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At least 973 records · Page 54Linked to original sources
PubMed2000

Transforming growth factor-beta stimulates inorganic phosphate transport and expression of the type III phosphate transporter Glvr-1 in chondrogenic ATDC5 cells.

Members of the transforming growth factor (TGF)-beta family are important regulators of skeletal development. In this study, we investigated the effect of TGF-beta1 on inorganic phosphate (Pi) transport and on expression of the type III Pi carriers Glvr-1 and Ram-1 in murine ATDC5 chondrocytes. TGF-beta1 induced a selective, dose- and time-dependent increase in sodium-dependent Pi transport in ATDC5 cells. This response was dependent on RNA and protein synthesis and reflected a change in the maximal rate of the transport system, suggesting that TGF-beta1 induces the synthesis of new Pi carriers and their insertion into the plasma membrane. Consistently, Northern blotting analysis showed a dose-dependent increase in Glvr-1 messenger RNA expression in response to TGF-beta1, which preceded the maximal stimulation of Pi transport by several hours. Glvr-1 thus likely mediates at least part of the increase in Pi uptake induced by TGF-beta1. Ram-1 messenger RNA expression was not affected by TGF-beta1. TGF-beta1 activated the Smad signaling pathway and the mitogen-activated protein kinases ERK and p38 in ATDC5 cells. Unlike the regulation of Pi transport by receptor tyrosine kinase agonists in osteoblasts, the effect of TGF-beta1 on Pi uptake in ATDC5 cells did not involve protein kinase C or mitogen-activated protein kinases, suggesting that a specific, possibly Smad-dependent, signal mediates this response. In conclusion, TGF-beta1 stimulates Pi transport and Glvr-1 expression in chondrocytes, suggesting that, like proliferation, differentiation, and matrix synthesis, Pi handling is subject to regulation by TGF-beta3 family members in bone-forming cells.

Animals↗
PubMed1975

Active transport of potassium by the Cecropia midgut; tracer kinetic theory and transport pool size.

1. Tracer influx kinetics have been analysed theoretically to determine the size of the transport pool with no assumptions regarding the transport pathway. 2. For a calculation of the size of the transport pool to be made, the following six conditions are required by the theory: tracer steady state attained, tissue steady state attained, Isc measures next flux, small magnitude and constant time-course of efflux, and correction for decay in pumping rate. 3. The size of the pool, SI, is given by the steady state influx, Finfinity, divided by the mixing-time constant, alpha. 4. Some experimental results are analysed by three different graphical methods, and it is shown that these three methods are equivalent. Specifically, alpha is equal to the reciprocal of the 75% mixing time, t75, divided by 1n 4 and is equal to the reciprocal of the lag time, X. 5. The tracer kinetic theory is applied to active potassium transport across the isolated short-circuited midgut: the transport meets the six conditions required by the theory. 6. The size of the transport pool of potassium in one midgut is calculated to be 80.5 muequiv./g wet weight under high-K steady-state conditions. A value as high as this suggests that the pool is intracellular.

Animals↗
PubMed1975

An analysis of air transport results in the sick newborn infant: Part I. The transport team.

Regionalization of neonatal intensive care has necessitated air transport of the critically ill infant in sparsely populated areas. All newborn air transports to four Denver area newborn intensive-care units over a 14-month period were reviewed. An emergency-care nurse and a neonatal intensive-care nurse provided the basic transport team with physician assistance in selected cases. Infants were evaluated and stabilized at the referring hospital before moving the infant. The transports were analyzed for the type of air craft utilized, reason for referral, and mortality. The results indicate that prior planning will permit the use of the most appropriate aircraft and transport team. When using well-trained transport personnel, the presence of a physician may be limited to specific situations without adversely affecting overall neonatal mortality.

Aircraft↗
PubMed1992

Glucose transporter oligomeric structure determines transporter function. Reversible redox-dependent interconversions of tetrameric and dimeric GLUT1.

This study investigates the relationship between human erythrocyte glucose transport protein (GLUT1) oligomeric structure and glucose transporter function. Oligomeric structure was analyzed by hydrodynamic studies of cholate-solubilized GLUT1, by chemical cross-linking studies of membrane-resident GLUT1 and by using conformation-specific antibodies. Transporter function (substrate binding) was analyzed by equilibrium cytochalasin B and D-glucose binding measurements. Erythrocyte-resident glucose transporter is a GLUT1 homotetramer, binds 1 mol of cytochalasin B/2 mol of GLUT1, and presents at least two binding sites to D-glucose. Native structure and function appear to be stabilized by intramolecular disulfide bonds and are preserved during GLUT1 purification by the omission of reductant. Native structure is independent of in vitro and in vivo membrane GLUT1 density but is transformed to dimeric GLUT1 by alkaline reduction. Dimeric GLUT1 binds 1 mol of cytochalasin B/mol of GLUT1, presents a single population of binding sites to D-glucose, and is obtained upon GLUT1 purification in the presence of reductant. Native structure and function are restored by treatment of dimeric GLUT1 with glutathione-disulfide (K0.5 glutathione disulfide = 29 microM). We propose that native structure is established prior to transporter translocation to the plasma membrane and that intrasubunit disulfide bonds promote cooperative subunit interactions that stabilize transporter structure and function.

Binding Sites↗
PubMed2004

Transport of 99mTc-MAG3 via rat renal organic anion transporter 1.

UNLABELLED: Recently, complementary DNA (cDNA) encoding a p-aminohippurate (PAH) transporter designated rat organic anion transporter 1 (OAT1) was isolated. OAT1, a multispecific organic anion transporter at the basolateral membrane, is exclusively expressed in the middle segment of the proximal tubule in the rat kidney. It has been proposed that OAT1 is indirectly involved in PAH uptake via the Na(+) dicarboxylate cotransporter. In this study, in molecular biologic experiments using OAT1-expressing Xenopus laevis oocytes, we obtained evidence that (99m)Tc-mercaptoacetylglycylglycylglycine (MAG3) is transported via OAT1. METHODS: Capped OAT1 complementary RNA (cRNA) was synthesized from library plasmid cDNA linearized with BamHI using in vitro transcription. Defolliculated oocytes were injected with 10 ng of OAT1 cRNA. Two to 3 d after injection, uptake of (99m)Tc-MAG3 was measured using ND96 solution containing 18.5 kBq of (99m)Tc-MAG3. Before the uptake experiments, OAT1-expressing oocytes were preincubated for 2 h with 1 mmol/L glutarate (a dicarboxylate), to generate an outwardly directed glutarate gradient. Then, after incubation for 60 min at room temperature, radioactivity of oocytes was determined. For the inhibition experiments, uptake was assessed in the absence or presence of inhibitor: 2 mmol/L of PAH, o-iodohippurate (OIH), probenecid, 3,5-diiodo-4-pyridone-N-acetate (iodopyracet), furosemide, ethacrynic acid, glucoheptonate, maleic acid, L-Tyr, or tetraethylammonium (TEA) or 0.1 mmol/L of 2,4-dinitrophenol (DNP). RESULTS: Na(+) had a significant effect on (99m)Tc-MAG3 uptake (P < 0.05). Accumulated glutarate stimulated simultaneous (99m)Tc-MAG3 uptake and glutarate excretion (P < 0.001). The following compounds significantly inhibited (99m)Tc-MAG3 uptake: PAH, 8.5% +/- 16.2% of (99m)Tc-MAG3 uptake in the absence of an inhibitor; OIH, 26.4% +/- 21.7%; probenecid, 29.1% +/- 12.4%; iodopyracet, 15.8% +/- 7.9%; furosemide, 30.5% +/- 15.7%; ethacrynic acid, 21.6% +/- 10.6%; glucoheptonate, 35.6% +/- 22.6%; and maleic acid, 60.1% +/- 18.7%. (99m)Tc-MAG3 accumulation in Xenopus laevis oocytes was not significantly inhibited by TEA, L-Tyr, or DNP. CONCLUSION: The following substances had a cis-inhibitory effect on (99m)Tc-MAG3 transport: PAH, OIH, probenecid, iodopyracet, furosemide, ethacrynic acid, and glucoheptonate. Glutarate had a trans-stimulative effect on (99m)Tc-MAG3 transport. (99m)Tc-MAG3 acts as a substrate of OAT1, an organic anion/dicarboxylate exchanger.

Animals↗
PubMed1992

Transepithelial transport of oral cephalosporins by monolayers of intestinal epithelial cell line Caco-2: specific transport systems in apical and basolateral membranes.

The accumulation and the transepithelial transport of p.o. cephalosporins by monolayers of human intestinal epithelial cell line Caco-2 grown on microporous membrane filters were evaluated. Cephradine was accumulated concentratively in the monolayers from the apical side, and was transported to the basolateral side. The accumulation and the apical-to-basolateral transport of cephradine were temperature-dependent and sensitive to the pH of the apical side, with the optimal pH 6.0 to 6.5. The efflux of cephradine from the monolayers to the basolateral side was also temperature-dependent and was more rapid than its efflux to the apical side. The accumulation and the apical-to-basolateral transport of cephradine, cephalexin and cefixime, all p.o. agents, were significantly higher than those of cefotiam, a parenteral agent. The apparent Km and Vmax values for cephradine accumulation were 8.3 mM and 2.49 nmol/mg of protein per min, respectively. Dipeptides inhibited the accumulation and the apical-to-basolateral transport of cephradine. Both the accumulation and the efflux of cephradine in the monolayers were inhibited significantly by the sulfhydryl reagent p-chloromercuribenzene sulfonate. These findings suggest that p.o. cephalosporins accumulate in the Caco-2 cell monolayers via the H+/dipeptide cotransport system localized in the apical membranes and that a specific transport system is involved in the efflux of these antibiotics across the basolateral membranes.

Amino Acids↗
PubMed1990

Insulin regulation of hexose transport in mouse 3T3-L1 cells expressing the human HepG2 glucose transporter.

Complementary DNA encoding a HepG2 cell-facilitated glucose transporter (GLUT1) was subcloned into a metal-inducible, mammalian expression vector, pLEN. Mouse 3T3-L1 fibroblasts transfected with this new construct, pLENGT, exhibited zinc-inducible expression of human glucose transporter mRNA, protein, and glucose transport activity, before and after differentiation into adipocytes. Both mouse host GLUT1 and expressed human GLUT1 proteins distributed about equally between 3T3-L1 adipocyte plasma membranes and low density microsomal membranes, while host skeletal muscle/adipocyte-type glucose transporter (GLUT4) was concentrated in the latter fraction. Mouse GLUT1 and GLUT4 proteins and the constitutively expressed human GLUT1 protein in pLENGT adipocytes were all redistributed from low density microsomal membrane to plasma membrane fractions in response to insulin. Insulin stimulated 2-deoxyglucose uptake in untransfected fibroblasts about 2-fold, while untransfected adipocytes displayed a 14-fold increase in deoxyglucose uptake in response to insulin. Both the expression of human GLUT1 protein and basal 2-deoxyglucose uptake by 75 microM zinc-treated pLENGT fibroblasts and adipocytes were increased approximately 3-fold over untransfected cells. In such pLENGT fibroblasts expressing human GLUT1 protein, however, the absolute values for insulin-stimulated increases in sugar uptake were no different than in control fibroblasts. As was observed in pLENGT fibroblasts, the increased basal sugar uptake by pLENGT adipocytes was additive with the insulin-stimulated increase in the rate of sugar uptake and, therefore, the -fold stimulation by insulin was markedly reduced. These data indicate that: 1) the membrane distributions of a glucose transporter protein, which is not responsive to insulin in HepG2 cells, and both mouse GLUT1 and GLUT4 glucose transporter isoforms are regulated by insulin in mouse 3T3-L1 adipocytes, and 2) the expressed human GLUT1 appears to contribute significantly to the rate of basal uptake but not to the insulin-stimulated increase in 2-deoxyglucose uptake by 3T3-L1 fibroblasts and adipocytes.

Adipose Tissue↗
PubMed1990

Stimulation of glucose transport and glucose transporter phosphorylation by okadaic acid in rat adipocytes.

Okadaic acid, an inhibitor of Type I and IIa protein phosphatases, was recently found to stimulate 2-deoxyglucose uptake in rat adipocytes (Haystead, T. A. J., Sim, A. T. R., Carling, D., Honnor, R. C., Tsukitani, Y., Cohen, P., and Hardie, D. G. (1989) Nature 337, 78-81). In the present experiments the effect of okadaic acid on the phosphorylation and subcellular distribution of the insulin-regulatable glucose transporter (IRGT) was investigated. At maximally effective concentrations, insulin and okadaic acid increased the amount of IRGT in the plasma membrane by 10- and 4-fold, respectively. Thus, the stimulation of glucose transport by okadaic acid was apparently due to an increase in the surface concentration of the IRGT. However, despite its stimulatory actions, okadaic acid partially inhibited the ability of insulin to enhance glucose transport and translocation of the transporter. When cells were incubated with okadaic acid alone or in combination with insulin, phosphorylation of the IRGT in the plasma membrane was increased by approximately 3-fold relative to the intracellular pool of transporters in control cells. Phosphorylation of the IRGT was confined to the presumed cytoplasmic domain at the COOH terminus of the protein. Glucose transporters were dephosphorylated in vitro by Type I or Type IIa protein phosphatases, indicating that inhibition of one or both of these phosphatases could account for the increased phosphorylation produced by okadaic acid. The observation that okadaic acid stimulated translocation of the IRGT implicated a serine/threonine phosphorylation event in triggering movement of the intracellular IRGT-containing vesicles (GTV) to the cell surface. Immunoadsorption of GTV from 32P-labeled adipocytes revealed that the IRGT was the major phosphoprotein in these vesicles. The phosphorylation of at least three other GTV proteins was increased by okadaic acid, and these species would appear to be candidates for regulators of GTV movement to the plasma membrane. It is unlikely that phosphorylation of the IRGT is the signal for translocation because insulin did not increase phosphorylation of the protein. Rather, the inhibitory effect of okadaic acid on insulin-stimulated translocation is consistent with the hypothesis that phosphorylation of the IRGT promotes its internalization.

Adipose Tissue↗
PubMed1990

Isolation of polyamine transport-deficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins.

Escherichia coli KK313, which was deficient in spermidine transport, was isolated by treatment of E. coli MA261 with N-methyl-N'-nitro-N-nitrosoguanidine. E. coli NH1596, which was deficient in spermidine transport and has a 90% decreased putrescine transport activity, was obtained by a second treatment of E. coli KK313 with the same mutagen. Genes for polyamine transport systems were isolated by transforming E. coli NH1596 through DNA fragments from E. coli DR112 using pACYC184 as a vector. One clone for the gene of protein(s) catalyzing both putrescine and spermidine uptake (pPT104) was isolated. Two clones for the genes of protein(s) catalyzing only putrescine uptake (pPT79 and pPT71) were obtained. The genes encoded by pPT104, pPT79, and pPT71 were mapped at 15, 19, and 16 min of E. coli chromosome, respectively. Spermidine uptake by NH1596 carrying pPT104, and by MA261, was not inhibited by putrescine and several polyamine analogues, and the Kt values of these two systems were both approximately 0.1 microM. Putrescine transport by NH1596 carrying pPT104 was inhibited completely by spermidine, N,N-dimethyl-4,4'-bipyridylium (paraquat), and N1-acetyl-spermidine, and the Kt value was 1.4 microM. Putrescine uptake by NH1596 carrying pPT79 or pPT71 was not inhibited by spermidine and several polyamine analogues, and the Kt values were 0.5 and 1.8 microM, respectively. In MA261, the putrescine uptake was inhibited by 25-35% by paraquat and N1-acetyl-polyamines and showed two Kt values, 0.5 and 1.5 microM. Based on these findings, the polyamine transport systems of E. coli are discussed.

Bacterial Proteins↗
PubMed1979

Insulin and glucagon stimulation of amino acid transport in isolated rat hepatocytes. Synthesis of a high affinity component of transport.

Insulin and glucagon stimulate amino acid transport in freshly prepared suspensions of isolated rat hepatocytes. The kinetic properties of alpha-amino[1-14C]isobutyric acid (AIB) transport were investigated in isolated hepatocytes following stimulation by either hormone in vitro. In nonhormonally treated cells (i.e. basal state), saturable transport occurred mainly through a low affinity (Km approximately equal to 40 mM) component. In insulin or glucagon-treated hepatocytes, saturable transport occurred through both a low affinity component (similar to that observed in the basal state) and a high affinity (Km approximately equal to 1 mM) component. At low AIB concentrations (less than 0.5 mM), insulin and glucagon at maximally stimulating doses increased AIB uptake about 2-fold and 5-fold, respectively. The high affinity component induced by either hormone exhibited the properties of the A (alanine preferring) mediation of amino acid transport. This component required 2 to 3 h for maximal expression, and its emergence was completely prevented by cycloheximide. Half-maximal stimulation was elicited by insulin at about 3 nM and by glucagon at about 1 nM. Dibutyryl cyclic AMP mimicked the glucagon effect and was not additive to it at maximal stimulation. Maximal effects of insulin and glucagon, or insulin and dibutyryl cyclic AMP, were additive. We conclude that insulin and glucagon can modulate amino acid entry in hepatocytes through the synthesis of a high affinity transport component.

Amino Acids↗
PubMed1984

Induction and decay of amino acid transport in the liver. Turnover of transport activity in isolated hepatocytes after stimulation by diabetes or glucagon.

System A-mediated amino acid transport in liver tissue is stimulated by diabetes or by exogenous glucagon. The present report describes the decay process for stimulated System A activity in isolated rat hepatocytes. Transport induced by glucagon, insulin, or spontaneous diabetes (BB/G rats) decayed rapidly after initiation of primary cultures; the estimated half-life was about 1.5 h. In contrast, the stimulated activity in cultured hepatocytes from streptozotocin-diabetic rats had a half-life of about 2.5 h. It is not known if the loss of System A activity is the result of proteolysis or of another form of inactivation. The decay was blocked by either actinomycin or cycloheximide, but was unaffected by leupeptin, methylamine, chloroquine, dinitrophenol, rotenone, or tunicamycin. Studies with cycloheximide and actinomycin suggest the following: 1) within 30 min after initiation of cell cultures, synthesis of the corresponding mRNA for the transport-inactivating protein has begun; 2) the mRNA for transport-inactivating protein is relatively long-lived, but the inactivating protein itself has a half-life of less than 1 h; and 3) actinomycin blocks the decay through inhibition of transport-inactivating protein biosynthesis rather than by protection of the mRNA for the protein responsible for System A activity. A working model for the synthesis and decay of System A activity is presented. Cationic amino acid transport, System y+, was also stimulated severalfold after induction of diabetes or glucagon injection of rats. Systems ASC, X-, and N were enhanced to varying degrees in hepatocytes from diabetic or glucagon-injected rats, but the level of stimulation for each was not as great as that found for Systems A or y+.

Amino Acids↗
PubMedDate not supplied

[Electron paramagnetic resonance of electron transport in photosynthetic systems. XI. Effects of photosynthetic control: dependence of the rate of electron transport on the energization of bean chloroplast thylakoid membrane].

The kinetics of light-induced P700 redox transients in bean chloroplast was studied. It has been shown that the rate of electron transport decreased during few seconds of illumination of coupled chloroplasts without addition of ADP and inorganic phosphate. The evidence were obtained that there is a feedback inhibition of electron transport governed by the internal pH of thylakoid. This results in the overshoot in the kinetics of P700 redox transients induced by continuous actinic light. Under the phosphorylation condition (addition of Mg-ADP and inorganic phosphate) the effect of decreasing of the rate of electron transport between two photosystems was not observed. Addition of uncouplers (FCCP or gramicidine) also increased the steady-state rate of noncyclic electron transport. After adding only Mg-ADP (without phosphate) or Mg-ATP to coupled chloroplasts the effect of the light-driven inhibition of electron transport was observed as in the case of chloroplasts without any additions. We showed that the regulation for the electron transport rate was realized at the step of the plastoquinol oxidation by photosystem 1. Light-driven energization of the thylakoid membrane also leads to the the slowing of the reduction of spin label TEMPO. Evidences were obtained that TEMPO interacts with the semiquinone localized in the acceptor side of photosystem 2. From the comparative study of P700+ and TEMPO reduction by photosystem 2 we have concluded that there are two points of inhibitory action of DCMU localized at the acceptor and donor sides of photosystem 2. The mechanisms of photosynthetic control and the role of transmembrane proton gradient for energy transmission in chloroplasts are discussed.

Adenosine Diphosphate↗
PubMed1984

[Systems of membrane transport, genetics and nutrition; the example of congenital anomalies of intestinal transport in children].

As the plasma membrane of the cell, the intestinal epithelium ensures the selective functions of the entry and exit of nutriments or metabolites. These functions are controlled genetically by structural genes and eventually by regulatory genes which direct the expression of the former. The influence of some essential nutriments also plays a role. These aspects are illustrated for microorganisms. Selective, congenital intestinal malabsorptions, which are hereditary, occur in humans; their study leads to a better understanding of the genetic and nutritional control of transport mechanisms. Known anomalies of the intestinal transport of basic amino acids have been studied by showing the probable relationships with selective reabsorption deficiencies in the renale tubule and possible disorders of the urea cycle. Amino acid transport through the intestinal epithelium may be under a dual genetic control i.e. at the brush border (co-transport with sodium) as well as at the basal-lateral membrane (diffusion). It is emphasized that small peptides must be present in dietary solutions of enteral origin for amino acid absorption to be optimal. Selective malabsorption of glucose and galactose due to loss of the co-transport systems of glucose-sodium and galactose-sodium at the brush border is discussed. A comparison is made with anomalies of glucose reabsorption in the renal tubule. The digestive consequences (watery diarrhea) of the absence of sodium co-transports has been underlined. A generalization is proposed.

Amino Acids↗
PubMed1983

Characterization of ascorbic acid transport by adrenomedullary chromaffin cells. Evidence for Na+-dependent co-transport.

Ascorbic acid transport by bovine adrenomedullary chromaffin cells in primary cultures has been characterized. Ascorbic acid uptake can be measured by either high performance liquid chromatography with electrochemical detection or radiometric techniques with L-[1-14C]ascorbic acid. The transport system is temperature- and energy-dependent and exhibits Michaelis-Menten kinetics with an apparent Km of 29 microM when the external Na+ concentration is 150 mM. Uptake of ascorbate by chromaffin cells is ouabain-sensitive and dependent on the presence of external Na+. Ascorbate transport by chromaffin cells is, thus, an active process driven by the Na+ electrochemical gradient. The kinetics of this co-transport system fits an "affinity type" model where binding of Na+ to the carrier increases the affinity to ascorbate and vice versa. Thus, the data suggest that binding of either Na+ or ascorbate induces a conformational change in the transporter, which results in a change in the association constant for the second ligand while the mobility of the carrier remains unchanged. Cellular uptake of ascorbate into adrenomedullary chromaffin cells appears to be followed by its distribution into several subcellular compartments. One subcellular compartment for concentration of ascorbate is the chromaffin vesicle where it accumulates at a relatively slow rate. The interrelationships between ascorbate transport and other aspects of ascorbate metabolism and chromaffin vesicle function and dopamine beta-hydroxylation are also considered.

Adrenal Medulla↗
PubMed1982

pH gradient-dependent phosphate transport catalyzed by the purified mitochondrial phosphate transport protein.

The mitochondrial phosphate transport protein (Wohlrab, H. (1980) J. Biol. Chem. 255, 8170-8173), which co-purifies with the adenine nucleotide translocase, has been isolated with a modified procedure resulting in an increased yield and in a preparation that is stable to storage in liquid nitrogen. The phosphate transport protein was incorporated into liposomes (phosphatidylethanolamine/phosphatidylcholine/phosphatidic acid, 2.75:1:1), and phosphate/phosphate exchange rates were determined. With pHe (extraliposomal) = pHi (intraliposomal) = 7.2, we found a Km of 2.5 mM independent of [(Pi)i] and a Vmax of 12 mumol/min . mg of protein. Parallel phosphate transport experiments were carried out with liposomes containing phosphate transport protein isolated from mitochondria inhibited by N-ethylmaleimide. Phosphate transported unidirectionally [pHe = pHi = 6.8; = 1.0 mM, (Pi)i = 0 mM] reaches a maximum at 30 s and is 0.13 and 0.05 mumol/mg for active and inhibited protein, respectively. At pHe = 6.8 and pHi = 8.0, the respective amounts are 0.45 and 0.05. At pHe = 8.0, the uptake becomes the same with active and inhibited protein (pHi = 6.8, 0.15 and 0.14; pHi = 8.0, 0.25 and 0.20). At all the above pH values, about the same uptake is observed with liposomes prepared without protein as those prepared with inhibited protein. The initial rate of protein catalyzed unidirectional flux [(Pi)e = 1.0 mM, pHe = 6.8; (Pi)i = 0 mM, pHi = 8.0) is 2 mumol/min . mg of protein or 8 mumol/min . mg of phosphate transport protein estimated without the adenine nucleotide translocase.

Animals↗
PubMed1982

Riboflavin transport by rabbit kidney slices: characterization and relation to cyclic organic acid transport.

The transport of riboflavin and the relationship of riboflavin transport to the transport of the cyclic organic acids, aminohippurate and penicillin, were investigated in small renal slices in vitro. Riboflavin was accumulated by rabbit renal slices by a transport system that was inhibited by sugar-containing and sugarless flavins, cyclic organic acids including aminohippurate and penicillin, dinitrophenol and cold temperatures, but not by D-ribose or the weak base tolazoline. The transport of riboflavin into renal slices was not solely due to intracellular binding or metabolism of the riboflavin. Aminohippurate, penicillin and riboflavin inhibited the active accumulation of [14C] aminohippurate and [14C]penicillin by kidney slices. These studies support the notions that: 1) riboflavin is accumulated in kidney cortex slices by an energy-dependent saturable transport system; 2) riboflavin accumulation by kidney slices is inhibited by cyclic organic acids and sulfhydryl reagents, but not weak bases; and 3) riboflavin is a competitive inhibitor of aminohippurate as well as an inhibitor of penicillin G accumulation by kidney slices.

Aminohippuric Acids↗
PubMed1982

Expression of a differentiated transport function in apical membrane vesicles isolated from an established kidney epithelial cell line. Sodium electrochemical potential-mediated active sugar transport.

Electrogenic Na+ gradient-stimulated active accumulation of alpha-methyl-D-glucopyranoside was demonstrated using apical membrane vesicles isolated from an established kidney epithelial cell line (LLC-PK1). Apical membrane vesicles were purified from densely confluent cell cultures after cell disruption by nitrogen cavitation using a rapid Mg2+ differential precipitation procedure. Such preparations were 11-fold enriched in apical-specific enzyme markers, were not enriched in basolateral-specific markers, and were relatively free from contamination by intracellular membranes. Sugar accumulated within vesicles was sensitive to osmotic pressure differences across the membrane. alpha-Methyl-D-glucopyranoside transport activity in vesicles exhibited similar hexose specificities and sensitivity to inhibition by phlorizin to the corresponding transport system expressed in intact LLC-PK1 cells and in kidney proximal tubule. Vesicles prepared from subconfluent cultures, which have not yet developed the expression of this transport system, had diminished Na+-stimulated sugar transport activity yet expressed Na+-stimulated amino acid transport activity. Active accumulation as a function of increasing Na+ gradient and an interior-negative membrane potential suggested a stoichiometry between sugar and Na+ uptake of 1:2, respectively. Experimental generation of interior-negative membrane potentials in vesicles produced a further stimulation of sugar accumulation, consistent with an additive contribution from both a Na+ chemical gradient and an electrical membrane potential in energizing active sugar transport.

Animals↗
PubMed1980

Neonatal transport nurses: an analysis of their role in the transport of newborn infants.

From September 1976 to March 1979, nurses selected from the newborn intensive care unit (NICU) assumed the transport team leadership role for 443 newborns. Each nurse had successfully completed an eight-week didactic and practical educational program in the assessment, management, stabilization, and transport of ill newborns including premature infants, those with various medical and surgical disorders, and those requiring assisted ventilation. Physician supervision and consultation was always available. The overall survival rate for these infants was 81%, a rate similar to that for newborns transported by physicians. The transport nurses consistently demonstrated the ability to effectively assess, manage, stabilize, and transport ill newborns. In addition, their utilization was alleviated a physician shortage on the NICU, has improved the response time to transport requests, and has enhanced educational opportunities for physicians and nurses.

Education, Nursing, Continuing↗