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PubMed1990

Sequence conservation among the glucose transporter from the cyanobacterium Synechocystis sp. PCC 6803 and mammalian glucose transporters.

Synechocystis sp. PCC 6803 is capable of facultative photoheterotrophy with glucose as the sole carbon source. Eight mutants that were unable to take up glucose were transformed with plasmids from pooled gene banks of wild-type Synechocystis DNA prepared in an Escherichia coli vector that does not replicate in Synechocystis. One mutant (EG216) could be complemented with all gene banks to restore ability for photoheterotrophic growth. One of the gene banks was fractionated into single clones and plasmid DNA from each clone used to complement EG216. This yielded a 1.5 kb DNA fragment that was sequenced. It contained one complete open reading frame (gtr) whose putative gene product displayed high sequence conservation with the xylose transporter of E. coli and the mammalian glucose transporters. Further, the isolated gtr gene interrupted in vitro by a kanamycin resistance cassette could be used to construct mutants from wild-type Synechocystis sp. PCC 6803 that lacked a functional glucose transporter, thus confirming the identity of the gtr gene with the glucose transporter gene. This is the first prokaryotic glucose transporter known to share a sequence relationship with mammalian glucose transporters and the first sugar transporter from a cyanobacterium characterized at the sequence level.

Amino Acid Sequence↗

PubMed1984

Relationship between the transport from isolated nuclei of two abundant cytoplasmic messengers and the source of a messenger RNA transport factor.

Messenger RNA transport from isolated nuclei requires a 35 X 10(3) dalton cytoplasmic protein(s) which is present in both the cytosol and polyribosome fractions. Recombinant DNA probes containing cDNA inserts were used to quantitate the transport of rat liver-specific albumin and male rat liver-specific alpha 2U-globulin messenger RNA (mRNA) from male rat liver nuclei in response to the mRNA transport factors from homologous and heterologous tissues. No mRNA transport occurs in the absence of the transport factor(s). Both messengers are transported proportionately in response to the factor(s) from male or female rat liver cytosol, or from the polyribosomes (messenger ribonucleoprotein) of male or female rat liver, or brain. The transport factor(s) do not, therefore, appear to differentiate between the coding sequences of two unrelated hepatic messenger RNA's.

Albumins↗

PubMedDate not supplied

Neonatal transportation: the effects of a national neonatal transportation programme.

BACKGROUND: The transport of critically ill newborns by specialised transport teams has been shown to be associated with a significant improvement in their clinical condition on arrival at the receiving hospital. AIM: To determine if the National Neonatal Transport Programme introduced in 2001 improved clinical condition of newborns at the end of transfer. METHODS: A retrospective study of all 176 patients transported by the National Neonatal Transport Programme between March 2001 and March 2002. RESULTS: Before transfer, 17% of patients were hypothermic, 2% hypoglycaemic and 11% acidotic as were 7%, 3% and 5% respectively at the end of transfer. A review of 172 neonatal transports between 1987 and 1989 revealed that 21% of patients were hypothermic, 13% hypoglycaemic and 20% acidotic at the end of transfer. CONCLUSIONS: The National Neonatal Transport Programme has resulted in improved clinical condition of newborns at the end of transfer when compared to their condition before transfer and compared to outcomes prior to the introduction of the programme.

Critical Illness↗

PubMed2001

An integrated view of the kinetics of glucose and phosphate transport, and of glucose 6-phosphate transport and hydrolysis in intact rat liver microsomes.

The dynamics of the glucose 6-phosphatase system were investigated in intact rat liver microsomes using a fast-sampling, rapid-filtration apparatus. Glucose and phosphate transport followed single exponential kinetics, appeared to be homogeneous, was unaffected by unlabeled substrate concentrations up to 100 mM, proved insensitive to various potential inhibitors, and demonstrated similarly low energies of activation. The extent of tracer accumulation from glucose 6-phosphate depended on which of the glucose or phosphate moieties was the labeled species in the parent molecule. The rates of tracer equilibration reflected those of glucose or phosphate transport but similar initial rates of uptake were observed for the glucose and phosphate products of hydrolysis. However, the latter accounted for only 12-13% of the steady-state rate of total glucose production. It is concluded that tracer uptake cannot represent substrate transport, that labeled glucose 6-phosphate at best represents a tiny fraction of the intramicrosomal glucose or phosphate pools, and that glucose 6-phosphate transport is not an obligatory prerequisite to its hydrolysis. The latter conclusion invalidates a major postulate of the substrate transport-catalytic unit concept but proves compatible with a conformational model whereby glucose 6-phosphate transport and hydrolysis are tightly coupled processes while glucose and phosphate share, along with water and a variety of other organic and inorganic solutes, a common porelike structure for their transport through the microsomal membrane.

Animals↗

PubMed2005

Heterologous expression of a pleiotropic drug resistance transporter from Phytophthora sojae in yeast transporter mutants.

A system for the expression of an ATP binding cassette (ABC) transporter from the soybean pathogen Phytophthora sojae is described. Pdr1, an ABC transporter with homology to the pleiotropic drug resistance (PDR) family of transporters, was cloned by primer walking from a P. sojae genomic library. Reverse transcriptase PCR assays showed that the transcript disappeared after encystment of zoospores and was not detected in hyphal germlings in dilute salts, in hyphae growing in liquid V8 media, or in tissue extracts from infected hypocotyls. BLAST analysis of Pdr1 against the P. sojae EST database also revealed that this gene was present only in zoospore libraries. Comparison of the number of hits to Pdr1 with that of a set of housekeeping genes revealed that Pdr1 was expressed at rates two- to threefold higher than other transcripts. To test the hypothesis that Pdr1p functions as a broad substrate membrane transporter, Pdr1 was transformed into yeast mutants deficient in several drug resistance transporters. Yeast mutants transformed with Pdr1 possessed partial drug resistance against only 5 of 17 chemically distinct compounds. Thus, when expressed in yeast, this transporter has a significantly narrower substrate specificity in comparison to the yeast transporters, Pdr5p, Yorlp, and Snq2p.

Amino Acid Sequence↗

PubMed1979

Thymidine transport in cultured mammalian cells. Kinetic analysis, temperature dependence and specificity of the transport system.

The transport of thymidine has been characterized kinetically and thermodynamically in Novikoff rat hepatoma cells grown in culture and, less extensively, in mouse L cells, Chinese hamster ovary cells, P388 murine leukemia cells and HeLa cells. That the characterizations pertained to the transport system per se was ensured, (i) by employing recently developed methods for rapid sampling of cell/substrate mixtures in order to follow isotope movements within a few seconds after initial exposure of cells to substrate; (ii) by utilizing cells rendered, by genetic or chemical means, incapable of metabolizing thymidine; and (iii) by demonstrating conformity of the transport data to an integrated rate equation derived for a simple, carrier-mediated system. The results indicate that thymidine is transported into mammalian cells by a functionally symmetrical, non-concentrative system for which the carrier : substrate dissociation constant ranges from about 100 microM in Chinese hamster ovary cells, to 230 microM in Novikoff hepatoma cells. In all cell lines investigated, the velocity of transport was sufficient to nearly completely equilibrate low concentration of thymidine across the membrane membrane within 15 s. Temperature dependence of transport velocity and substrate : carrier dissociation were continuous (EA = 18.3 kcal/mol, delta H0' = 9.3 kcal/mol, respectively), and showed no evidence of abrupt transitions. Several natural and artificial nucleosides and nucleic acid bases inhibited influx of radiolabeled thymidine, apparently by competing with thymidine for the transport carrier.

Animals↗

PubMed1988

Cloning of a rabbit brain glucose transporter cDNA and alteration of glucose transporter mRNA during tissue development.

A full-length cDNA clone that codes for glucose transporter protein was isolated from a rabbit brain cDNA library by using synthetic oligonucleotide probe derived from the sequence of human glucose transporter cDNA. The coding region shared 93.2% nucleotide and 97.0% amino-acid similarities with those of human glucose transporter and 89.4% nucleotide and 97.4% amino-acid similarities with those of rat transporter. Northern blot analysis revealed that glucose transporter mRNA is most abundant in the placenta and that it is also abundant in the brain. The fat tissue, heart, liver, and skeletal muscle of adult rats contained a very small amount of mRNA, while heart, liver, skeletal muscle and kidney of fetal rats contained a very high amount of glucose transporter mRNA. These results suggest that this type of glucose transporter might be closely related with cell proliferation and tissue development.

Aging↗

PubMed1982

Axonal transport of protein in motor fibres of experimentally diabetic rats--fast anterograde transport.

Fast axonal transport of radiolabelled proteins in motor fibres of rat sciatic nerves was studied after 14 days of streptozotocin-induced diabetes. The rate of fast transport as measured at two time intervals after application of [3H]leucine to the motor neurone cell bodies in the spinal cord was reduced by 21% in diabetic rats. There was no significant change in the time between injection of isotope and the start of fast transport. The amount of axonal transport of radiolabelled proteins as measured by accumulation of proteins proximal to a ligation on the sciatic nerve was also unchanged. The reduction in fast transport rate in the diabetic rats was eliminated by maintenance of normal blood glucose levels in twice daily insulin administration. The results are discussed with regard to the known effects of experimental diabetes on axonal transport in sensory fibres and to the role of fast axonal transport in peripheral neuropathies in general.

Animals↗

PubMed1989

Transfers between free and combined oxygen flows in determining facilitated transport with membranes on the transport path.

The facilitated transport of a species brought about by a diffusible carrier is mediated by the sharing of the total flow between the flow of the free species (fd) and of the species-carrier compound (fc). The presence of membranes impermeable to the carrier on the transport path is accompanied by transfers between fd and fc in regions next to the membranes. These transfers are associated with differences between the current species-carrier concentration and the one that would exist at chemical equilibrium with the free species. These differences determine that the actual facilitated transport is smaller than the possible maximum. Analytic approximations to describe these differences are obtained; they are expressed in terms of physiochemical entities germane to the transport. This leads to a better conceptual understanding of the process. A relatively small system of algebraic equations for the numerical solution of the facilitated transport is formulated. A feature of this approach is that, instead of matching the values of functions at some points, the flows derived from integrals evaluated over some intervals are matched. The expressions for the physicochemical entities obtained contain the parameters explicitly; this permits analysis of the mechanisms involved in the dependence of the facilitated transport on the parameters of the system. It is shown, for instance, that the increase of the "on" chemical coefficient may result in either an increase or a decrease of the facilitated transport, depending on the current values of the parameters.

Biological Transport, Active↗

PubMed1991

Hepatocellular uptake of peptides by bile acid transporters: relationship of carrier-mediated transport of linear peptides with renin-inhibiting activity to multispecific bile acid carriers.

The uptake of a linear peptide with renin-inhibiting activity (code number EMD 51921) was characterized in isolated rat liver cells. Isolated hepatocytes take up EMD 51921 in a time-, concentration-, energy- and temperature-dependent manner. Transport of the peptide follows mixed-type kinetics. Diffusion occurs at a rate of 8.123 x 10(-6) cm/sec at 6 degrees C. For the saturable part of uptake, a Km of 2.0 microM and a Vmax of 160 pmol/mg per min were calculated. Various substrate analogues inhibit the uptake of EMD 51921. Absence of oxygen or decreased cellular ATP content (e.g., by metabolic inhibitors or xylulose) blocks hepatocellular uptake of EMD 51921. Temperatures above 20 degrees C accelerate the uptake. The activation energy was calculated to be 58.3 kJ/mol. The apparently active uptake of EMD 51921 was not sodium dependent. The membrane potential is a driving force for the accumulation of EMD 51921. Mutual competitive transport inhibition of EMD 51921, cholate and taurocholate is indicative of a common transport system. Benzamidotaurocholate and a cyclosomatostatin analog 008, not phalloidin and iodipamide, however, considerably decrease the uptake of EMD 51921. AS 30D ascites hepatoma cells, unable to accumulate bile acids and certain cyclopeptides, also fail to transport EMD 51921. BSP, a foreign substrate of the bilirubin carrier, noncompetitively inhibits the transport of EMD 51921. The inhibition of the uptake of EMD 51921 by rifampicin, a further substrate of the bilirubin carrier, is mixed: competitive at high EMD 51921 concentrations and uncompetitive at low EMD 51921 concentrations. The uptake of rifampicin into isolated rat liver cells, however, is not influenced by EMD 51921. Substrates of the transport systems for cations, amino acids, long chain fatty acids and hexoses did not influence the transport of EMD 51921.

Animals↗

PubMed1982

Inhibition of axoplasmic transport in the developing visual system of the rat-II, Quantitative analysis of alterations in transport of tritiated proline or fucose.

Developmental alterations in the amount of tritiated proline and fucose incorporated by retinal neurons and transported within axons of the optic nerve to the dorsal lateral geniculate nucleus and superior colliculus were measured at 1, 5, 10 and 15 days postnatal using quantitative autoradiography and liquid scintillation analysis. The amount of axon transport inhibition induced by introacular injections of colchicine (10-4 M-5 X 10-3M) and xylocaine (10-3 M-10-1 M) was also determined by this methodology. Grain counts of retinal autoradiograms obtained from animals of all ages employed in this study demonstrated that [3H] proline is rapidly incorporated by all retinal neurons but becomes increasingly concentrated within the inner nuclear, ganglion cell and optic fiber layers between 2h and 2 days after injection. [3H] fucose is preferentially taken up and concentrated within the plexiform and sensory element layers. Intraocular colchicine administered 24 h prior to isotope injection exhibited no significant effect on incorporation but depressed the amount of activity in the layer of optic fibers. Comparison of the effects of colchicine and xylocaine on axon transport of [3H] proline injected at 3 days of age revealed dose-dependent suppression of transport occurring up to six hr after isotope injection; however, with longer survival periods the effects of xylocaine were no longer significant whereas colchicine maintained suppression of axon transport to 20% of normal for periods of up to 10 days. Additionally, the rate and quantity of 3H] proline transported to the dorsal lateral geniculate nucleus and tectum of 1-15 day old animals was found to be inversely proportional to the age of the animal. Maximally-effective concentrations of colchicine, determined for each age level examined by the previous study to be highest compatible with the viability of the retino-fugal projection, 34 also reduced transport to from 20-40% of normal, being most effective in animals of 1-10 days of age. Autoradiographs of the optic disc demonstrated a colchicine-induced suppression of the amount of label in the exiting optic fibers and similar preparations of the tectum revealed an elimination of activity in the stratum griseum superficialis and stratum opticum which are normally heavily labeled following intraocular [3H] proline or fucose. Following [3H] fucose injection at 10 days of age, isotope appears in the contralateral visual cortex between 3 and 10 days later, indicating a substantial amount of transneuronal transfer of label which appeared to occur in concert with periods of maximal synaptogenesis. Injection of colchicine reduced the amount of label in the cortex to background levels. Concomitantly, autoradiographs of the dorsal lateral geniculate nucleus revealed cytoplasmic labeling of geniculate neurons in control animals but this was eliminated following colchicine injection...

Animals↗

PubMed2006

Drug transport in corneal epithelium and blood-retina barrier: emerging role of transporters in ocular pharmacokinetics.

Corneal epithelium and blood-retina barrier (i.e. retinal capillaries and retinal pigment epithelium (RPE)) are the key membranes that regulate the access of xenobiotics into the ocular tissues. Corneal epithelium limits drug absorption from the lacrimal fluid into the anterior chamber after eyedrop administration, whereas blood-retina barrier restricts the entry of drugs from systemic circulation to the posterior eye segment. Like in general pharmacokinetics, the role of transporters has been considered to be quite limited as compared to the passive diffusion of drugs across the membranes. As the functional role of transporters is being revealed it has become evident that the transporters are widely important in pharmacokinetics. This review updates the current knowledge about the transporters in the corneal epithelium and blood-retina barrier and demonstrates that the information is far from complete. We also show that quite many ocular drugs are known to interact with transporters, but the studies about the expression and function of those transporters in the eye are still sparse. Therefore, the transporters probably have greater role in ocular pharmacokinetics than we currently realise.

Animals↗

PubMed2005

EPR study of electron transport in the cyanobacterium Synechocystis sp. PCC 6803: oxygen-dependent interrelations between photosynthetic and respiratory electron transport chains.

In this work, we investigated electron transport processes in the cyanobacterium Synechocystis sp. PCC 6803, with a special emphasis focused on oxygen-dependent interrelations between photosynthetic and respiratory electron transport chains. Redox transients of the photosystem I primary donor P700 and oxygen exchange processes were measured by the EPR method under the same experimental conditions. To discriminate between the factors controlling electron flow through photosynthetic and respiratory electron transport chains, we compared the P700 redox transients and oxygen exchange processes in wild type cells and mutants with impaired photosystem II and terminal oxidases (CtaI, CydAB, CtaDEII). It was shown that the rates of electron flow through both photosynthetic and respiratory electron transport chains strongly depended on the transmembrane proton gradient and oxygen concentration in cell suspension. Electron transport through photosystem I was controlled by two main mechanisms: (i) oxygen-dependent acceleration of electron transfer from photosystem I to NADP(+), and (ii) slowing down of electron flow between photosystem II and photosystem I governed by the intrathylakoid pH. Inhibitor analysis of P700 redox transients led us to the conclusion that electron fluxes from dehydrogenases and from cyclic electron transport pathway comprise 20-30% of the total electron flux from the intersystem electron transport chain to P700(+).

Electron Spin Resonance Spectroscopy↗

PubMed2002

Human Na+ -coupled citrate transporter: primary structure, genomic organization, and transport function.

This paper describes the cloning and functional characterization of the human Na(+)-coupled citrate transporter (NaCT). The cloned human NaCT shows 77% sequence identity with rat NaCT. The nact gene is located on human chromosome 17 at p12-13. NaCT mRNA is expressed most predominantly in the liver, with moderate expression detectable in the brain and testis. When functionally expressed in mammalian cells, human NaCT mediates the Na(+)-coupled transport of citrate. Studies with several monocarboxylates, dicarboxylates, and tricarboxylates show that the transporter is selective for citrate with comparatively several-fold lower affinity for other intermediates of citric acid cycle. The Michelis-Menten constant for citrate is approximately 650 microM. The activation of citrate transport by Na(+) is sigmoidal, suggesting involvement of multiple Na(+) ions in the activation process. The transport process is electrogenic. This represents the first plasma membrane transporter in humans that mediates the preferential entry of citrate into cells. Citrate occupies a pivotal position in many important biochemical pathways. Among various citric acid cycle intermediates, citrate is present at the highest concentrations in human blood. The selectivity of NaCT towards citrate and its predominant expression in the liver suggest that this transporter may facilitate the utilization of circulating citrate for the generation of metabolic energy and for the synthesis of fatty acids and cholesterol.

Amino Acid Sequence↗

PubMed1997

Purine nucleobase transport in bloodstream forms of Trypanosoma brucei is mediated by two novel transporters.

The mechanism and inhibitor sensitivity of hypoxanthine transport by bloodstream forms of Trypanosoma brucei brucei was investigated. The dose response curve for the inhibition of hypoxanthine transport (1 microM) by guanosine was biphasic; approximately 90% of transport activity was inhibited with a Ki value of 10.8 +/- 1.8 microM, but 10% of the activity remained insensitive to concentrations as high as 2 mM. These two components of hypoxanthine transport are defined as guanosine-sensitive (H2) and guanosine-insensitive (H3). Hypoxanthine influx by both components was saturable, but there was a marked difference in their Km values (123 +/- 15 nM and 4.7 +/- 0.9 microM for H2 and H3, respectively) although the Vmax values (1.1 +/- 0.2 and 1.1 +/- 0.1 pmol (10[7] cells)[-1] s[-1], n = 3) were similar. Hypoxanthine uptake via the H2 carrier was inhibited by purine bases and analogues as well as by some pyrimidine bases and one nucleoside (guanosine), whereas the H3 transporter was sensitive only to inhibition by purine nucleobases. H2-mediated hypoxanthine uptake was inhibited by ionophores, ion exchangers and the potential H+-ATPase inhibitors, N,N'-dicyclohexylcarbodiimide (DCCD) and N-ethylmaleimide (NEM). Measurements of the intracellular pH and membrane potential of bloodstream trypanosomes in the presence and absence of these agents established a linear correlation between protonmotive force and rate of [3H]hypoxanthine (30 nM) uptake. We conclude that hypoxanthine transport in bloodstream forms of T. b. brucei occurs by two transport systems with different affinities and substrate specificities, one of which, H2, appears to function as a H+-/hypoxanthine symporter.

Animals↗

PubMed1989

Kinetics of the purified glucose transporter. Direct measurement of the rates of interconversion of transporter conformers.

There is considerable evidence that the mechanism of glucose transport by the transporter of human erythrocytes is one in which the transporter oscillates between two conformations, To and Ti. Each conformer possesses a single glucose binding site that in vivo faces either the extracellular space (conformer To) or the cytoplasm (conformer Ti). In this study, the interconversions of these conformers in the absence and presence of D-glucose have been directly observed by means of the stopped-flow method with fluorescence detection. Nearly unidirectional conversion of one conformer to the other was accomplished by rapidly mixing purified transporter (a mixture of To and Ti) with either 4,6-ethylidene-D-glucose, which preferentially binds to To, or phenyl beta-D-glucoside, which preferentially binds to Ti. The values of the individual rate constants for the conversion of Ti to To and vice versa in the absence and presence of D-glucose at 10.0 degrees C have been obtained, and these show that the kinetics are consistent with the alternating conformation model for transport. Conformational change occurs much more rapidly with glucose bound to the transporter. Furthermore, the activation energy Ea for conformer interconversion is much less when glucose is bound than for unliganded transporter. For example, Ea is approximately 28 kcal/mol for Ti----To versus 17 kcal/mol for Ti + S----ToS, where S is glucose. The alpha-anomer of glucose was 37% more effective than the beta-anomer in speeding the interconversion.(ABSTRACT TRUNCATED AT 250 WORDS)

Glucose↗

PubMed1994

Transcellular transport of benzoic acid across Caco-2 cells by a pH-dependent and carrier-mediated transport mechanism.

The pH-dependent transcellular transport of [14C]benzoic acid across a Caco-2 cell monolayer is shown to be mediated by a monocarboxylic acid-specific carrier-mediated transport system, localized on the apical membrane. Evidence for the carrier-mediated transport of benzoic acid includes (a) the significant temperature and concentration dependence, (b) the metabolic energy dependence, (c) the inhibition by unlabeled benzoic acid and other monocarboxylic acids, (d) countertransport effects on the uptake of [14C]benzoic acid, and (e) effects of a proteinase (papain) and amino acid-modifying reagents. Furthermore, since carbonylcyanide p-trifluoromethoxyphenylhydrazone and nigericin significantly inhibited the transport of [14C]benzoic acid, the direct driving force for benzoic acid transport is suggested to be the inwardly directed proton gradient. From these results, together with previous observations using intestinal brush border membrane vesicles, the pH dependence of the transcellular transport of certain organic weak acids across Caco-2 cells is considered to result mainly from a proton gradient-dependent, carrier-mediated transport mechanism, rather than passive diffusion according to the pH-partition theory.

Acetates↗

PubMed1994

Transepithelial transport and metabolism of thyrotropin-releasing hormone (TRH) in monolayers of a human intestinal cell line (Caco-2): evidence for an active transport component?

Cell culture models for gastrointestinal transport and metabolism are important mechanistic tools. Our studies of Caco-2 monolayers demonstrate heterogeneity in transport characteristics depending on passage number and origin of the cells. In accordance with data obtained in animals and humans, TRH shows a carrier-mediated, saturable transport component, which operates parallel to a passive pathway in Caco-2 cells at passage number 89-99. At low TRH concentrations (< 3 mM) active transport becomes prominent, as demonstrated by the temperature dependence of TRH transport and inhibition experiments. The Michaelis-Menten parameters of the active, saturable transport component are: Km = 1.59 mM and Vmax = 1.84 microM/min. The pH optimum was determined to be at pH 6.0. On the other hand an exclusively paracellular passive route was found with Caco-2 cells at passage number 30-34. These results are also in agreement with observations made by others in cell culture experiments. The aspect of rigorously characterizing the specific Caco-2 clone under investigation is emphasized, especially when active transport mechanisms are suspected.

Amino Acid Sequence↗