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PubMed1977

Amino acid transport in isolated hepatocytes: effect of glucagon.

Amino acid transport was studied in freshly isolated adult rat hepatocytes using non-metabolizable alpha-amino-1-[14C] isobutyric acid and 1-aminocyclopentane-1-[14C] carboxylic acid. In the presence of sodium, hepatocytes concentrated alpha-aminoisobutyric acid; this concentrative component of the transport had properties similar to transport system A. The sodium-independent transport of aminocyclopentane carboxylic acid had properties similar to transport system L (facilitated diffusion). Glucagon stimulated the influx of alpha-aminoisobutyric acid into hepatocytes. The glucagon effect (a) occurred rapidly, but its full expression required two hours of exposure of the cells to hormone; (b) involved new protein (and possibly RNA) synthesis; and (c) occurred at low concentrations of glucagon (50% effect with 0.4 nm). Glucagon stimulated only system A. Cyclic AMP also stimulated the transport of alpha-aminoisobutyric acid. Freshly isolated hepatocytes appear conveniently suited to the investigation of various aspects of the regulation of liver amino acid transport in normal and pathophysiological states.

Amino Acids↗
PubMed2003

Role of ascorbate in oxidative protein folding.

Both in prokaryotic and eukaryotic cells, disulfide bond formation (oxidation and isomerization steps) are catalyzed exclusively in extracytoplasmic compartments. In eukaryotes, protein folding and disulfide bond formation are coupled processes that occur both co- and posttranslationally in the endoplasmic reticulum (ER), which is the main site of the synthesis and posttranslational modification of secretory and membrane proteins. The formation of a disulfide bond from the thiol groups of two cysteine residues requires the removal of two electrons, consequently, these bonds cannot form spontaneously; an oxidant is needed to accept the electrons. In aerobic conditions the ultimate electron acceptor is usually oxygen; however, oxygen itself is not effective in protein thiol oxidation. Therefore, a small molecular weight membrane permeable compound should be supposed for the transfer of electrons from the ER lumen. The aim of the present study was the investigation of the role of ascorbate/dehydroascorbate redox couple in oxidative folding of proteins. We demonstrated that ascorbate addition or its in situ synthesis from gulonolactone results in protein thiol (and/or glutathione; GSH) oxidation in rat liver microsomes. Since microsomal membrane is hardly permeable to ascorbate, the existence of a transport metabolon was hypothesized. Three components of the system have been described and partially characterized: (i) A microsomal metalloenzyme is responsible for ascorbate oxidation on the outer surface of the ER. Ascorbate oxidation results in ascorbate free radical and dehydroascorbate production. (ii) Facilitated diffusion of dehydroascorbate is present in microsomal vesicles. The transport is presumably mediated by a GLUT-type transporter. On the contrary, the previously hypothesized glutathione disulfide (GSSG) transport is practically absent, while GSH is transported with a moderate velocity. (iii) Protein disulfide isomerase catalyzes the reduction of dehydroascorbate in the ER lumen. Both GSH and protein thiols can be electron donors in the process. Intraluminal dehydroascorbate reduction and the consequent ascorbate accumulation strictly correlate with protein disulfide isomerase activity and protein thiol concentration. The concerted action of the three components of the system results in the intraluminal accumulation of ascorbate, protein disulfide and GSSG. In fact, intraluminal ascorbate and GSSG accumulation could be observed upon dehydroascorbate and GSH uptake. In conclusion, ascorbate is able to promote protein disulfide formation in an in vitro system. Further work is needed to justify its role in intact cellular and in vivo systems, as well as to explore the participation of other antioxidants (e.g. tocopherol, ubiquinone, and vitamin K) in the electron transfer chain responsible for oxidative protein folding in the ER.

Animals↗
PubMed1984

Cysteine uptake and taurine biosynthesis in freshly isolated and primary cultured rat hepatocytes.

Analysis of the uptake and metabolism of [14C]cysteine in rat liver was undertaken using freshly isolated hepatocytes and hepatocytes maintained in primary culture. The uptake of [14C]cysteine by freshly isolated hepatocytes was by means of both saturable and non-saturable transport systems and the former system was thought to involve facilitated diffusion. The uptake of [14C]cysteine by hepatocytes maintained in primary culture for 24 h also consisted of non-saturated and saturated transport mechanisms. The magnitude of the saturable transport system in cultured hepatocytes was, however, much greater than that found in freshly isolated hepatocytes, and was considered to be operated by active transport. Both freshly isolated and primary cultured hepatocytes had cysteine sulphinic acid decarboxylase activity, but this enzyme activity in the latter cells was noticeably reduced in comparison with that found in freshly isolated hepatocytes. Hepatocytes maintained in primary culture produced not only radiolabelled taurine, but also radiolabelled cysteine sulphinic acid, hypotaurine and alanine when incubated with [14C]cysteine. The present results indicate that cultured hepatocytes actively transport cysteine as well as metabolizing cysteine to taurine via cysteine sulphinic acid and hypotaurine.

Animals↗
PubMed1994

Immunocytochemical expression of the blood-brain barrier glucose transporter (GLUT-1) in neural transplants and brain wounds.

The present study examined the immunocytochemical expression of the blood-brain barrier glucose transporter (GLUT-1) in a series of fetal neocortical transplants, autonomic tissue transplants, and stab wounds to the rat brain. GLUT-1 is one of a family of different glucose transporters and is found exclusively on barrier-type endothelial cells. In the brain it is responsible for the regulated facilitative diffusion of glucose across the blood-brain barrier. This investigation is the first to determine if this important molecule is altered during the process of angiogenesis that occurs following neural transplantation procedures or direct brain injury. Beginning in late fetal brain, e.g., E18 and continuing into maturity, GLUT-1 was strongly and exclusively expressed on normal cerebral vessels. In solid fetal central nervous system (CNS) transplants up to around 3 weeks postoperative, GLUT-1 was only weakly expressed, particularly as exemplified by colloidal gold immunostaining when compared with the host. At later times examined, up to 15 months postoperative, GLUT-1 immunoexpression was comparable with the normal adjacent brain. In autonomic tissue transplants, where the vessels do not have a blood-brain barrier, as expected, GLUT-1 was not expressed. In stab wounds, at 1 week there was extensive gliosis, and the injured vessels appeared fragmented and collapsed but still expressed GLUT-1, although to a somewhat lesser extent than normal brain. Between 3 and 6 weeks, GLUT-1 was expressed on tortuous vessels and in apparently fibrillar processes in the wound vicinity with a similar pattern to astrocyte (GFAP) reactivity. These results suggest the occurrence of a down-regulation of GLUT-1 in early transplants, perhaps related to reduced glycolytic activity or transient ischemia, or possibly due to the utilization of alternative energy sources. That GLUT-1 expression was not entirely lost in stab wounds to the mature brain suggests that the protein may be more labile in fetal or perinatal brain than in the adult and may not be affected by direct injury. Coupled with previous transplantation studies that have shown reduced neuronal glycolysis and potential barrier alterations, the reduction of GLUT-1 activity within nearly the identical time frame could indicate a relatively early critical period in cellular metabolism following transplantation of CNS tissue.

Animals↗
PubMed1989

Different capacities for amino acid transport in periportal and perivenous hepatocytes isolated by digitonin/collagenase perfusion.

Periportal and perivenous hepatocytes were isolated from rat liver by digitonin/collagenase perfusion for investigating the acinar heterogeneity of amino acid transport activities related to glutamine and ammonia metabolism. Immunocytochemical staining of the respective subpopulations for glutamine synthetase demonstrated that periportal subpopulations were essentially free of glutamine synthetase-positive cells, whereas perivenous subpopulations showed a 2- to 3-fold enrichment of glutamine synthetase-positive hepatocytes. The high perivenous/periportal ratio of 59 found for glutamine synthetase activity as well as the perivenous/periportal ratios of other marker enzymes further indicated the good separation of periportal and perivenous cells. alpha-Aminoisobutyric acid, histidine and glutamate were used to determine the distribution pattern of amino acid transport systems A, N and G-, as well as of the sodium-independent uptake of these compounds 1 hr after isolation and after maximal hormonal stimulation during primary culture. The strong heterogeneity of the sodium-independent transport of histidine, characterized by higher perivenous transport rates [perivenous/periportal ratio: 1.5 (1 hr) to 3.5 (48 hr)], suggests a significant role of facilitated diffusion, presumably in glutamine export. Conversely, the strong heterogeneity of the sodium-dependent glutamate transport (System G-) characterized by higher uptake rates in nonstimulated [perivenous/periportal ratio: 6.6 (1 hr)] and in hormonally treated perivenous hepatocytes (perivenous/periportal ratio: 2.2) reflects its possible significance with respect to the substrate availability for glutamine synthesis. The observed heterogeneities provide a basis for understanding how substrate fluxes related to glutamine metabolism might be established and regulated.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMed1992

Acute and chronic signals controlling glucose transport in skeletal muscle.

Glucose transport into muscle cells occurs through facilitated diffusion mediated primarily by the GLUT1 and GLUT4 glucose transporters. These transporter proteins are controlled by acute and chronic exposure to insulin, glucose, muscle contraction, and hypoxia. We propose that acute responses occur through recruitment of pre-formed glucose transporters from an intracellular storage site to the plasma membrane. In contrast, chronic control is achieved by changes in transporter biosynthesis and protein stability. Using subcellular fractionation of rat skeletal muscle, recruitment of GLUT4 glucose transporters to the plasma membrane is demonstrated by acute exposure to insulin in vivo. The intracellular pool appears to arise from a unique organelle depleted of transverse tubule, plasma membrane, or sarcoplasmic reticulum markers. In diabetic rats, GLUT4 content in the plasma membranes and in the intracellular pool is reduced, and incomplete insulin-dependent GLUT4 recruitment is observed, possibly through a defective incorporation of transporters to the plasma membrane. The lower content of GLUT4 transporters in the muscle plasma membranes is reversed by restoration of normoglycemia with phlorizin treatment. In some muscle cells in culture, GLUT1 is the only transporter expressed yet they respond to insulin, suggesting that this transporter can also be regulated by acute mechanisms. In the L6 muscle cell line, GLUT1 transporter content diminishes during myogenesis and GLUT4 appears after cell fusion, reaching a molar ratio of about 1:1 in the plasma membrane. Prolonged exposure to high glucose diminishes the amount of GLUT1 protein in the plasma membrane by both endocytosis and reduced biosynthesis, and lowers GLUT4 protein content in the absence of changes in GLUT4 mRNA possibly through increased protein degradation. These studies suggest that the relative contribution of each transporter to transport activity, and the mechanisms by which glucose exerts control of the glucose transporters, will be key subjects of future investigations.

Animals↗
PubMed1992

Alterations in glucose transporter expression and function in diabetes: mechanisms for insulin resistance.

Insulin resistance is a major pathologic feature of human obesity and diabetes. Understanding the fundamental mechanisms underlying this insulin resistance has been advanced by the recent cloning of the genes encoding a family of facilitated diffusion glucose transporters which are expressed in characteristic patterns in mammalian tissues. Two of these transporters, GLUT1 and GLUT4, are present in muscle and adipose cells, tissues in which glucose transport is markedly stimulated by insulin. To understand the mechanisms underlying in vivo insulin resistance, regulation of these transporters is being investigated. Studies reveal divergent changes in the expression of GLUT1 and GLUT4 in a single cell type as well as tissue specific regulation. Importantly, alterations in glucose transport in rodent models of diabetes and in human obesity and diabetes cannot be entirely explained by changes in glucose transporter expression. This suggests that defects in glucose transporter function such as impaired translocation, fusion with the plasma membrane, or activation probably contribute importantly to in vivo insulin resistance.

Adipose Tissue↗
PubMed1976

Carbohydrate uptake by Escherichia coli.

In contrast to active transport, the uptake of carbohydrates via the phosphoenolpyruvate-dependent phosphotransferase system (PTS) leads to the appearance in the cell of the sugar initially as a 1- or 6-phosphate ester. The components of the PTS that transfer phosphate to the sugar are not absolutely specific for any one sugar. Both their synthesis and their activity are controlled; in the latter, "fine" control, glucose-6-phosphate appears to play an important role. Studies of growth on, and uptake of, galactose by E.coli mutants devoid of components of the PTS and also devoid of active transport systems for galactose, suggest that proteins effecting facilitated diffusion of hexoses may be part of, or be closely associated with, the sugar-specific components of the PTS.

Carbohydrate Metabolism↗
PubMed1978

Transport and phosphorylation of hexoses in normal and Rous sarcoma virus-transformed chick embryo fibroblasts.

Effects of transformation by Rous sarcoma virus on sugar uptake and activity and the subcellular distribution of hexokinase isozymes in chick embryo fibroblasts were examined. Transformation caused a several-fold increase in the maximum velocity for uptake of 2-deoxyglucose without a significant change in Km. Cytochalasin B (CB), was used to differentiate between the effects of transformation on facilitated diffusion and the nonsaturable (CB-insensitive) mode. Transformation was found to stimulate 2-deoxyglucose transport by both mechanisms, but the increase in transport by the CB-insensitive mode was greater. Transformation enhances the activity of hexokinase, the enhancement being confined to the particulate fraction of the enzyme. Heat-inactivation and electrophoretic mobility studies showed that although hexokinase Type I is the major form in both normal and transformed fibroblasts, there is a significant increase in the proportion of the Type II isozyme in the transformed cells.

Animals↗
PubMed2006

Basolateral aromatic amino acid transporter TAT1 (Slc16a10) functions as an efflux pathway.

Basolateral efflux is a necessary step in transepithelial (re)absorption of amino acids from small intestine and kidney proximal tubule. The best characterized basolateral amino acid transporters are y+LAT1-4F2hc and LAT2-4F2hc that function as obligatory exchangers and thus, do not contribute to net amino acid (re)absorption. The aromatic amino acid transporter TAT1 was shown previously to localize basolaterally in rat's small intestine and to mediate the efflux of L-Trp in the absence of exchange substrate, upon expression in Xenopus oocytes. We compared here the amino acid influx and efflux via mouse TAT1 in Xenopus oocytes. The results show that mTAT1 functions as facilitated diffusion pathway for aromatic amino acids and that its properties are symmetrical in terms of selectivity and apparent affinity. We show by real-time RT-PCR that its mRNA is highly expressed in mouse small intestine mucosa, kidney, liver, and skeletal muscle as well as present in all other tested tissues. We show that mTAT1 is not N-glycosylated and that it localizes to the mouse kidney proximal tubule. This expression is characterized by an axial gradient similar to that of the luminal neutral amino acid transporter B0AT1 and shows the same basolateral localization as 4F2hc. mTAT1 also localizes to the basolateral membrane of small intestine enterocytes and to the sinusoidal side of perivenous hepatocytes. In summary, we show that TAT1 is a basolateral epithelial transporter and that it can function as a net efflux pathway for aromatic amino acids. We propose that it, thereby, may supply parallel exchangers with recycling uptake substrates that could drive the efflux of other amino acids.

Amino Acid Transport Systems, Neutral↗
PubMed2002

Cellular and subcellular distribution of metals in molluscs.

The cellular processes involved in metal metabolism in molluscs are reviewed, with emphasis on the contribution of microscopy (AMG, ARG, EPMA, and SIMS) to both basic research of metal cell biology and applied environmental research. In molluscs, metal uptake may occur by facilitated diffusion, active transport, or endocytosis, and can be enhanced by MT synthesis or formation of mineralized granules. In aquatic molluscs, gills constitute a key interface for dissolved metal uptake, where metals are bound to MT, incorporated into lysosomes, and released basally towards the blood plasma and circulating hemocytes. However, particulate metal uptake is mainly achieved via the digestive tract by endocytosis; further metals are transferred first to lysosomes and then to residual bodies, especially in the digestive cells of the digestive gland. Additionally, metals can be accumulated selectively in specific cell types. As ligands pools differ from cell to cell, different metals may be retained in different cell types. Class "a" metals are localized in cells with granules composed of carbonate, oxalate, phosphate, and sulfate (oxygen donors), whereas "b" metals are associated with those cell types rich in sulfur and nitrogen ligands (sulfur donors). In molluscs, oxygen donors occur in connective tissue calcium cells and basophilic cells, whereas sulfur donors are present in digestive cells, podocytes, nephrocytes, and rhogocytes. Hemocytes, which constitute the most relevant system for metal transport between tissues, move around the body and may penetrate tissues and remove metals from the inner medium to be accumulated in lysosomes as nondigested products. Rhogocytes also participate in metal mobilization, accumulation, and release. The assessment of metal levels in target cells of sentinel molluscs by microscopic techniques provides an early-warning measure, with promising applications as an exposure biomarker for environmental monitoring programs.

Animals↗
PubMed2001

Glucose and lactate metabolism during brain activation.

The dependence of brain function on blood glucose as a fuel does not exclude the possibility that lactate within the brain might be transferred between different cell types and serve as an energy source. It has been recently suggested that 1) about 85% of glucose consumption during brain activation is initiated by aerobic glycolysis in astrocytes, triggered by demand for glycolytically derived energy for Na+ -dependent accumulation of transmitter glutamate and its amidation to glutamine, and 2) the generated lactate is quantitatively transferred to neurons for oxidative degradation. However, astrocytic glutamate uptake can be fueled by either glycolytically or oxidatively derived energy, and the extent to which "metabolic trafficking" of lactate might occur during brain function is unknown. In this review, the potential for an astrocytic-neuronal lactate flux has been estimated by comparing rates of glucose utilization in brain and in cultured neurons and astrocytes with those for lactate release and uptake. Working brain tissue and isolated brain cells release large amounts of lactate. Cellular lactate uptake occurs by carrier-mediated facilitated diffusion and is normally limited by its dependence on metabolism of accumulated lactate to maintain a concentration gradient. The rate of this process is similar in cultured astrocytes and glutamatergic neurons, and, at physiologically occurring lactate concentrations, lactate uptake corresponds at most to 25% of the rate of glucose oxidation, which accordingly is the upper limit for "metabolic trafficking" of lactate. Because of a larger local release than uptake of lactate and the necessity for rapid lactate clearance to maintain the intracellular redox state to support lactate production in the presence of normal oxygen levels, brain activation in vivo is probably, in many cases, accompanied by a substantial overflow of glycolytically generated lactate, both to different brain areas and under some conditions (spreading depression, hyperammonemia) to circulating blood.

Animals↗
PubMed1989

Sodium-independent transport of noradrenaline in mouse and rat astrocytes in primary culture.

The uptake of noradrenaline by primary cultures of mouse and rat astrocytes was investigated in order to examine whether an inhibition of extraneuronal noradrenaline uptake was the mechanism whereby some trace biogenic amines potentiate neuronal responses to noradrenaline. In the presence of inhibitors of the enzymes monoamine oxidase and catechol-O-methyl transferase, it was found that astrocytes took up noradrenaline by a temperature-dependent, sodium-independent mechanism that was saturable with a Km = 3.4 x 10(-7) M and a Vmax = 1.6 pmole/mg protein/2 min. This uptake mechanism did not concentrate noradrenaline within the cell. The uptake of noradrenaline was inhibited by ascorbic acid (IC50 = 3.4 x 10(-7) M), adrenaline (IC50 = 7.9 x 10(-7) M), and dopamine (IC50 = 1.5 x 1.0(-6) M). It was not inhibited by the tricyclic antidepressants amitriptyline and desmethylimipramine or the trace biogenic amines beta-phenylethylamine, phenylethanolamine, p- and m-tyramine and p- and m-octopamine. Nor was the uptake inhibited by fluoxetine or 5-hydroxytryptamine. It is concluded that astrocytes take up noradrenaline by a facilitated-diffusion mechanism and that this uptake resembles the extraneuronal uptake described in preparations of brain tissue. It is also concluded that the trace biogenic amines do not potentiate neuronal responses to noradrenaline by inhibiting extraneuronal uptake.

Animals↗
PubMed1987

Uptake of propranolol by microvessels isolated from bovine brain.

To study the transport system of propranolol (PL), a basic drug, in the blood-brain barrier, the uptake of PL into isolated bovine brain microvessels was investigated. The uptake of PL was a concentrative one via saturable process (Km = 42.5 microM) that was decreased by hypothermia (Q10 = 2.2), but not by metabolic inhibitors (2,4-dinitrophenol, KCN, ouabain). Although basic drugs such as quinidine and imipramine decreased both the initial rate of uptake and the steady-state cell-to-medium concentration ratio (C/M) of PL, acidic drugs (phenobarbital, salicylic acid) did not affect them. These results suggest that PL is taken up by the endothelial cells of the isolated brain microvessels by facilitated diffusion which is specific for basic drugs and then binds to certain binding sites in the cells.

2,4-Dinitrophenol↗
PubMed1977

The inhibitory effect of the artificial electron donor system, phenazine methosulfate-ascorbate, on bacterial transport mechanisms.

The artificial electron donor system, phenazine methosulfate (PMS)-ascorbate, inhibited active transort of solutes in Pseudomonas aeruginosa irrespective of whether the active transport systems were shock sensitive or shock resistant. N,N,N',N'-tetramethylphenylenediamine could be substituted for PMS but a higher concentration was required. PMS-ascorbate also inhibited active transport in several other bacterial species with the exception of Escherichia coli and of a nonpigmented strain of Serratia marcescens. PMS-ascorbate previously has been shown to energize active transport in isolated membrane vesicles, even those prepared from the same bacterial species in whose intact cells active transport was inhibited. The apparent Km of glucose active transport in untreated cells of P. aeruginosa was 40 micron while the Km of glucose transport in cells incubated with PMS-ascorbate was 25 mM, and PMS-ascorbate had no effect on efflux of accumulated glucose. These results strongly suggested that facilitated diffusion resulted upon exposure of the cells to PMS- ascorbate. Thus, PMS-ascorbate appeared to have an uncoupler-like effect on cells of P. aeruginosa. The experimental data also pointed out that there are fundamental differences between the response of intact cells and membrane vesicles to exogenous electron donors.

Ascorbic Acid↗
PubMed2003

Distal heme pocket regulation of ligand binding and stability in soybean leghemoglobin.

Leghemoglobins facilitate diffusion of oxygen through root tissue to a bacterial terminal oxidase in much the same way that myoglobin transports oxygen from blood to muscle cell mitochondria. Leghemoglobin serves an additional role as an oxygen scavenger to prevent inhibition of nitrogen fixation. For this purpose, the oxygen affinity of soybean leghemoglobin is 20-fold greater than myoglobin, resulting from an 8-fold faster association rate constant combined with a 3-fold slower dissociation rate constant. Although the biochemical mechanism used by myoglobin to bind oxygen has been described in elegant detail, an explanation for the difference in affinity between these two structurally similar proteins is not obvious. The present work demonstrates that, despite their similar structures, leghemoglobin uses methods different from myoglobin to regulate ligand affinity. Oxygen and carbon monoxide binding to a comprehensive set of leghemoglobin distal heme pocket mutant proteins in comparison to their myoglobin counterparts has revealed some of these mechanisms. The "distal histidine" provides a crucial hydrogen bond to stabilize oxygen in myoglobin but has little effect on bound oxygen in leghemoglobin and is retained mainly for reasons of protein stability and prevention of heme loss. Furthermore, soybean leghemoglobin uses an unusual combination of HisE7 and TyrB10 to sustain a weak stabilizing interaction with bound oxygen. Thus, the leghemoglobin distal heme pocket provides a much lower barrier to oxygen association than occurs in myoglobin and oxygen dissociation is regulated from the proximal heme pocket.

Amino Acids↗
PubMedDate not supplied

Substrate-accelerated death of Saccharomyces cerevisiae CBS 8066 under maltose stress.

When Saccharomyces cerevisiae CBS 8066 was grown under maltose limitation, two enzymes specific for maltose utilization were present: a maltose carrier, and the maltose-hydrolysing alpha-glucosidase. The role of these two enzymes in the physiology of S. cerevisiae was investigated in a comparative study in which Candida utilis CBS 621 was used as a reference organism. Maltose pulses to a maltose-limited chemostat culture of S. cerevisiae resulted in 'substrate-accelerated death'. This was evident from: (1) enhanced protein release from cells; (2) excretion of glucose into the medium; (3) decreased viability. These effects wee specific with respect to both substrate and organism: pulses of glucose to maltose-limited cultures of S. cerevisiae did not result in cell death, neither did maltose pulses to maltose-limited cultures of C. utilis. The maltose-accelerated death of s. cerevisiae is most likely explained in terms of an uncontrolled uptake of maltose into the cell, resulting in an osmotic burst. Our results also provide evidence that the aerobic alcoholic fermentation that occurs after pulsing sugars to sugar-limited cultures of s. cerevisiae (short-term Crabtree effect) cannot solely be explained in terms of the mechanism of sugar transport. Both glucose and maltose pulses to maltose-limited cultures triggered aerobic alcohol formation. However, glucose transport by S. cerevisiae occurs via facilitated diffusion, whereas maltose entry into this yeast is mediated by a maltose/proton symport system.

Carrier Proteins↗
PubMed1993

Immunological analysis of glucose transporters expressed in different regions of the rat brain and central nervous system.

Glucose is the major energy source for brain tissue. It is now well established that glucose crosses the blood-brain barrier by facilitated diffusion mediated by the erythrocyte-type (GLUT 1) glucose transporter. Northern blot analysis has indicated that brain tissue expresses two different glucose transporters, the erythrocyte-type transporter and the brain-type transporter (GLUT 3). Here we use a panel of antibodies specific for four glucose transporters to examine the distribution of these transporters in various regions of rat brain and central nervous system. We show that GLUT 1 and GLUT 3 are expressed in virtually all regions of the brain examined, but that the relative levels of the proteins differ. We also demonstrate that GLUT 2 appears to be widely expressed in all brain regions, but at apparently low levels. In addition, GLUT 4 is expressed in the pituitary, the hypothalamus and the medulla. These results are discussed in the light of potential glucose-regulated processes in the brain.

Animals↗