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Regulation of cerebral glucose metabolism.

The brain uses glucose as a primary fuel for energy generation. Glucose gains entry into the brain by facilitated diffusion across the blood-brain barrier. Glucose transport may adapt during changes in cerebral glucose metabolism, neural activation and changes in plasma glucose levels. Within the brain, glucose is either oxidized to produce ATP or used to synthesize glycogen. To ensure the delivery of a continuous supply of glucose to maintain normal cellular function, the brain has developed a complex regulatory system to preserve its supply. Gluco-sensing neurons have been demonstrated in various regions of the brain and they appear to play an important role in not only detecting changes in brain glucose levels but also in initiating responses to maintain constant brain glucose levels. In this review, we will discuss the regulation of brain glucose metabolism (CMR(gluc)) and how it adapts to chronic changes in glycemia, like that seen in hyperglycemic patients with diabetes mellitus or patients with type 1 diabetes, recurrent hypoglycemia, and hypoglycemia unawareness. We will also consider the role of brain glycogen in providing fuel for energy under conditions of stress.

Blood-Brain Barrier↗

Purine and pyrimidine transport by cultured Novikoff cells. Specificities and mechanism of transport and relationship to phosphoribosylation.

Adenine, guanine, and hypoxanthine were rapidly incorporated into the acid-soluble nucleotide pool and nucleic acids by wild type Novikoff cells. Incorporation followed normal Michaelis-Menten kinetics, but the following evidence indicates that specific transport processes precede the phosphoribosyltransferase reactions and are the rate-limiting step in purine incorporation by whole cells. Cells of an azaguanine-resistant subline of Novikoff cells which lacked hypoxanthine-guanine phosphoribosyltransferase activity and failed to incorporate guanine or hypoxanthine into the nucleotide pool, exhibited uptake of guanine and hypoxanthine by a saturable process. Similarly, wild type cells which had been preincubated in a glucose-free basal medium containing KCN and iodoacetate transported guanine and hypoxanthine normally, although a conversion of these purines to nucleotides did not occur in these cells. The mutant and KCN-iodoacetate treated wild type cells also exhibited countertransport of guanine and hypoxanthine when preloaded with various purines, uracil, and pyrimidine nucleosides. The cells also possess a saturable transport system for uracil although they lack phosphoribosyltransferase activity for uracil. In the absence of phosphoribosylation, none of the substrates was accumulated against a concentration gradient. Thus transport is by facilitated diffusion (nonconcentrative transport). Furthermore, the apparent Km values for purine uptake by untreated wild type and azaguanine-resistant cells were higher and the apparent Vmax values were lower than those for the corresponding phosphoribosyltransferases...

Adenine↗

Transport of amino acid amide sarcosinamide and sarcosinamide chloroethylnitrosourea in human glioma SK-MG-1 cells.

The transport of the amino acid amide N-[3H]sarcosinamide (methyl glycinamide) was investigated in human glioma SK-MG-1 cells. Sarcosinamide uptake was found to be temperature dependent, sodium independent, and linear up to 1 min at 22 degrees C. Equilibrium was reached after 10 min at 22 degrees C with accumulation slightly above unity. Sarcosinamide was not metabolized in the cells as shown by thin layer chromatography. The uptake of sarcosinamide was significantly decreased when the extracellular pH was lowered from 7.5 to 6.0 and significantly enhanced at pH values above 7.5. The latter effect may be due mainly to increased cell permeability at high pH. The uptake of the labeled sarcosinamide was trans-stimulated by excess cold sarcosinamide. Sarcosinamide uptake over a 200-fold range of concentrations followed Michaelis-Menten kinetics with a Km of 0.284 +/- 0.041 mM and a Vmax of 0.154 +/- 0.024 nmol/10(6) cells/min. The uptake of sarcosinamide was significantly reduced by iodoacetate but not by the metabolic poisons NaF, ouabain, or dinitrophenyl, suggesting that the uptake is not dependent on energy, rather it proceeds by facilitated diffusion. Several naturally occurring substrates were unable to inhibit the uptake of sarcosinamide. Leucine significantly reduced the uptake of sarcosinamide, while sarcosinamide was a weak inhibitor of leucine transport. 2-Aminobicyclo[2,2,1]heptane-2-carboxylic acid a specific substrate for the sodium-independent, 2-aminobicyclo[2,2,1]heptane-2-carboxylic acid-sensitive amino acid system L failed to inhibit the uptake of sarcosinamide. Epinephrine reduced the uptake of sarcosinamide and sarcosinamide was equally potent as an inhibitor of epinephrine transport. Dixon plot analysis demonstrated that epinephrine (Km = 0.270 mM) inhibits the uptake of sarcosinamide competitively (Ki = 0.260 mM). These results indicate that sarcosinamide is a substrate for the catecholamine transporter. The alkylating agent, sarcosinamide chloroethylnitrosourea, was tested for its ability to inhibit the uptake of sarcosinamide. The results of Dixon plot analysis were consistent with competitive inhibition of sarcosinamide uptake and the inhibition constant Ki for SarCNU was found to be 3.26 +/- 0.57 mM. The steady-state intracellular concentration of SarCNU was found to be significantly higher (cell:medium ratio of 1.03 +/- 0.01) than that of BCNU cell:medium ratio of 0.52 +/- 0.12). These findings indicate that SarCNU and sarcosinamide share the same carrier for uptake in SK-MG-1 cells. This transport mechanism may be responsible for the increased accumulation of SarCNU as compared to BCNU, a nitrosourea which enters cells by passive diffusion.

Biological Transport, Active↗

Cellular pharmacology of cyclopentenyl cytosine in Molt-4 lymphoblasts.

The toxicity, uptake, and metabolism of the oncolytic nucleoside cyclopentenyl cytosine (CPEC) have been examined in the Molt-4 line of human lymphoblasts. This compound is known to be converted to its 5'-triphosphate, which inhibits CTP synthetase and depletes the pools of cytidine nucleotides. In the Molt-4 system, the concentration of drug reducing proliferation by 50% in a 24-h incubation was between 50 and 100 nM. Cytidine, uridine, and nitrobenzylthioinosine almost fully prevented the cytotoxicity of CPEC when introduced shortly before or together with the drug, but only cytidine was effective as an antidote when added 12 h after 200 nM CPEC. Studies of the cellular entry of CPEC revealed that nitrobenzylthioinosine fully blocked this process over a 60-s interval and for as long as 2 h, suggesting that the initial interiorization was mediated by facilitated diffusion. In Molt-4 cells incubated with tritiated CPEC, 9 metabolites could be distinguished: prominent among these was cyclopentenyl uridine (CPEU), the deamination product of CPEC; other major metabolites included the 5'-mono-, di-, and triphosphates of CPEC, and of CPEU, along with two phosphodiesters provisionally identified as CPEC-diphosphate choline and CPEC-diphosphate ethanolamine. When the accumulation of CPEC-5'-triphosphate was measured as a function of concentration of the drug in the medium, the process was found not to be saturable by levels of CPEC up to 1000 nM. In cells incubated with 200 nM drug, CPEC-5'-triphosphate accumulated rapidly and linearly for approximately 4 h, the time for doubling of the concentration being 2 h. After a 16-h incubation with 100 nM CPEC, the concentration of CPEC-5'-triphosphate was 50-fold that of the parent drug in the medium and could be readily monitored spectrophotometrically in high-pressure liquid chromatography effluents without recourse to radiolabeled nucleoside. In 2-h incubations, the concentration of free CPEC required to reduce CTP by 50% was 150 nM; this corresponded to a CPEC-5'-triphosphate level of 750 nM. After washout of extracellular CPEC, CPEC-5'-triphosphate decayed with a half-life that ranged from 9 to 14 h. Twenty-four h after washout of 200 nM CPEC (the concentration of drug reducing proliferation by 80%), cells had not resumed proliferation, and CTP pools were still depressed by 90%. Cytidine, uridine, and nitrobenzylthioinosine all strongly repressed the anabolic phosphorylation of CPEC when added to Molt-4 cells along with the drug.(ABSTRACT TRUNCATED AT 400 WORDS)

Antineoplastic Agents↗

Affinity of different local anesthetic drugs and catecholamines for the contraluminal transport system for organic cations in proximal tubules of rat kidneys.

To study the cellular uptake of [3H]tetraethylammonium (TEA) and its inhibition by different local anesthetic drugs and catecholamines, the capillary stopped flow microperfusion method was used. [3H]TEA concentration in the peritubular capillaries decreased in a time and concentration-dependent manner. This cellular uptake of [3H]TEA could be described by a facilitated diffusion model (Jmax = 0.57 +/- 0.08 pmol sec-1 cm-1, Km = 0.28 +/- 0.01 mmol/l). Between the pKa values of the local anesthetic drugs (range, 2.8-8.9) and their apparent Ki values, a significant correlation was found (r = -0.916, n = 12). In the case of catecholamines, hydrophobic substitution in the form of an alkyl chain in the alpha-position or at the nitrogen increased the inhibitory potency, whereas hydroxyl substitution in the beta-position decreased the affinity. Except for the catecholamines with complex substitutions at the benzene ring (--CH2OH,--NHCONH2,--OOCN[CH3)2, --Cl, --NH2) the apparent Ki values of the catecholamines were directly correlated with the hydrophobicity. It is concluded that hydrophobicity and pKa are two important physicochemical parameters which influence the affinity of a molecule for the transport system for organic cations at the contraluminal side of renal proximal tubules.

Anesthetics↗

Ultracytochemical localization of the erythrocyte/HepG2-type glucose transporter (GLUT1) in cells of the blood-retinal barrier in the rat.

The blood-retinal barrier is part of the blood-ocular barrier. Retinal pigment epithelial cells connected by tight junctions serve as an outer blood-retinal barrier, and the nonfenestrated endothelial cells of blood vessels sealed by tight junctions serve as an inner blood-retinal barrier. Using antibodies specific for the erythrocyte/HepG2-type glucose transporter (GLUT1), one isoform of facilitated-diffusion glucose transporters, it was found, by ultrastructural cytochemical examination, that GLUT1 in the rat was localized at both the apical and basolateral plasma membranes of retinal pigment epithelial cells. The fenestrated endothelial cells of the underlying choriocapillaries were negative for GLUT1. In the inner retina, GLUT1 was found at both the luminal and contraluminal plasma membranes of endothelial cells. These observations show that GLUT1 is concentrated at the critical plasma membranes of the blood-retinal barrier and may serve as the machinery for glucose transport across the barrier.

Animals↗

Hypoxanthine transport by cultured Chinese hamster lung fibroblasts.

The uptake of hypoxanthine by Chinese hamster lung fibroblasts grown in tissue culture was studied in wild type clones and 8-azaguanine-resistant mutant clones devoid of hypoxanthine-guanine phosphoribosyltransferase. Wild type fibroblasts rapidly accumulate [3H]hypoxanthine from the medium and over 80% of the intracellular radioactivity is found in acid-soluble nucleotides. The phosphoribosyltransferase-deficient clones accumulate much lower levels of hypoxanthine and over 85% of the intracellular 3H label is associated with chemically unaltered hypoxanthine. The internal level of hypoxanthine in the mutant clones rapidly approaches but does not exceed that present in the medium. Wild type and phosphoribosyltransferase-deficient cells take up hypoxanthine at almost identical initial rates at external hypoxanthine levels from 2 to 300 muM. Analysis of these data reveals two transport systems that obey the Michaelis-Menten relationship. These differ markedly in affinity, yielding average Km values of 20 and 600 muM for both cell types. Hypoxanthine transport by both low and high affinity transport systems is blocked by p-chloromercuriphenylsulfonate and N-ethylmaleimide. Counter-transport of hypoxanthine was demonstrated in phosphoribosyltransferase-deficient fibroblasts. It is concluded that hypoxanthine is transported into Chinese hamster cells by means of carrier-mediated processes (facilitated diffusion) that operate independently of phosphoribosylation.

4-Chloromercuribenzenesulfonate↗

Substrate specificity, kinetics, and stoichiometry of sodium-dependent adenosine transport in L1210/AM mouse leukemia cells.

Two equilibrative (facilitated diffusion) nucleoside transport processes and a concentrative Na(+)-dependent co-transport process contribute to zero-trans inward fluxes of nucleosides in L1210 mouse leukemia cells. Na(+)-linked inward adenosine fluxes in L1210/AM cells (a clone deficient in adenosine, deoxyadenosine, and deoxycytidine kinase activities) were measured as initial rates of [3H]adenosine influx in medium containing Na+ salts and 10 microM dipyridamole. The Na(+)-linked transporter distinguished between the D- and L-enantiomers of adenosine, the latter being a virtual nonpermeant in the initial-rate assay. Adenine arabinoside, inosine, 2'-deoxyadenosine and 2'-deoxyadenosine derivatives with halogen atoms at the purine C-2 position were recognized as substrates of the Na(+)-linked system because of their inhibition of adenosine (10 microM) fluxes under the condition of Na(+)-dependence with IC50 values ranging between 25 and 183 microM; uridine, deoxycytidine, and cytosine arabinoside (each at 400 microM) inhibited adenosine fluxes by 10-40%. Inward Na(+)-linked adenosine fluxes were saturable with respect to extracellular adenosine and Na+ concentrations [( Na+]o); Km and Vmax values for adenosine influx were 9.4 +/- 2.6 microM and 1.67 +/- 0.2 pmol/microliter cell water/s when [Na+]o was 100 mM. The stoichiometry of Na+:adenosine co-transport, determined by Hill analysis of the dependence of adenosine fluxes on [Na+]o, was 1:1. The thiol-reactive agents, N-ethylmaleimide (NEM), showdomycin and p-chloromercuriphenylsulphonate (pCMPS), inhibited Na(+)-linked adenosine fluxes with IC50 values of 40, 10, and 2 microM, respectively. This inhibition was partially reversed by the presence of adenosine in incubation media containing pCMPS, but not NEM. Thiol groups accessible to pCMPS may be involved in substrate recognition by the transporter and in the permeation step.

4-Chloromercuribenzenesulfonate↗

Comparative pharmacology of the nitrobenzylthioguanosine-sensitive and -resistant nucleoside transport mechanisms of Ehrlich ascites tumor cells.

A variety of nucleoside transport inhibitors and substrates were compared for their capacities to inhibit the zero-trans influx of [3H]uridine in Ehrlich ascites tumor cells. ATP-depleted cells accumulated [3H]uridine primarily by facilitated diffusion (Vmax = 16 pmol/sec/microliter cell water) via both nitrobenzylthioguanosine (NBTGR)-sensitive (IC50 = 0.53 nM, 100 microM [3H]uridine) and NBTGR-resistant (IC50 = 71 microM, 100 microM [3H]uridine) mechanisms with uridine Km estimates of 99 and 284 microM, respectively. Dilazep also distinguished between the transporter subtypes with IC50 values of 1.4 nM and 1.8 microM, respectively, for inhibiting 100 microM [3H]uridine influx. Incubation of cells with 50 nM NBTGR allowed the selective study of inhibitor effects on NBTGR-resistant [3H]uridine influx. Dipyridamole, cyclopentyladenosine, 2-phenylaminoadenosine, etoposide, teniposide, diazepam, chlordiazepoxide, triazolam and the lidoflazine derivative 2-(aminocarbonyl)-N-(4-amino-2,6-dichlorophenyl)-4-[5,5-bis-(4- fluorophenyl)pentyl]-1-piperazineacetamide (R75231), were significantly less potent as inhibitors of NBTGR-resistant influx, when compared with their capacities to inhibit the total mediated influx of [3H]uridine. In contrast, 2-fluoroadenosine, 2-chloroadenosine, 5'-N-ethylcarboxamidoadenosine and soluflazine were relatively more effective as inhibitors of the NBTGR-resistant component. Mioflazine, a compound related to both soluflazine and R75231, did not distinguish between transporter subtypes. The NBTGR-resistant transporter also had a distinctive substrate specificity; guanosine, 2'-deoxyguanosine, cytidine and 2'-deoxycytidine were significantly less effective as inhibitors of NBTGR-resistant [3H]uridine influx.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Isolation and characterization of an L1210 cell line retaining the sodium-dependent carrier cif as its sole nucleoside transport activity.

Nucleoside permeation across mammalian cell membranes is complex with at least four distinct transporters known. Two of these (es and ei) are equilibrative (facilitated diffusion) carriers that have been studied is considerable detail. The other two (cif and cit) are concentrative, Na(+)-dependent carriers. A major obstacle to the characterization of the latter two mechanisms has been the lack of suitable model systems expressing only a single nucleoside transport activity. The present study describes the isolation of a cell line that has cif as its sole nucleoside transporter. L1210/MC5-1 cells, which have es and cif transport activity, were mutagenized and plated in soft agar containing two cytotoxic nucleosides (tubercidin (7-deazaadenosine) and cytosine arabinoside) that are substrates for es but not cif. A clonal line (L1210/MA-27.1) was isolated which retained the capacity for Na(+)-dependent [3H]formycin B transport but was unable to transport [3H]thymidine, a substrate for es but not cif. Failure of the mutant to transport thymidine was also demonstrated by the inability of thymidine (with adenine as a purine source) to rescue these cells from methotrexate toxicity. Furthermore, the mutant lacked nitrobenzylthioinosine (NBMPR) binding activity (an integral part of the es transporter) as demonstrated by reversible NBMPR binding and photoaffinity labeling with [3H]NBMPR. Loss of es transport activity was also demonstrated by the failure of NBMPR to affect the toxicity of 2-chlorodeoxyadenosine (IC50 approximately 30 nM) in L1210/MA27.1 cells. In contrast, NBMPR decreased the IC50 for 2-chlorodeoxyadenosine from 100 to 30 nM in the parental L1210/MC5-1 cell line. These results are consistent with the mechanism of NBMPR potentiation of 2-chlorodeoxyadenosine toxicity in L1210 cells being a blockade of efflux via es while the nucleoside is pumped into the cells by the concentrative cif carrier.

2-Chloroadenosine↗

Substitution of basic amino acids within endonuclease V enhances nontarget DNA binding.

Several DNA-interactive proteins, including the DNA repair enzyme T4 endonuclease V, have been shown to locate their target recognition sites utilizing an electrostatically mediated facilitated diffusion mechanism. Previous work indicates that a decrease in the affinity of endonuclease V for nontarget DNA results in an increased nontarget dissociation rate. This study was designed to investigate the effect of an increase in the affinity of endonuclease V for nontarget DNA. Using a working structural model of the enzyme as a guide, the electrostatic character of endonuclease V was altered. Substitution of Thr-7 with Lys-7 resulted in an enzyme with wild type in vitro characteristics. Mutations which increased the positive charge along a proposed solvent-exposed alpha-helical face had significant effects. The mutants Ala-30, Val-31----Lys-30, Leu-31 and Asn-37----Lys-37 displayed wild type in vitro apurinic-specific and dimer-specific nicking activities. Although the processive dimer-specific nicking rate of the Lys-37 mutant resembled that of wild type, the rate of the Lys-30, Leu-31 mutant was reduced by 60%. In addition, the salt concentration range over which these mutants processively nick dimer-containing DNA has been greatly expanded. Both mutants are shown to have an increased affinity for nontarget DNA.

Amino Acids↗

Sodium-dependent nucleoside transport in mouse leukemia L1210 cells.

Nucleoside permeation in L1210/AM cells is mediated by (a) equilibrative (facilitated diffusion) transporters of two types and by (b) a concentrative Na(+)-dependent transport system of low sensitivity to nitrobenzylthioinosine and dipyridamole, classical inhibitors of equilibrative nucleoside transport. In medium containing 10 microM dipyridamole and 20 microM adenosine, the equilibrative nucleoside transport systems of L1210/AM cells were substantially inhibited and the unimpaired activity of the Na(+)-dependent nucleoside transport system resulted in the cellular accumulation of free adenosine to 86 microM in 5 min, a concentration three times greater than the steady-state levels of adenosine achieved without dipyridamole. Uphill adenosine transport was not observed when extracellular Na+ was replaced by Li+, K+, Cs+, or N-methyl-D-glucammonium ions, or after treatment of the cells with nystatin, a Na+ ionophore. These findings show that concentrative nucleoside transport activity in L1210/AM cells required an inward transmembrane Na+ gradient. Treatment of cells in sodium medium with 2 mM furosemide in the absence or presence of 2 mM ouabain inhibited Na(+)-dependent adenosine transport by 50 and 75%, respectively. However, because treatment of cells with either agent in Na(+)-free medium decreased adenosine transport by only 25%, part of this inhibition may be secondary to the effects of furosemide and ouabain on the ionic content of the cells. Substitution of extracellular Cl- by SO4(-2) or SCN- had no effect on the concentrative influx of adenosine.

Adenosine↗

Ultracytochemical localization of the erythrocyte/HepG2-type glucose transporter (GLUT1) in the ciliary body and iris of the rat eye.

Aqueous humor, with its unique low concentration of proteins, is produced by the ciliary body and isolated by the blood-aqueous barrier from the body fluid. Glucose in aqueous humor is a major source of nutrients for lens and corneal cells, and is maintained near the plasma level, suggesting a specific glucose transport mechanism in the blood-aqueous barrier. Using antibodies against erythrocyte/HepG2-type glucose transporter (GLUT1), one isoform of the facilitated diffusion glucose transporters, the authors found immunocytochemically that GLUT1 localizes in the epithelial cells of ciliary body and iris. GLUT1 is also found in the endothelial cells of blood vessels in the iris, whereas no labeling is seen in the blood vessels in the ciliary body. In the ciliary body epithelium, the plasma membranes of both the pigmented epithelial (PE) and nonpigmented epithelial (NPE) cells are positive for GLUT1. By the colloidal gold particle counting, the basal infoldings of PE cells show approximately two-fold denser labeling than those of NPE cells. Since PE and NPE cells make up a functional syncytium with numerous gap junctions, the authors suggest that glucose transport in the ciliary body occurs in this manner: glucose diffuses out from blood vessels through the pores of fenestrated endothelial cells, is transported into PE cells by GLUT1 in their plasma membrane, enters NPE cells through gap junctions connecting PE and NPE cells, and is finally transported into the aqueous humor by GLUT1 of NPE cells. The higher density of GLUT1 in PE cells may account for the consumption of glucose by PE and NPE cells in addition to the transepithelial transport.

Animals↗

Different mammalian facilitative glucose transporters expressed in Xenopus oocytes.

Xenopus oocytes exhibit an extremely low basal glucose transport and are thus ideally suited for the expression of heterologous glucose transporters. They have, therefore, proven to be a very valuable expression system to functionally express the erythrocyte/brain (GLUT1), the liver (GLUT2), and the adipocyte/muscle (GLUT4) glucose transporters. Characterization of their functional properties indicates that they fulfill the criteria of a glucose transport protein by demonstrating saturation kinetics, stereospecificity, and inhibition by cytochalasin B. Although mammalian facilitative glucose transporters have been expressed in bacteria and eukaryotic cell lines, the present data emphasize the advantage of using Xenopus oocytes for comparative kinetic analysis of the various members of the facilitated diffusion glucose transporter gene family.

Animals↗

Mechanism and regulation of intestinal phosphate absorption.

Proper absorption of inorganic phosphate (Pi) from the lumen of the small intestine is of great importance for the achievement of Pi homeostasis. Although due to intralumenal H+ and Pi concentrations, Pi probably can be absorbed as H2PO4- by passive means in the duodenum, transepithelial transport of HPO4(2)- requires uptake from the lumen by an active transport system. The latter has been identified in many species as a Na(+)-Pi cotransport system at the brush-border membrane of the enterocyte. Although it is still a matter of debate whether the intestinal Na+ gradient-driven Pi transport system is electrogenic or electroneutral, there is agreement that the transporter accepts H2PO4- and HPO4(2)- alike. Recently, two laboratories independently isolated a Na(+)-Pi-binding protein which has been tentatively identified as part of the Na(+)-Pi cotransport system. Movement of Pi from the cytosol across the basolateral membrane into the interstitial space has only been preliminarily characterized as transfer by facilitated diffusion. Na(+)-Pi cotransport across the brush-border membrane is under control by the active vitamin D metabolite, 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3). The sterol increases the intrinsic activity, i.e. the number and/or mobility of Na(+)-Pi carriers through genomic and probably also nongenomic actions. In addition, the rate of Na(+)-gradient-driven Pi transport can be enhanced by the hormone also through reduction of transmembrane Na+ fluxes so that more energy for translocation becomes available from the transmembrane Na+ gradient. Evidence is accumulating that thyroid hormones as well as glucocorticoids, apart from stimulating vitamin D-independent Pi uptake, potentiate the effect of 1,25-(OH)2D3 on Na(+)-Pi cotransport across the brush-border membrane.

Animals↗

Properties of permeation pathways induced in the human red cell membrane by malaria parasites.

The intracellular development of malaria parasites in mature erythrocytes imposes on the host cell a major demand for supply of nutrients and disposal of waste products. So as to cope with these demands, the erythrocyte membrane undergoes profound alterations in its basic permeability properties. A few hours after being invaded by Plasmodium falciparum parasites, and before any structural changes are apparent on the surface, the molecular traffic across the red cell membrane changes both in intensity and in composition of permeating substances. The changes are of a gradual nature, developmentally related and dependent on de novo protein synthesis, but do not occur concurrently for all the classes of permeants. Molecules which permeate very poorly into uninfected cells, such as hexitols (e.g., sorbitol and myoinositol), amino acids (e.g., glutamine, threonine, and histidine), a variety of organic acids and metal ions show a marked increase in their permeation rates across the host cell membrane. Likewise, substances whose normal permeation pathways conform with those of facilitated diffusion (e.g., hexoses, nucleosides, choline, and some amino acids), gain access into the host cytosol either by modified or additional permeation pathways. It has been proposed that three major new pathways are induced in the membrane of infected cells: (1) one of pore-like properties, which can accommodate most of the water soluble permeants, including anionic substances; (2) a protein-lipid interface, which can accommodate compounds of relatively higher hydrophobic character; and (3) modified constitutive transporters or modified lipid surroundings with altered transport activities. The pores are blocked by permeant bioflavonoid glycosides whose sites of binding are endofacial, and amount to less than a thousand per cell. In addition to serving as specific targets for transport blockers, the new sites of permeation can also serve as routes for enhanced delivery of cytotoxic agents into parasitized cells.

Animals↗

Arabinosyl-5-azacytosine: mechanisms of native and acquired resistance.

Factors influencing the activity of the nucleoside analogue arabinosyl-5-azacytosine (ara-AC) were studied in P388 murine lymphoblasts in vitro and in vivo, in variants of these cells with artificially acquired resistance, in the naturally resistant colon 38 carcinoma in vivo, and in a panel of six human tumors maintained in continuous culture. Differences were noted not only between the sensitive and artificially developed resistant variants of P388, but also between the naturally sensitive (P388) and naturally resistant (colon 38) tumors. The artificially developed resistant P388 cell lines showed an inhibited capacity to accumulate nucleotides derived from ara-AC and deoxycytidine, whereas the accumulation of cytidine nucleotides remained unchanged. Studies of the initial velocity of facilitated diffusion of ara-AC showed only minor differences between parental and resistant lines, while the nucleotide formation rates from both ara-AC and deoxycytidine were markedly depressed in the latter cells. It is concluded, therefore, that the failure of resistant P388 cells to accumulate these compounds results not from a transport deficit per se but rather from a failure to convert the nucleosides to nondiffusible (i.e., phosphorylated) species inside the cell. This failure was accompanied by a substantial reduction in the incorporation of a radiolabeled product derived from deoxycytidine into the nucleic acids of the resistant clones. The common factor responsible for the resistance of P388 variants toward ara-AC appears to be a markedly decreased level of deoxycytidine kinase activity. The naturally resistant colon 38 carcinoma, on the other hand, in addition to a decrease in the activity of its deoxycytidine kinase, showed a lower level of activity of all its purine and pyrimidine kinases, along with a notably elevated nucleoside triphosphatase activity (with ATP as substrate) when compared to P388. These differences were reflected in lower endogenous nucleoside triphosphate pool sizes in colon 38, and in a lower level of ara-AC-5'-triphosphate accumulation in colon 38 than in P388 after comparable drug exposure. In the six human tumor lines, a positive correlation was established between sensitivity to ara-AC (as determined by its median inhibitory concentration) and cellular content of deoxycytidine kinase. It is concluded that this latter enzyme is a generally important determinant of sensitivity to arabinosyl-5-azacytosine.

Animals↗

Penetration of nalidixic acid into Escherichia coli K-12 cells.

Transport of nalidixic acid (NAL) into Escherichia coli cells subjected to osmotic shock, permeabilised with toluene or treated with DNP, CCCP or EDTA, was studied. It was found that osmotic shock and protonophores do not inhibit the transport of [3H]NAL, however, the transport of [3H]DAP and [3H]glucose is reduced. EDTA and toluene enhance penetration of [3H]NAL. This effect is, however, abolished in the presence of Mg++ ions. It is suggested that NAL penetrates into the cell by simple or facilitated diffusion and that the outer membrane of E. coli is the penetration barrier for the drug.

Carbonyl Cyanide m-Chlorophenyl Hydrazone↗