrier-independent diffusion. Phloretin inhibited carrier-dependent but not carrier-independent diffusion. Estimates of intracellular water space based on 3-O-methyl-D-glucose uptake varied between 0.7 and 6.9 μL∙106 cells−1 for 2-week-old monolayers.

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