scholarly journals Metal transport in cells: cadmium uptake by rat hepatocytes and renal cortical epithelial cells.

1995 ◽  
Vol 103 (suppl 1) ◽  
pp. 73-75 ◽  
Author(s):  
Z A Shaikh ◽  
M E Blazka ◽  
T Endo
Keyword(s):  
Epithelial Cells ◽  
Rat Hepatocytes ◽  
Metal Transport ◽  
Cadmium Uptake ◽  
In Cells

Oxidation of glucose carbon entering the TCA cycle is reduced by glutamine in small intestine epithelial cells

1995 ◽  
Vol 268 (6) ◽  
pp. G879-G888 ◽  
Author(s):  
C. E. Kight ◽  
S. E. Fleming
Keyword(s):  
Small Intestine ◽  
Epithelial Cells ◽  
Glucose Oxidation ◽  
Tca Cycle ◽  
Proximal Segment ◽  
Distal Small Intestine ◽  
Glucose Carbon ◽  
The Tca Cycle ◽  
Oxidation Of Glucose ◽  
In Cells

The influence of glutamine on glucose oxidation was assessed in epithelial cells isolated from the mucosa of the proximal, mid-, and distal small intestine of young, fed, male rats. Glucose oxidation declined along the length of the small intestine, with values from the mid- and distal segments representing approximately 55% and 40%, respectively, of the value from the proximal segment. A gradient along the small intestine was noted also in the influence of glutamine on glucose oxidation: glutamine suppressed glucose oxidation approximately 60% in the proximal small intestine, 39% in the mid-intestine, and 31% in the distal small intestine. Glutamine suppressed the oxidation of glucose carbon that entered the tricarboxylic acid (TCA) cycle; this was determined using CO2 ratios derived from acetate and glucose isotopes. In cells from the proximal segment, the probability that carbon entering the cycle would complete one full turn was reduced by glutamine from 0.77 to 0.28. The entry of glucose-derived pyruvate into the TCA cycle did not appear to be influenced by the presence of glutamine, however. Glutamine had no influence on the proportion of glucose metabolism that occurred via the pentose phosphate pathway (which averaged 5% or less), but reduced flux of carbon through pyruvate carboxylase relative to flux through pyruvate dehydrogenase from 40% to 9% in cells from the proximal segment. These data suggest that, in the presence of glutamine, the fate of pyruvate carbon (derived from glucose or elsewhere) entering the TCA cycle is altered from that of oxidation to anaplerosis and subsequent efflux of TCA cycle intermediates into newly synthesized compounds.

Glucose and glutamine provide similar proportions of energy to mucosal cells of rat small intestine

1997 ◽  
Vol 273 (4) ◽  
pp. G968-G978 ◽  
Author(s):  
Sharon E. Fleming ◽  
Kirsten L. Zambell ◽  
Mark D. Fitch
Keyword(s):  
Small Intestine ◽  
Epithelial Cells ◽  
Metabolic Pathways ◽  
Glycolytic Flux ◽  
Net Energy ◽  
Intestinal Epithelial ◽  
Atp Production ◽  
Distal Small Intestine ◽  
Mucosal Cells ◽  
In Cells

The objectives of this study were to establish a reliable method for quantifying glycolytic flux in intestinal epithelial cells, to determine the proportion of energy provided to small intestine epithelial cells by glucose vs. glutamine, and to determine whether there was an energetic advantage to having both substrates present simultaneously. There was substantial retention of 3H in alanine and lactate when [2-3H]glucose was used as tracer for quantifying glycolysis, and the magnitude of the3H retention was influenced by the presence of other substrates and metabolites. Detritiation was at least 99% complete, however, when [3-3H]glucose was used as tracer in this system and the tritium was recovered as3H2O. Glycolytic flux was six- to sevenfold higher in cells of the proximal than distal small intestine but was not significantly different for young adult (4 mo) vs. aged adult (24 mo) rats. Net ATP production from exogenous substrates was higher when both glucose and glutamine were present simultaneously than when either substrate was present alone, and glucose was calculated to provide 50–60% of the net ATP produced from these two substrates. Most of the energy produced from glucose was produced via the anaerobic metabolic pathways (78% for glucose alone, 95% with glucose and glutamine). Net energy production was calculated to be 10% lower in cells from aged animals than in those from young animals, since CO2 production from these major substrates was lower in cells from aged animals.

Melanogenesis in amphibians

Development ◽  
1970 ◽  
Vol 24 (2) ◽  
pp. 447-454
Author(s):  
John J. Eppig
Keyword(s):  
Electron Microscopy ◽  
Epithelial Cells ◽  
Notophthalmus Viridescens ◽  
Retinal Pigmented Epithelium ◽  
Pigmented Epithelium ◽  
In Cells

Electron microscopy of 11-day-old Notophthalmus viridescens retinal pigmented epithelium reveals particulate premelanosomes which are identical to the melanosomes found in the oocyte. These organelles, when found in the pigmented epithelium, are called premelanosomes because they undergo further maturation to form relatively homogeneous, spherical melanosomes. At this stage, oocyte melanosomes found in cells other than melanocytes have not undergone this subsequent maturation. Elongated melanosomes which develop from fibrillar premelanosomes are also found in the pigmented epithelial cells. Treatment with phenylthiourea blocks the maturation of both the fibrillar and particulate premelanosomes.

Aldosterone-stimulated transmethylations are linked to sodium transport

1985 ◽  
Vol 248 (1) ◽  
pp. F43-F47 ◽  
Author(s):  
W. P. Wiesmann ◽  
J. P. Johnson ◽  
G. A. Miura ◽  
P. K. Chaing
Keyword(s):  
Epithelial Cells ◽  
Sodium Transport ◽  
Short Circuit ◽  
Short Circuit Current ◽  
Toad Bladder ◽  
Methylation Inhibitor ◽  
In Cells

The effect of aldosterone (Aldo) on phospholipid (PL) biosynthesis in cultured toad bladder epithelial cells was studied in cells incubated with [1,2-14C]choline and [methyl-3H]methionine over a 5-h period. Aldo (10(-7) M) did not alter the uptake of either precursor but significantly stimulated the incorporation of both labels into phosphatidylcholine (PC), the only PL labeled. 3H labeling of PC increased 29% and 14C incorporation into PC increased 34% in cells exposed to Aldo. A similar 30% increase in protein carboxymethylation occurred in cells treated with Aldo. 3-Deazaadenosine (DZA), a methylation inhibitor, abolished the Aldo-stimulated increase in PC labeling from [3H]methionine. PC labeling from [1,2-14C]choline was not affected by DZA. Basal and Aldo-stimulated protein carboxy-methylation were inhibited by DZA. DZA (300 microM) caused a mild decrease in basal short-circuit current (ISC) but completely inhibited the ISC response to 10(-7) M Aldo. Inhibition was complete when DZA was added up to 2 h following exposure to Aldo, and was reversible. Cells previously exposed to Aldo showed a significant increase in ISC within 2 h following removal of DZA. We conclude that Aldo stimulates PL methylation, protein carboxymethylation, and turnover of PC from choline. Inhibition of methylation reactions coincides with the inhibition of ISC response to Aldo.

Kinetics of a novel cytosolic protein during the onset of renal epithelial cell growth

1988 ◽  
Vol 255 (5) ◽  
pp. F868-F873 ◽  
Author(s):  
H. N. Aithal ◽  
M. M. Walsh-Reitz ◽  
S. Kartha ◽  
S. L. Gluck ◽  
W. A. Franklin ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
High Performance ◽  
Rabbit Antiserum ◽  
Size Exclusion ◽  
Immunocytochemical Staining ◽  
Enzyme Linked Immunosorbent Assay ◽  
Renal Epithelial Cell ◽  
Control Value ◽  
Low K ◽  
In Cells

Exposure of monkey kidney epithelial cells (BSC-1 line) to medium with a reduced K concentration (3.2 mM) stimulated growth and transiently activated glyceraldehyde-3-phosphate dehydrogenase (G3PD). The increase in enzyme activity was mediated by a cytosolic modifier protein that was purified using affinity and size-exclusion chromatography, and anion-exchange high-performance liquid chromatography. The apparent molecular mass of the protein was 62 kDa. A monospecific antibody to the protein was prepared from rabbit antiserum and used as an immunoprobe. Immunocytochemical staining and Western blotting revealed that the protein was a normal constituent of the cytosol and that it accumulated in cells exposed to low-K medium. A quantitative enzyme-linked immunosorbent assay showed that the amount of modifier protein increased progressively for up to 2 h in cells exposed to low-K medium, and then returned to the control value, a kinetic profile similar to that observed for G3PD activity. These results indicate that the modifier protein is a constituent of renal epithelial cells and accumulates transiently in the cytosol where it could regulate G3PD activity during the onset of growth induced by the low-K mitogenic signal.

High affinity L-aspartate transport in chick small intestine

1987 ◽  
Vol 252 (1) ◽  
pp. C105-C114 ◽  
Author(s):  
T. G. Wingrove ◽  
G. A. Kimmich
Keyword(s):  
Small Intestine ◽  
Membrane Potential ◽  
Epithelial Cells ◽  
Intracellular Ph ◽  
Transport Function ◽  
Flux Enhancement ◽  
High Affinity ◽  
Absolute Requirement ◽  
Potential Sensitivity ◽  
In Cells

Epithelial cells isolated from chick small intestine were used to study the mechanism of L-aspartate transport. Two kinetically distinct uptake systems of high (Km' = 16 microM) and low (Km'' = 2.7 mM) affinity are observed. This paper examines the cation dependence and membrane potential sensitivity of the high affinity system. Unidirectional influx studies indicate that extracellular Na+ is an absolute requirement for transport function. Flux is optimal when K+ is present intracellularly, however this cation is not required for Na+-dependent L-aspartate uptake. In the absence of K+, flux enhancement is observed when the intracellular pH is acidic. In contrast, acidic intracellular pH is inhibitory in cells that are preequilibrated with K+. Sodium ([Na+]o greater than [Na+]i gradients, and potassium ([K+]o less than [K+]i) or proton ([H+]o less than [H+]i) gradients can independently energize the Na+-dependent accumulation of L-aspartate above equilibrium levels, suggesting that Na+ and L-aspartate cotransport occurs with concomitant K+ or H+ antiport. L-Aspartate influx is insensitive to membrane potential changes created by inwardly directed anion gradients in the presence or absence of intracellular K+. A model is presented that is consistent with electroneutral Na+-coupled transfer with an ion antiport site of low specificity.

Specific effect of oestrone sulphate on protein synthesis and secretion by cultured epithelial cells from guinea-pig endometrium

1989 ◽  
Vol 123 (2) ◽  
pp. 233-NP ◽  
Author(s):  
G. Chaminadas ◽  
M. Alkhalaf ◽  
J. P. Rémy-Martin ◽  
A. Y. Propper ◽  
G. L. Adessi
Keyword(s):  
Protein Synthesis ◽  
Epithelial Cells ◽  
Progesterone Receptor ◽  
Guinea Pig ◽  
Cultured Cells ◽  
Polyacrylamide Gel Electrophoresis ◽  
Specific Effect ◽  
Cellular Proteins ◽  
Oestrone Sulphate ◽  
In Cells

ABSTRACT Patterns of induced protein synthesis and secretion in guinea-pig endometrial epithelial cell cultures in response to oestrone sulphate alone and oestrone sulphate plus progesterone were investigated. Epithelial cells were cultured for 3 days in growth medium, then washed three times in a steroid-free medium. For each experiment, anticytokeratin immunostaining was used to discriminate the epithelial cells from the stromal cells. Only experiments in which the control dishes displayed more than 80% of anticytokeratinimmunostained cells were further processed. After this period oestradiol-17β (20 nmol/l; control), oestradiol-17β (20 nmol/l) plus progesterone (0·5 μmol/l), oestrone sulphate (1 μmol/l) or oestrone sulphate (1 μmol/l) plus progesterone (0·5 μmol/l) were added to the medium for 48 h. An immunocytochemical progesterone receptor assay showed that oestradiol-17β increased the progesterone receptor content of cells, and progesterone added to cultured cells in the presence of oestradiol-17β induced a significant increase in oestrogen sulphotransferase activity assessing the hormone responsiveness of the cultured cells. In these culture conditions and after 16 h of incubation, oestradiol-17β induced a 1·7-fold increase in [3H]thymidine incorporation into DNA, and [35S]methionine incorporation into cellular proteins was linearly increased up to 8 h. Biochemical changes induced by the different hormone treatments were studied by labelling the proteins with a 6-h pulse of [35S]methionine. The proteins present in the medium and in cells were analysed by two-dimensional polyacrylamide gel electrophoresis, followed by fluorography. Addition of oestrone sulphate alone or with progesterone produced a change in the patterns of cellular and secreted proteins compared with those in cells cultured with either oestradiol-17β or oestradiol-17β plus progesterone. Three cellular proteins (Mr < 14 000, isoelectric point (pI) 5·2 and 5·3; Mr 75 000, pI 4·9) and one secreted protein (Mr 155 000, pI 5·6–5·9) were specifically induced and could serve as markers of oestrone sulphate action. Journal of Endocrinology (1989) 123, 233–241

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