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PubMed1985

Calcium transport in the cellular slime mould Dictyostelium discoideum.

Transport of Ca2+ into amoebae of Dictyostelium discoideum was studied using 45Ca and a lanthanum stopping technique. Ca2 uptake was found to be rapid and showed saturation kinetics. No difference was found in Ca2+ uptake between vegetative and aggregation competent cells, the V(max) for unstimulated amoebae being approx. 10 nmol/10(7) cells per min. Ca2+ uptake had the characteristics of passive facilitated diffusion using a saturatable carrier and NaN3 and ouabain were not inhibitory. The chemoattractants cAMP and folate, previously reported to stimulate the uptake of Ca2+ into amoebae, did not stimulate the rate of Ca2+ uptake by this carrier but increased the extent of Ca2+ taken up over the period 10-30 s after chemotactic stimulation. The significance of these findings for the function of Ca2+ in chemotactic signalling is discussed.

Journal Article↗

PubMed1986

Facilitated transport of 3-O-methyl-D-glucose in human polymorphonuclear leukocytes.

Transport of the nonmetabolizable hexose analogue 3-O-methyl-D-glucose (30MG) was measured in human polymorphonuclear leukocytes at 37 degrees C, pH 7.4. 3OMG at very low concentration (0.05 mM) equilibrated with the intracellular water with a rate constant of about 0.08 s-1. Transport of 3OMG in the presence of 20 microM cytochalasin B and transport of L-glucose were insignificant. Countertransport of 14C-labelled 3OMG was demonstrated. Exchange of 3OMG between the extracellular and intracellular water showed saturation with a Km of about 4 mM. Thus, the transport of 3OMG is mediated almost exclusively by facilitated diffusion.

Biological Transport↗

PubMed1988

Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle.

The active uptake and efflux of Ca2+ from suspensions of vesicles from heavy rabbit muscle sarcoplasmic reticulum have been examined using the antipyrylazo III dye method in the presence of various nucleotide triphosphate substrates to support active Ca2+ accumulation. On addition of ATP, Ca2+ is rapidly accumulated and maintained at high internal concentrations until the substrate for pump protein is exhausted. Ca2+-induced Ca2+ release which is inhibited by ruthenium red can be demonstrated. The kinetics of Ca2+ release via these channels is different from the Ca2+ efflux observed after substrate exhaustion. This rate was found to be dependent on the type of nucleotide triphosphate, decreasing in the order ATP greater than GTP greater than CTP greater than ITP UTP. It is suggested that different conformations of the Ca2+ pump protein induced by the different substrates may result in the creation of pathways for the facilitated diffusion of Ca2+.

Adenosine Monophosphate↗

PubMed1989

The hexose carrier from Chlorella. cDNA cloning of a eucaryotic H+-cotransporter.

The cDNA coding for the inducible H+/hexose cotransporter of Chlorella kessleri has been cloned and sequenced. It was isolated by differential screening of a cDNA library prepared from glucose-induced cells. The increase in expression of the gene correlates quantitatively with the increase in uptake activity due to induction; it is not expressed in a hexose transport mutant. An open reading frame allows for a membrane protein of 533 amino acids with a relative molecular mass of 57 kDa. This protein is highly homologous to the human and rat glucose transporters catalyzing facilitated diffusion and to the bacterial H+/pentose cotransporters. It is not related to the H+/lactose cotransporter of E. colli and to the mammalian Na+/glucose cotransporter.

Base Sequence↗

PubMed1995

Uptake of iron by symbiosomes and bacteroids from soybean nodules.

Symbiosomes and bacteroids isolated from soybean nodules are able to take up the iron-citrate complex. The kinetics are characterized by initial high rates of iron internalization, and ATPase inhibitors significantly lower the uptake. This is consistent with an energy-dependent process on both membranes, although the involvement of a simultaneous facilitated diffusion can not be completely ruled out. Citrate alone is poorly absorbed by symbiosomes; this uptake is greatly enhanced by addition of iron. Iron-citrate was found both in the nodule cytosol and in the bacteroids. These results provide the first experimental evidence for the existence, at least in young nodules, of an important iron trafficking system from the plant host cell to the microsymbiont, through the peribacteroid membrane.

Arsenates↗

PubMed1990

Folic acid transport in organ-cultured mucosa of human intestine. Evidence for distinct carriers.

The transport of folic acid was investigated in organ-cultured endoscopic biopsy specimens of intestinal mucosa from normal subjects. In the proximal small intestine at pH 5.5 and 6.5, [3H]folic acid accumulated to concentrations 2.64- and 2.17-fold higher than those of the medium, respectively, but at pH 7.5 the concentration was same as that of the medium. Saturability of initial rates of uptake was demonstrable with respect to luminal concentrations of [H+] and folic acid. Two proton-dependent transport mechanisms were evident: (a) a carrier with a low affinity for H+ and a low capacity for folic acid, and (b) a high-affinity, high-capacity carrier (Km, 635 and 54.6 nmol/L [H+]; Vmax, 0.066 and 2.583 pmol folic acid/microL intracellular water per 10 minutes, respectively). Kinetic studies of folic acid uptake at pH 5.5 and 7.5 revealed a difference in Km for folic acid (15.76 and 34.38 mumol/L, respectively) with no change in Vmax. In the colon, folic acid did not accumulate against a concentration gradient, and the initial rate of uptake was not affected by luminal pH. The accumulation of folic acid in colonic mucosa was significantly higher at pH 5.5 than at 7.5 and showed significant regional variation, with optimal uptake in the sigmoid colon. Methotrexate inhibited folic acid uptake competitively both in the proximal small intestine and in the cecum (inhibition constant 6.9 and 54 mumol/L, respectively, at pH 5.5). These data indicate the presence of a proton-dependent, active transport of folic acid in the proximal small intestine at pH 5.0-6.5. At pH 7.5 and in the mucosa of the colon, uptake of folic acid proceeds by facilitated diffusion through a low-affinity carrier.

Biological Transport, Active↗

PubMed1986

Corticosterone-binding proteins and behavioral effects of high plasma levels of corticosterone during the breeding period in the pied flycatcher.

In the pied flycatcher there exists an anomaly in the relationship between cortical histology and plasma levels of corticosterone during the breeding period. In an attempt to study this anomaly, binding capacity and binding affinity of plasma corticosterone-binding proteins (CBP) were studied in free-living pied flycatchers during the early and late parts of the breeding period. Binding capacity of CBP showed a significant decrease with the progress of the breeding season in both males and females. During the early parts of the breeding season binding capacity was significantly higher in males than in females. No difference between sexes was observed during the nestling period. In males there also was a seasonal decrease in the binding affinity of CBP. The results show that there is a good relationship between periods with high plasma levels of corticosterone and its binding capacity in the blood. A second study showed that an experimentally increased plasma level of corticosterone during the nestling period drastically reduced reproductive success. Parents given silastic implants containing corticosterone fed their nestlings less frequently and produced significantly fewer fledglings than did controls. Unlike the control birds, the body weight of the corticosterone-implanted birds did not decrease during the nestling period. Birds given corticosterone implants in which one small hole had been punched, in order to facilitate diffusion of corticosterone, all abandoned their territories and, consequently, these parents produced no fledglings. Thus, the results show that an elevation of plasma levels of corticosterone in adult pied flycatchers during the nestling period affects parental as well as territorial behavior.

Animals↗

PubMed1989

Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli. Implications for protein function.

The Vitreoscilla hemoglobin protein has been implicated in earlier studies to serve a globin-like function under oxygen-limited growth conditions. Evidence is presented using fractionation as well as proteinase K accessibility techniques to prove that a considerable amount of this protein is localized in the periplasmic space of the cell. Genetic evidence points towards the existence of information within the N-terminal domain of the protein that plays a role in the process of protein export. However, this sequence is not cleaved in the process of translocation. Analysis of the primary structure of this region reveals several unusual features. Instead of positively charged residues at its amino terminus, it has a negative charge. The overall hydrophobicity of the central region of this sequence is significantly lower than in typical leader peptides due to the presence of a charged residue. In keeping with the likelihood that such an export signal may not be very efficient, a substantial fraction of the total cellular hemoglobin can also be detected in the cytoplasm. Heme is incorporated in both cytoplasmic and periplasmic globin as indicated by the ability of protein from both fractions to bind carbon monoxide. The secretion of this protein into the periplasm raises questions concerning the physiological significance of its localization. Dimensional analysis of a model based on the facilitated diffusion hypothesis, which was initially proposed to account for the effects of eukaryotic globins on oxygen transport, suggests that periplasmic globin can support an additional oxygen flux to the respiratory apparatus that may be physiologically significant.

Amino Acid Sequence↗

PubMed1994

Different mechanism for insulin induced and contraction induced increases in skeletal muscle glucose uptake.

Glucose facilitated diffusion into cells depends on concentration gradients between intracellular and extracellular spaces and can be modified by several factors such as insulin and contractions. Calmodulin participates in the insulin induced recruitment of vesicles containing glucose transporter molecules and its inhibition by trifluoperazine blocks insulin increases in glucose uptake. In the present study we tested if calmodulin inhibition with trifluoperazine blocks hindlimb muscle glucose uptake increase induced by contractions. Trifluoperazine does not inhibit exercise induced increases in glucose uptake; therefore, the mechanisms by which insulin and functional activity increase glucose uptake are different.

Animals↗

PubMed1993

Effect of red blood cell shape on oxygen transport in capillaries.

A mathematical model of oxygen (O2) transport within a capillary utilizes axisymmetric red blood cell (RBC) shapes that were predicted theoretically by Zarda et al. in 1977. Chemical kinetics and both free and facilitated diffusion of O2 are accounted for in this time-dependent model. The finite-element method is used to solve the governing partial differential equations. It is found that the shape of RBCs, characterized by the shape parameter theta adapted from Zarda et al., affects such important O2 transport characteristics as capillary wall O2 flux and hemoglobin (Hb) saturation. At an RBC residence time (time for an RBC to travel from the capillary inlet to a given point) of 0.22 s, a change in the shape parameter theta from 0 (undeformed cell) to 26 (parachute-shaped cell) decreases the spatially averaged O2 flux by 26%. The dependence of O2 flux on RBC shape diminishes as the RBC residence time increases. The difference in Hb saturation at the RBC residence time of 0.22 s can be as large as 10% for different values of theta. The mass transfer Nusselt number, which is inversely proportional to transport resistance, decreases with increases in theta. The fractional transport resistance in the plasma region accounts for approximately 65-80% of the total intracapillary resistance. Calculations show that local chemical equilibrium in the O2-Hb chemical reaction is attained everywhere except within a thin boundary layer adjacent to the erythrocyte membrane, where significant deviation from chemical equilibrium occurs.

Animals↗

PubMed1990

Ascorbic acid uptake by young and aged guinea pig lenses.

The dynamics of in vitro uptake of [14C]-ascorbic acid into intact lenses of young (50 days old) and old (730 days old) guinea pigs was evaluated in this study. Two-dimensional protein gel analysis of [35S]-methionine labeled proteins provided evidence that the isolated lenses were viable throughout the culture period. It was found that the in vitro uptake of ascorbate into these lenses follows similar saturation kinetics for lenses from both age groups. Moreover, the linear uptake rate was identical. Ascorbate transport was inhibited by phloretin, p-chloromercuribenzoate, insulin, glucose and ouabain; however, no inhibition was observed with 2,4-dinitrophenol or NaF. These results suggest that the lenticular ascorbate concentration is regulated by a facilitated diffusion process and it not energy-dependent. Data on ascorbate transport into lenses from aged guinea pigs provide strong evidence that the abnormally low ascorbic acid concentrations in lenses of old mammals is not likely the result of a decreased lenticular uptake ability.

Aging↗

PubMed1983

Regulation of purine uptake in normal and neoplastic cells.

Purine bases and purine nucleosides pass the cell membrane by facilitated diffusion. For purine bases two different carrier proteins seem to exist. Purine bases are trapped intracellularly immediately after passage of the cell membrane by the action of purine phosphoribosyltransferases (PRTs). Comparison of kinetic data of transport and intracellular enzyme reactions shows that intracellular metabolism is rate limiting for the whole uptake process. Since phosphate stimulates the uptake of bases, limited availability of phosphoribosylpyrophosphate (PRPP) might play a regulatory role. Purine nucleosides apparently enter cells via a common carrier. Of the nucleosides under investigation, only adenosine was taken up in significant amounts. Uptake of adenosine is mainly determined by the ratio of adenosine deaminase (ADA) and adenosine kinase (AK) activities. For uptake of purine nucleotides sequential action of ecto-5'-nucleotidase (ecto-5'-NT), nucleoside carrier and intracellular metabolism is necessary. Cells without ecto-5'-NT activity did not accumulate radioactivity from nucleotides. Proliferating neoplastic cells (K 562 and HL 60 cells) showed enhanced uptake of purine bases and nucleosides, when compared to quiescent cells (erythrocytes and granulocytes). From initial rates of uptake and intracellular enzyme activities it could be concluded that this enhanced uptake was due to alterations of enzyme pattern in the neoplastic cells.

5'-Nucleotidase↗

PubMed1980

Formation and resolution of DNA catenanes by DNA gyrase.

We have discovered that DNA gyrase interlocks duplex DNA circles to form catenanes and resolves catenanes into component monomers. The reactions were inhibited by novobiocin and oxolinic acid and required ATP, Mg++ and spermidine. DNA sequence homology is not involved in catenation, since hybrid catenanes were formed efficiently between supercoiled phi X174 and Col E1 DNA. Strikingly different results were obtained with native and relaxed Col E1 DNA substrates. Up to 50-60% of input native DNA was converted into oligomeric catenanes, predominantly dimers and trimers. Relaxed substrates were instead converted into vast interlocked networks and were occasionally knotted. Optimal catenation occurred only in the narrow range of 20-35 mM KCl; increased ionic strength blocked catenation completely but activated the back reaction of decatenation. Gyrase resolved both the oligomeric catenanes and interlocked networks it produced, as well as naturally occurring catenanes. These results imply that the mechanism of gyrase involves a transient double-strand break and passage of a DNA segment through the resulting gap. Gyrase is representative of a general class of enzymes, found in both procaryotic and eucaryotic cells, that facilitate diffusion of duplex DNA segments through each other and may thereby solve topological problems arising from the replication, recombination and condensation of DNA.

Bacteriocin Plasmids↗

PubMed1982

Calcium ions, drug action and the red cell membrane.

Intracellular calcium regulates a number of membrane functions in the erythrocyte, including control of shape, membrane lipid composition and cation permeability. Measurement of total red cell calcium has yielded values between 5 and 15 nmol/ml cells, and these low values in part reflect the absence of Ca2+ -containing organelles. Most intracellular Ca2+ is bound and the low cell ionized Ca2+ concentration (approximately 0.2 microM) is maintained by a combination of low membrane permeability and a powerful Ca2+ -pump. This pump has been identified with a (Ca2+ + Mg2+)-stimulated ATPase, and both Ca2+ transport and ATP splitting are stimulated by calmodulin, a low molecular weight protein which binds Ca2+ avidly and activates many Ca2+ -dependent enzymes. Both high and low affinity kinetics for Ca2+ pumping have been demonstrated, depending on the extent of binding of calmodulin to the pump. A stoichiometry of either 1 or 2 Ca2+ ions pumped per ATP molecule split has been shown, and the value may vary with the level of intracellular Ca2+. Phenothiazines, such as chlorpromazine inhibit the Ca2+ -pump by antagonizing the increment in activity produced by calmodulin. The passive inward leak of Ca2+ into erythrocytes can be quantitated by 45Ca2+ uptake into red cells whose Ca2+ -pump has been inhibited. Estimates of the Ca2+ permeability, based on unidirectional influx, yield values many orders of magnitude lower than for nucleated cells. Influx of Ca2+ into human erythrocytes occurs by a facilitated diffusion process, which can be inhibited by phenothiazines and the cinchona alkaloids. Calcium affects many membrane functions including cation permeability, lipid composition and some cytoskeletal interactions which may determine cell shape. Any rise in intracellular Ca2+ activates a specific K+ channel which normally makes little contribution to K+ fluxes. Kinetic studies of this process demonstrate either high or low affinity Ca2+ -activation of K+ efflux, with low affinity of the channel to Ca2+ being the probable state in vivo. Propranolol is the best known activator of Ca2+ -stimulated K+ efflux, although the mechanism of stimulation is unclear. Like other tissues, red cells possess a Ca2+ -activated phosphoinositol phosphodiesterase. Although it has been suggested that the echinocytic shape change induced by Ca2+ is due to the hydrolysis of polyphosphoinositides, it seems more likely that this shape change results from an effect of Ca2+ on the macromolecular interactions of the cytoskeleton. Abnormal Ca2+ permeability may contribute to red cell destruction in a variety of diseases. For example, in sickle cell anemia a large Ca2+ influx occurs when cells are sickled under deoxy conditions, and moreover, the ability of the Ca2+ -pump to extrude the increment of cell Ca2+ is impaired. Thus, red cell Ca2+ is increased 3-7-fold above normal and this may contribute to the short survival of sickle red cells...

Anemia, Hemolytic↗

PubMed1995

Glucose transporter gene expression: regulation of transcription and mRNA stability.

The facilitated diffusion of D-glucose across the plasma membrane is carried out by a set of stereospecific transport proteins known as the glucose transporters. These integral membrane proteins are members of a gene family where tissue-specific expression of one or more members will determine in part the net rate of glucose entry into the cell. The regulation of glucose transporter gene expression is a critical feature of cellular homeostasis, as defects in specific transporter expression can lead to profound alterations in cellular physiology. In this review, we provide a brief descriptive background on the family of glucose transporters and examine in depth the regulation of the two transporters expressed in adipose tissue, GLUTI, a basal growth-related transporter and GLUT4, the insulin-responsive glucose transporter.

Animals↗

PubMed1996

Localization and ontogeny of GLUT3 expression in the rat retina.

This study investigates the presence, localization, and developmental expression of a neuron-specific facilitated-diffusion glucose transporter, GLUT3, in the rat retina so as to elucidate molecular mechanisms regulating glucose homeostasis in support of the visual function. Immunoblot analysis using anti-GLUT3 antibody (ALM3-C) revealed the presence of GLUT3 as a heterogeneously glycosylated protein with an average molecular weight of approximately 44 kDa. Although immunofluorescence staining showed it to be localized primarily in the inner and outer plexiform layers, some of the cell bodies in the inner nuclear layer also showed weak immunoreactivity. Immunoblot analysis of developing rat retinal tissues revealed the presence of the GLUT3 protein as early as embryonic day 15 (E15), and immunofluorescence staining revealed its expression in the inner plexiform layer near the time of birth and in the outer plexiform layer at postnatal day 14 (P14), i.e., when the eyes normally open and retinal activity commences. The protein's abundance remained at a relatively low level during the embryonic stages and up until the end of the first postnatal week (P7), though a transient increase was confirmed to occur at E18. From P13, however, the abundance steadily increased, rapidly reaching the adult level at P24. Based on these observations, we hypothesize that GLUT3 is expressed in some subsets of retinal neurons, being preferentially abundant in their neuronal processes, and that its ontogeny is closely associated with morphological and functional development of the retina. As such, this suggests that GLUT3 plays some important role(s) in the retina where glucose metabolism is essential.

Animals↗

PubMed1987

Identification and characterization of a ribose transport system in Leishmania donovani promastigotes.

A transport system for ribose in Leishmania donovani promastigotes was identified and characterized by measuring the uptake of radioisotope-labeled ribose. The pentoses arabinose, 2-deoxyribose and xylose inhibited ribose uptake, whereas hexoses (glucose, alpha-methylglucoside, thioglucose, galactose, lactose, maltose, mannose), adenosine, and proline did not inhibit uptake, indicating that the transporter exhibited substrate specificity. Intracellular ribose exchanged with 2-deoxyribose. Uptake of ribose showed saturation kinetics with an apparent Km = 2 mM and Vmax = 11 nmol (mg protein)-1 min-1. Both N-ethylmaleimide and p-hydroxymercuribenzoate inhibited ribose uptake which was prevented by dithiothreitol. The uncoupling agents 2,4-dinitrophenol and carbonylcyanide p-(trifluoromethoxy)phenylhydrazone and a variety of inhibitors of energy-driven transport had no significant effect on ribose uptake. Following transport, the intracellular ribose pool contained two-thirds of the sugar in the phosphorylated form and one-third in the neutral form. These cumulative results indicate that a specific carrier mediates ribose uptake via a facilitated diffusion system in L. donovani promastigotes.

Animals↗

PubMedDate not supplied

Active transport of 2-deoxy-D-glucose in Trypanosoma brucei procyclic forms.

The characteristics of glucose transport by procyclic forms of Trypanosoma brucei were examined in a rapid transport assay using the glucose analogue 2-deoxyglucose. In contrast to bloodforms where the Km for 2-deoxyglucose transport is about 1 mM, procyclic forms have a Km of about 38 microM. Procyclic forms show temperature-dependent, saturable import, and import of 2-deoxyglucose is competitive with glucose and mannose. Unlike the bloodforms which employ facilitated diffusion, the procyclic forms actively transport glucose. Use of inhibitors and ionophores suggests that a protonmotive force is required for glucose transport in procyclic forms. Unlike the human erythrocyte glucose transporter, the glucose transporter of the T. brucei procyclic form is relatively insensitive to inhibition by cytocholasin B.

Animals↗