Phosphate Transport Processes of Animal Cells

1982 ◽  
pp. 645-663 ◽  
Author(s):  
Peter L. Pedersen ◽  
Janna P. Wehrle
Keyword(s):  
Phosphate Transport ◽  
Transport Processes ◽  
Animal Cells

Presence of multiple sodium-dependent phosphate transport processes in proximal brush-border membrane

1987 ◽  
Vol 252 (2) ◽  
pp. F226-F231 ◽  
Author(s):  
J. J. Walker ◽  
T. S. Yan ◽  
G. A. Quamme
Keyword(s):  
Proximal Tubule ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Phosphate Transport ◽  
Transport Processes ◽  
Proximal Tubules ◽  
High Affinity ◽  
Medullary Tissue ◽  
Sodium Dependent ◽  
Early Proximal Tubule

Renal brush-border membrane phosphate transport was studied in early and late segments of the pig proximal tubule. Vesicles were prepared from early proximal tubules (outer cortical tissue) and late proximal tubules (outer medullary tissue). Sodium-dependent phosphate uptake into brush-border membrane vesicles was determined using voltage clamp at 5-6 s, 21 degrees C. Sodium-dependent D-glucose uptake was determined to verify the cortical and medullary tissue cuts. At pH 8.0 (pHi = pHo), two sodium-dependent phosphate transport systems were evident in the early proximal tubule: a high-affinity system [Km, 0.06 +/- 0.01 mM; maximal transport activity (Vmax), 3.6 +/- 1.1 nmol X mg protein-1 X min-1] and a low-affinity system (Km, 4.11 +/- 0.02 mM; Vmax, 9.7 +/- 0.7 nmol X mg protein-1 X min-1). In the late proximal tubule at pH 8.0, only a single high-affinity transport process (Km, 0.19 +/- 0.7 mM; Vmax, 3.4 +/- 0.5 nmol X mg protein-1 X min-1) was evident. D-Glucose kinetics at pH 7.0 revealed both a high-affinity (Km, 0.55 +/- 0.09 mM) and a low-affinity (Km, 20.09 +/- 1.39 mM) system in the early proximal segment and a single high-affinity (Km, 1.27 +/- 0.36 mM) process in the late segment. These data suggest that two systems, distinct in their affinities and capacities, are involved in both D-glucose and phosphate transport across the brush-border membrane of the early proximal tubule, but that only a single high-affinity system is present in the late segment.

Brefeldin A inhibits phosphate transport in opossum kidney cells

1993 ◽  
Vol 264 (1) ◽  
pp. C40-C47 ◽  
Author(s):  
A. W. Capparelli ◽  
M. C. Heng ◽  
L. Li ◽  
O. D. Jo ◽  
N. Yanagawa
Keyword(s):  
Protein Synthesis ◽  
Golgi Apparatus ◽  
Phosphate Uptake ◽  
Brefeldin A ◽  
Phosphate Transport ◽  
Transport Processes ◽  
Free Medium ◽  
Opossum Kidney ◽  
Ok Cells ◽  
Phosphate Deprivation

Brefeldin A (BFA) is a fungal metabolite that blocks the transport processes between the endoplasmic reticulum and the Golgi apparatus. In the present study, we have tested the effect of BFA on phosphate transport in a kidney epithelial cell line, opossum kidney (OK) cells. Electron microscopy showed that exposure of OK cells to BFA caused a rapid and reversible disorganization of Golgi apparatus. Addition of BFA also caused a time (2-8 h)- and dose (1-10 micrograms/ml)-dependent inhibition of Na(+)-dependent cell phosphate uptake. The inhibition of cell phosphate uptake by BFA was reversible and was associated with a decrease in the maximum velocity of phosphate transport. Both the inhibition and the stimulation of cell phosphate uptake by parathyroid hormone and insulin, respectively, were not affected by BFA. BFA at 1 microgram/ml concentration did not affect protein synthesis as determined by [3H]leucine incorporation but diminished the adaptive increase in cell phosphate uptake in response to 2 or 8 h of incubation in nominally phosphate-free medium. On the other hand, inhibition of protein synthesis by cycloheximide (5 microM) abolished the adaptive increase in cell phosphate uptake in response to 8 but not 2 h of incubation in nominally phosphate-free medium, indicating the existence of an early response to phosphate deprivation, which does not require new protein synthesis but is sensitive to the effect of BFA. In summary, results of these studies show that, in OK cells, BFA inhibits phosphate uptake and curtails the adaptive response to phosphate deprivation.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Cl--stimulated adenosine triphosphatase: existence, location and function

1983 ◽  
Vol 106 (1) ◽  
pp. 143-161
Author(s):  
G. A. Gerencser ◽  
S. H. Lee
Keyword(s):  
Atpase Activity ◽  
Plasma Membranes ◽  
Direct Evidence ◽  
Chloride Transport ◽  
Indirect Evidence ◽  
Transport Processes ◽  
Animal Cells ◽  
Chemical Mechanisms ◽  
Mitochondrial Origin ◽  
And Function

The three universally accepted mechanisms of chloride transport across plasma membranes are: (i) sodium-coupled symport; (ii) anion-coupled antiport; and (iii) coupling to primary ion transport through electrical and/or chemical mechanisms. No direct evidence has been provided for primary chloride transport despite numerous reports of cellular, anion-stimulated ATPases and of chloride transport processes. Anion-stimulated ATPases are of mitochondrial origin and are a ubiquitous property of practically all animal cells. It also appears that there are other subcellular sites of anion-stimulated ATPase activity, especially the plasma membranes. Recent studies have provided indirect evidence (through parallel studies on the same tissue of anion-stimulated ATPase activity and chloride fluxes) which suggests a possible involvement of ATPase in net movement of chloride up its electrochemical gradient across plasma membranes. Further studies are required to substantiate a direct transport function to Cl--stimulated ATPases located in the plasma membrane.

Phosphate transport processes in eukaryotic cells

1989 ◽  
Vol 111 (3) ◽  
pp. 199-213 ◽  
Author(s):  
Janna P. Wehrle ◽  
Peter L. Pedersen
Keyword(s):  
Phosphate Transport ◽  
Transport Processes ◽  
Eukaryotic Cells

Pharmacological uses and perspectives of heavy water and deuterated compounds

1999 ◽  
Vol 77 (2) ◽  
pp. 79-88 ◽  
Author(s):  
D J Kushner ◽  
Alison Baker ◽  
T G Dunstall
Keyword(s):  
Cytochrome P450 ◽  
Heavy Water ◽  
Isotope Effects ◽  
Heat Stability ◽  
Transport Processes ◽  
Resistant Bacteria ◽  
Animal Cells ◽  
Duration Of Action ◽  
Membrane Function ◽  
Deuterium Isotope Effects

Since the discovery of D2O (heavy water) and its use as a moderator in nuclear reactors, its biological effects have been extensively, although seldom deeply, studied. This article reviews these effects on whole animals, animal cells, and microorganisms. Both "solvent isotope effects," those due to the special properties of D2O as a solvent, and "deuterium isotope effects" (DIE), which result when D replaces H in many biological molecules, are considered. The low toxicity of D2O toward mammals is reflected in its widespread use for measuring water spaces in humans and other animals. Higher concentrations (usually >20% of body weight) can be toxic to animals and animal cells. Effects on the nervous system and the liver and on formation of different blood cells have been noted. At the cellular level, D2O may affect mitosis and membrane function. Protozoa are able to withstand up to 70% D2O. Algae and bacteria can adapt to grow in 100% D2O and can serve as sources of a large number of deuterated molecules. D2O increases heat stability of macromolecules but may decrease cellular heat stability, possibly as a result of inhibition of chaperonin formation. High D2O concentrations can reduce salt- and ethanol-induced hypertension in rats and protect mice from gamma irradation. Such concentrations are also used in boron neutron capture therapy to increase neutron penetration to boron compounds bound to malignant cells. D2O is more toxic to malignant than normal animal cells, but at concentrations too high for regular therapeutic use. D2O and deuterated drugs are widely used in studies of metabolism of drugs and toxic substances in humans and other animals. The deuterated forms of drugs often have different actions than the protonated forms. Some deuterated drugs show different transport processes. Most are more resistant to metabolic changes, especially those changes mediated by cytochrome P450 systems. Deuteration may also change the pathway of drug metabolism (metabolic switching). Changed metabolism may lead to increased duration of action and lower toxicity. It may also lead to lower activity, if the drug is normally changed to the active form in vivo. Deuteration can also lower the genotoxicity of the anticancer drug tamoxifen and other compounds. Deuteration increases effectiveness of long-chain fatty acids and fluoro-D-phenylalanine by preventing their breakdown by target microorganisms. A few deuterated antibiotics have been prepared, and their antimicrobial activity was found to be little changed. Their action on resistant bacteria has not been studied, but there is no reason to believe that they would be more effective against such bacteria. Insect resistance to insecticides is very often due to insecticide destruction through the cytochrome P450 system. Deuterated insecticides might well be more effective against resistant insects, but this potentially valuable possibility has not yet been studied.Key words: deuterium, heavy water, D2O, deuterium isotope effects.

Saturn's E, G and F rings: modulated by the plasma sheet

1984 ◽  
Vol 75 ◽  
pp. 597
Author(s):  
E. Grün ◽  
G.E. Morfill ◽  
T.V. Johnson ◽  
G.H. Schwehm
Keyword(s):  
Solar Wind ◽  
Direct Contact ◽  
Transport Processes ◽  
Time Variable ◽  
Dust Particles ◽  
Spatial Diffusion ◽  
Drag Forces ◽  
Orbit Perturbation ◽  
Time Variations ◽  
F Ring

ABSTRACTSaturn's broad E ring, the narrow G ring and the structured and apparently time variable F ring(s), contain many micron and sub-micron sized particles, which make up the “visible” component. These rings (or ring systems) are in direct contact with magnetospheric plasma. Fluctuations in the plasma density and/or mean energy, due to magnetospheric and solar wind processes, may induce stochastic charge variations on the dust particles, which in turn lead to an orbit perturbation and spatial diffusion. It is suggested that the extent of the E ring and the braided, kinky structure of certain portions of the F rings as well as possible time variations are a result of plasma induced electromagnetic perturbations and drag forces. The G ring, in this scenario, requires some form of shepherding and should be akin to the F ring in structure. Sputtering of micron-sized dust particles in the E ring by magnetospheric ions yields lifetimes of 102to 104years. This effect as well as the plasma induced transport processes require an active source for the E ring, probably Enceladus.

Surface Structure of Nucleated Animal Cells: Carbon Replicas

1967 ◽  
Vol 25 ◽  
pp. 120-121
Author(s):  
Robert M. Glaeser ◽  
Thea B. Scott
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Particle Diameter ◽  
Cellular Functions ◽  
Animal Cells ◽  
Replica Technique ◽  
Carbon Replica ◽  
Characteristic Particle ◽  
Cell Surface Structure ◽  
Carbon Replicas

The carbon-replica technique can be used to obtain information about cell-surface structure that cannot ordinarily be obtained by thin-section techniques. Mammalian erythrocytes have been studied by the replica technique and they appear to be characterized by a pebbly or “plaqued“ surface texture. The characteristic “particle” diameter is about 200 Å to 400 Å. We have now extended our observations on cell-surface structure to chicken and frog erythrocytes, which possess a broad range of cellular functions, and to normal rat lymphocytes and mouse ascites tumor cells, which are capable of cell division. In these experiments fresh cells were washed in Eagle's Minimum Essential Medium Salt Solution (for suspension cultures) and one volume of a 10% cell suspension was added to one volume of 2% OsO4 or 5% gluteraldehyde in 0.067 M phosphate buffer, pH 7.3. Carbon replicas were obtained by a technique similar to that employed by Glaeser et al. Figure 1 shows an electron micrograph of a carbon replica made from a chicken erythrocyte, and Figure 2 shows an enlarged portion of the same cell.

Nuclear Envelope Dynamics During Mitosis

1988 ◽  
Vol 46 ◽  
pp. 224-225
Author(s):  
Brian Burke
Keyword(s):  
Nuclear Envelope ◽  
Membrane Vesicles ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Animal Cells ◽  
Interphase Chromosome ◽  
Lamin B ◽  
Chromosome Architecture ◽  
Complex Membrane ◽  
Pore Complexes

The nuclear envelope is a complex membrane structure that forms the boundary of the nuclear compartment in eukaryotes. It regulates the passage of macromolecules between the two compartments and may be important for organizing interphase chromosome architecture. In interphase animal cells it forms a remarkably stable structure consisting of a double membrane ouerlying a protein meshwork or lamina and penetrated by nuclear pore complexes. The latter form the channels for nucleocytoplasmic exchange of macromolecules, At the onset of mitosis, however, it rapidly disassembles, the membranes fragment to yield small vesicles and the lamina, which is composed of predominantly three polypeptides, lamins R, B and C (MW approx. 74, 68 and 65 kDa respectiuely), breaks down. Lamins B and C are dispersed as monomers throughout the mitotic cytoplasm, while lamin B remains associated with the nuclear membrane vesicles.

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