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At least 667 records · Page 37Linked to original sources
PubMed2000

Gizzard myoglobin contents and feeding habits in avian species.

In an attempt to consider physiological function of myoglobin (Mb), we determined Mb contents of gizzard smooth muscles with special reference to feeding habits in 85 avian species of 19 orders. The Mb content in 44 species of herbivorous birds was 7.52+/-3.81 mg/g wet muscle, which was significantly higher than the value of 2.34+/-1.74 mg/g in 41 species of carnivorous ones (P<0.001). Buffering capacity, as determined by in vitro titration method, was 37.3+/-5.5 slykes/g in gizzard smooth muscles of 75 species and 60.7+/-10.5 slykes in breast skeletal muscles of 77 species (P<0.001), which suggests a significantly higher dependence, almost comparable to cardiac muscles, of the gizzard muscular function on aerobic metabolism. Together with the fact that blood circulation in the gizzard is very low at resting, and might be further limited during activity, we conclude that the higher Mb content in gizzards of herbivorous birds is an adaptation, to allow storage and/or facilitated diffusion of oxygen, during process of high mechanical work required to grind down hard and fibrous vegetable food under the conditions of limited circulatory supply.

Adaptation, Physiological↗
PubMed2002

Fine-tuning the RAS signaling pathway: Zn(2+) makes the difference.

In the May, 2002 issue of Developmental Cell, Bruinsma et al. report that the CDF-1 cation diffusion facilitator protein is required for efficient Ras-mediated signaling in C. elegans. CDF-1 reduces intracellular Zn(2+) levels, indicating an inhibitory effect of Zn(2+) on the Ras pathway.

Animals↗
PubMed2006

Sequence similarity and functional relationship among eukaryotic ZIP and CDF transporters.

ZIP (ZRT/IRT-like Protein) and CDF (Cation Diffusion Facilitator) are two large metal transporter families mainly transporting zinc into and out of the cytosol. Several ZIP and CDF transporters have been characterized in mammals and various model organisms, such as yeast, nematode, fruit fly, and zebrafish, and many candidate genes have been identified by genome projects. Unexpected functions of ZIP and CDF transporters have been recently reported in some model organisms, leading to major advances in our understanding of the functions of mammalian counterparts. Here, we review the recent information on the sequence similarity and functional relationship among eukaryotic ZIP and CDF transporters obtained from the representative model organisms.

Animals↗
PubMed1987

Environmental sodium regulates cutaneous sugar transport in a digenean fluke.

Glucose uptake was examined in adult specimens of Proterometra macrostoma (Trematoda: Digenea) recovered from the stomach (endoparasites) and gills (ectoparasites) of longear sunfish, Lepomis megalotis. The endoparasitic forms transported glucose directly through the external body surface by Na+-independent, facilitated diffusion, but the ectoparasites absorbed glucose by free diffusion alone. To determine how this transport function is regulated, cercariae were incubated in solutions having Na+ concentrations normally found in fish gut (50 mM) and in fresh water (0.5 mM). Glucose transport capacity was retained in 50 mM Na+, but disappeared in worms incubated for 1-3 days in 0.5 mM Na+. Returning worms from the latter solution to one containing 50 mM Na+ fully restored glucose transport within a day. By contrast, incubation up to 5 days in 0.5 mM Na+ had no effect on glucose transport in endoparasitic adults of P. macrostoma and cercariae of P. edneyi. Thus, cutaneous sugar transport function in the migrating larva of P. macrostoma is subject to indirect regulation by environmental Na+.

Animals↗
PubMed2006

Characterization of D-glucose transport in Trypanosoma rangeli.

Like in other trypanosomatids D-glucose is a crucial source of energy to Trypanosoma rangeli, a non-pathogenic parasite that in Central and South America infects triatomine vectors and different mammalian species, including humans. In several trypanosome species, D-glucose transporters were already described and cloned. In this study, we characterized the D-glucose transport activity present in 2 life-stage forms of T. rangeli (epimastigotes and trypomastigotes) using D-[U-14C]glucose as substrate. Our results indicate that T. rangeli transports D-glucose with high affinity in both epimastigote (Km 30 microM) and trypomastigotes (Km 80 microM) life-forms. Both transport activities were inhibited by Cytochalasin B and Phloretin, indicating that probably D-glucose uptake in T. rangeli is mediated by facilitated diffusion of the sugar. Significant differences were observed between epimastigotes and trypomastigotes in relation to their affinity for D-glucose analogues, and the predicted amino acid sequence of a putative D-glucose transporter from T. rangeli (TrHT1) showed a larger identity with the T. cruzi D-glucose transporter encoded by the TcrHT1 gene than with other transporters already characterized in trypanosomatids.

Amino Acid Sequence↗
PubMed1991

Mutations in endonuclease V that affect both protein-protein association and target site location.

A general mechanism by which proteins locate their target sites within large domains of DNA is a one-dimensional facilitated diffusion process in which the protein scans DNA in a nonspecifically bound state. An electrostatic contribution to this type of mechanism has been previously established. This study was designed to question whether other characteristics of a protein's structure might contribute to the scanning mechanism of target site location. In this regard, T4 endonuclease V was shown to establish an ionic strength dependent monomer-dimer equilibrium in solution. A protein dimer interaction site was postulated to exist along a putative alpha-helix containing amino acid residues 54-62. The conservative substitutions of Phe-60----Leu-60 and Phe-59, Phe-60----Leu-59, Leu-60 resulted in mutant enzymes which remained in the monomeric state independent of the ionic strength of the solution. The target site location mechanism of these mutants has also been altered. Under conditions where wild-type endonuclease V processively scans nontarget DNA, the target location mechanism of the monomeric mutant proteins was shifted toward a less processive search. This decrease in the processivity of the mutants was especially surprising because the nontarget DNA binding affinity was found to be significantly increased. Thus, an additional component of the endonuclease V DNA scanning mechanism appears to be the formation of a stable endonuclease V dimer complex.

Base Sequence↗
PubMed1991

Glycolysis and glucose uptake in intact outer segments isolated from bovine retinal rods.

Glucose transport across the plasma membrane of isolated bovine rod outer segments (ROS) was measured by uptake of 14C-labeled 3-O-methylglucose and 2-deoxyglucose and was inferred from deenergization of ROS with 2-deoxyglucose. Glucose transport was mediated by a facilitated diffusion glucose transporter that equilibrated external and internal free hexose concentrations. Glucose transport in ROS displayed two components as judged from kinetic analysis of hexose equilibration and as judged from inhibition by cytochalasin B and phloretin. Transport under exchange conditions was considerably faster as compared with net hexose uptake, similar to that observed for the erythrocyte glucose transporter. Sensitivity to cytochalasin B and affinity to 3-O-methylglucose were similar to those observed for the hepatocyte glucose transporter. The cytochalasin-insensitive component appears unique to ROS and did not reflect leakage transport as judged from a comparison with L-glucose uptake. Glucose transport feeds glycolysis localized to ROS. We suggest that a major role for glycolysis in ROS is phosphorylation of GDP to GTP via pyruvate kinase and PEP, while phosphorylation of ADP to ATP can use the creatine kinase/phosphocreatine pathway as well.

Adenosine Diphosphate↗
PubMed1991

Mechanistic coupling of transport and phosphorylation activity by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system.

Mannitol bound to enzyme IImtl could be trapped specifically by rapid phosphorylation with P-HPr. The assay was used to demonstrate transport of mannitol across the cytoplasmic membrane with and without phosphorylation of mannitol. The latter was 2-3 orders of magnitude slower. The fraction of bound mannitol molecules that was actually phosphorylated, the efficiency of the trap, was less than 50%. The efficiency was not very different for enzyme IImtl embedded in the membrane of vesicles with an inside-out orientation or solubilized in detergent. Subsequently, it is argued that the fraction of the bound mannitol molecules that was not phosphorylated dissociated into the cytoplasmic space. A model for the catalytic mechanism of enzyme IImtl is proposed on the basis of interpretations of the present experiments. The main features of the model are the following: (i) mechanistically, the coupling between transport and phosphorylation is less than 50%; (ii) in the physiological steady state of mannitol transport and metabolism, the coupling is 100%; (iii) phosphorylated enzyme IImtl catalyzes facilitated diffusion at a high rate; (iv) the state of phosphorylation of the cytoplasmic domain modulates the activity of the translocator domain; (v) the enzyme catalyzes phosphorylation of free cytoplasmic mannitol at least as fast as it catalyzes transport plus phosphorylation of free periplasmic mannitol.

Binding Sites↗
PubMed1985

Functional and immunochemical characterization of a mutant of Escherichia coli energy uncoupled for lactose transport.

Right-side-out cytoplasmic membrane vesicles from Escherichia coli ML 308-22, a mutant "uncoupled" for beta-galactoside/H+ symport [Wong, P. T. S., Kashket, E. R., & Wilson, T. H. (1970) Proc. Natl. Acad. Sci. U.S.A. 65, 63], are specifically defective in the ability to catalyze accumulation of methyl 1-thio-beta-D-galactopyranoside (TMG) in the presence of an H+ electrochemical gradient (interior negative and alkaline). Furthermore, the rate of carrier-mediated efflux under nonenergized conditions is slow and unaffected by ambient pH from pH 5.5 to 7.5, and TMG-induced H+ influx is only about 15% of that observed in vesicles containing wild-type lac permease (ML 308-225). Alternatively, ML 308-22 vesicles bind p-nitrophenyl alpha-D-galactopyranoside and monoclonal antibody 4B1 to the same extent as ML 308-225 vesicles and catalyze facilitated diffusion and equilibrium exchange as well as ML 308-225 vesicles. When entrance counterflow is studied with external substrate at saturating and subsaturating concentrations, it is apparent that the mutation simulates the effects of deuterium oxide [Viitanen, P., Garcia, M. L., Foster, D. L., Kaczorowski, G. J., & Kaback, H. R. (1983) Biochemistry 22, 2531]. That is, the mutation has no effect on the rate or extent of counterflow when external substrate is saturating but stimulates the efficiency of counterflow when external substrate is below the apparent Km. Moreover, although replacement of protium with deuterium stimulates counterflow in ML 308-225 vesicles when external substrate is subsaturating, the isotope has no effect on the mutant vesicles under the same conditions.(ABSTRACT TRUNCATED AT 250 WORDS)

Antibodies, Monoclonal↗
PubMed1986

Dissociation of the lactose repressor-operator DNA complex: effects of size and sequence context of operator-containing DNA.

The dissociation kinetics for repressor-32P-labeled operator DNA have been examined by adding unlabeled operator DNA to trap released repressor or by adding a small volume of concentrated salt solution to shift the Kd of repressor-operator interaction. The dissociation rate constant for pLA 322-8, an operator-containing derivative of pBR 322, was 2.4 X 10(-3) s-1 in 0.15 M KCl. The dissociation rate constant at 0.15 M KCl for both lambda plac and pIQ, each of which contain two pseudooperator sequences, was approximately 6 X 10(-4) s-1. Elimination of flanking nonspecific DNA sequences by use of a 40 base pair operator-containing DNA fragment yielded a dissociation rate constant of 9.3 X 10(-3) s-1. The size and salt dependences of the rate constants suggest that dissociation occurs as a multistep process. The data for all the DNAs examined are consistent with a sliding mechanism of facilitated diffusion to/from the operator site. The ability to form a ternary complex of two operators per repressor, determined by stoichiometry measurements, and the diminished dissociation rates in the presence of intramolecular nonspecific and pseudooperator DNA sites suggest the formation of an intramolecular ternary complex. The salt dependence of the dissociation rate constant for pLA 322-8 at high salt concentrations converges with that for a 40 base pair operator. The similarity in dissociation rate constants for pLA 322-8 and a 40 base pair operator fragment under these conditions indicates a common dissociation mechanism from a primary operator site on the repressor.

Base Sequence↗
PubMed1990

The membrane-bound domain of the phosphotransferase enzyme IImtl of Escherichia coli constitutes a mannitol translocating unit.

The orientation of the mannitol binding site on the Escherichia coli phosphotransferase enzyme IImtl in the unphosphorylated state has been investigated by measuring mannitol binding to cytoplasmic membrane vesicles with a right-side-out and inside-out orientation. Enzyme IImtl is shown to catalyze facilitated diffusion of mannitol at a low rate. At equilibrium, bound mannitol is situated at the periplasmic side of the membrane. The apparent binding constant is 40 nM for the intact membranes. Solubilization of the membranes in detergent decreases the affinity by about a factor of 2. Inside-out membrane vesicles, treated with trypsin to remove the C-terminal cytoplasmic domain of enzyme IImtl, showed identical activities. These experiments indicate that the translocation of mannitol is catalyzed by the membrane-bound N-terminal half of enzyme IImtl which is a structurally stable domain.

Binding Sites↗
PubMedDate not supplied

Overloaded hollow-fiber liquid chromatography.

Liquid chromatography in hollow fibers can separate solutes like flavors and proteins by using a stationary phase of organic solvent, sometimes containing reversed micelles. Such separations, which have a much smaller pressure drop than equivalent separations in packed beds, show dispersion consistent with chromatographic theories at low flows and dilute feeds. These separations behave less predictably at high flows and concentrated feeds, which overload the hollow fibers. The results for flavors correlate well with the Graetz number, consistent with available theories of chromatography and adsorption. The results for proteins correlate poorly with the Graetz number but better with a dimensionless flux based on facilitated diffusion in the stationary phase.

Absorption↗
PubMedDate not supplied

Improved performance of preordered fungal protease-stearic acid biocomposites: enhanced catalytic activity, reusability, and temporal stability.

In an earlier report on fungal protease (F-prot)-fatty acid biocomposite film formation [Gole et al. Anal. Chem. 2000, 72, 4301], it was observed that the biocatalytic activity of the immobilized enzyme was comparable to that of the free enzyme in solution. However, a somewhat negative aspect of the protocol was the steady loss in activity during reuse and storage of the biocomposite film. In this paper, we address the latter issues and demonstrate successful attempts toward the realization of efficient biocomposite films with enhanced biological activity, temporal stability, and excellent reusability. The improved performance of the F-prot-stearic acid biocomposite is accomplished by preordering the fatty acid film by incorporation of Pb(2+) ions into the lipid matrix prior to enzyme immobilization. The lead cation induces lamellar ordering in the lipid film and thus facilitates diffusion of the F-prot molecules into the lipid matrix and accessibility of the substrate molecules (hemoglobin, Hb) to the entrapped F-prot enzyme molecules. The preordering consequently leads to effective control of the "mass transport" problem and might be responsible for the enhanced biological activity ( approximately 36%) of the enzyme molecules in the biocomposite in comparison with the free enzyme in solution, as well the excellent reusability of the composite film. In addition to biocatalytic activity measurements, the formation and characterization of the F-prot-lead stearate biocomposite films was done by quartz crystal microgravimetry and X-ray diffraction.

Catalysis↗
PubMed2001

Fluoride content of foods made with mechanically separated chicken.

The goal of the present study was to determine the extent to which foods made with mechanically separated chicken can contribute to total fluoride intake. Fluoride content of each blended sample was determined with a fluoride combination electrode following perchloric-acid-facilitated diffusion of hydrogen fluoride. Infant foods had the highest fluoride content followed by chicken sticks, luncheon meats, and canned meats. A single serving of chicken sticks alone would provide about half of a child's upper limit of safety for fluoride. Fluoride content of foods made with mechanically separated chicken was significantly correlated with calcium content, which is consistent with the possibility that the mechanical separation process was the source of the extra fluoride. Foods made with mechanically separated turkey were not a major source of fluoride.

Animals↗
PubMed2006

Highly dispersed Pt catalysts on single-walled carbon nanotubes and their role in methanol oxidation.

Well-dispersed Pt catalysts with very high utilization efficiencies for fuel cell reactions have been prepared by ethylene glycol reduction on polymer-wrapped single-walled carbon nanotubes (SWCNTs). By wrapping the SWCNTs in a polymer such as polystyrene sulfonate, we are able to break up the nanotube bundles to achieve better dispersion. These polymer-wrapped SWCNTs with platinum nanoparticles deposited on them show very high electrochemically active surface areas. The increase in utilization efficiencies for platinum catalysts on these SWCNT supports can be attributed to the increased surface areas and the well-dispersed nature of the carbon support and catalyst. The catalyst dispersion facilitates diffusion of reactant species which in turn results in higher methanol oxidation currents and more positive potentials for oxygen reduction.

Letter↗
PubMed1999

Saturable transport of H2-antagonists ranitidine and famotidine across Caco-2 cell monolayers.

The purpose of this study was to investigate the mechanism by which the H2-antagonists ranitidine and famotidine interacted with the paracellular space during their transport across Caco-2 cell monolayers. Transport experiments with ranitidine and famotidine across Caco-2 cell monolayers were performed to determine the apical-to-basolateral flux at various concentrations. Kinetic analysis of the transport data showed that ranitidine and famotidine were transported by both saturable and nonsaturable processes. Na+, K+-ATPase inhibitor ouabain and metabolic inhibitors sodium azide + 2-deoxy-D-glucose did not affect ranitidine transport, suggesting that the active transport was not involved. Famotidine and some other guanidine-containing compounds, e.g., guanethidine, Arg-Gly, L-arginine methyl ester, and L-argininamide, inhibited the transport of ranitidine, whereas other guanidine-containing compounds with an additional negative charge, e.g., L-arginine, did not. 2,4, 6-Triaminopyrimidine (TAP), an inhibitor of paracelluar cationic conductance, also inhibited the transport of both ranitidine and famotidine. On the basis of these results, it is proposed that the saturable transport of ranitidine and famotidine across Caco-2 cell monolayers appears to be via a facilitated diffusion process mediated by the paracellular anionic sites. This mechanism is consistent with the observation that ranitidine and famotidine caused a concentration-dependent increase in transepithelial electrical resistance (TEER) across Caco-2 cell monolayers, presumably by blocking the paracellular anionic sites and thus inhibiting the flux of cations (e.g., Na+).

Biological Transport↗
PubMedDate not supplied

Eukaryotic zinc transporters and their regulation.

The last ten years have witnessed major advances in our understanding of zinc transporters and their regulation in eukaryotic organisms. Two families of transporters, the ZIP (Zrt-, Irt-like Protein) and CDF (Cation Diffusion Facilitator) families, have been found to play a number of important roles in zinc transport. These are ancient gene families that span all phylogenetic levels. The characterized members of each group have been implicated in the transport of metal ions, frequently zinc, across lipid bilayer membranes. This remarkable conservation of function suggests that other, as yet uncharacterized members of the family, will also be involved in metal ion transport. Many of the ZIP family transporters are involved in cellular zinc uptake and at least one member, the Zrt3 transporter of S. cerevisiae, transports stored zinc out of an intracellular compartment during adaptation to zinc deficiency. In contrast, CDF family members mediate zinc efflux out of cells or facilitate zinc transport into intracellular compartments for detoxification and/or storage. The activity of many of these transporters is regulated in response to zinc through transcriptional and post-transcriptional mechanisms to maintain zinc homeostasis at both the cellular and organismal levels.

Amino Acid Sequence↗
PubMed1994

Carrier-mediated transport of H1-antagonist at the blood-brain barrier: mepyramine uptake into bovine brain capillary endothelial cells in primary monolayer cultures.

The transport mechanism of the H1-antagonist mepyramine at the blood-brain barrier (BBB) was studied by using primary cultured monolayers of bovine brain capillary endothelial cells (BCEC). The initial uptake of [3H]mepyramine into the BCEC showed strong temperature and concentration dependency, indicating that it involves both saturable and nonsaturable processes. Transport at the luminal membrane may be the rate-limiting process in the transcellular transport, since the values of the uptake coefficient of [3H]mepyramine at the luminal membrane (609 microliters/mg protein/min) and the transcellular permeability coefficient (488 microliters/mg protein/min) are very similar. The initial uptake of [3H]mepyramine was not affected by metabolic inhibitors, but was stimulated by preloading with the drug. Mepyramine appears to be transported into the BCEC by a carrier-mediated transport system which does not require metabolic energy, probably via a facilitated diffusion mechanism.

Animals↗