Intracellular distribution of Hg2+ applied to epidermis in mice. Analysis of subcellular fractions

1995 ◽  
Vol 10 (3) ◽  
pp. 233-237 ◽  
Author(s):  
Tsutomu Daian ◽  
Tatsuo Namikoshi ◽  
Hiroyuki Fujii
Keyword(s):  
Intracellular Distribution ◽  
Subcellular Fractions

Intracellular distribution of tritiated bilirubin during hepatic uptake and excretion

1964 ◽  
Vol 207 (6) ◽  
pp. 1237-1241 ◽  
Author(s):  
William R. Brown ◽  
Gerold M. Grodsky ◽  
John V. Carbone
Keyword(s):  
Serum Bilirubin ◽  
Hepatic Uptake ◽  
Hepatic Cell ◽  
Intracellular Distribution ◽  
Constant Function ◽  
Subcellular Fractions ◽  
Acid Hydrolase ◽  
Bilirubin Concentration ◽  
Extrahepatic Tissues

Physiologic amounts of bilirubin-H3 were injected into normal rats and the distribution of isotope was determined in serum, subcellular fractions of the liver, and bile at intervals during the phases of uptake and excretion. Recovery in the three spaces after 2, 5, 15, and 30 min was 75–85%, indicating little bilirubin entered the extrahepatic tissues. At 5 min, 50% of the dose (excluding trapped serum bilirubin-H3) was in the liver, a bilirubin concentration greater than in serum; biliary excretion of bilirubin was less than 3%. By 30–60 min, most of the label was excreted in the bile as intact, diazotizable and crystallizable bilirubin. Bilirubin-H3 appeared principally in the hepatic cell sap at a rate and concentration too high for an albumin-linked transfer. No differences in the distribution of isotope in subcellular fractions were detectable during the phases of uptake or excretion or when the quantity injected was increased 20–40 times. Thus, intracellular distribution was primarily a constant function of intracellular bilirubin concentration. When compared to in vitro experiments, significant amounts of bilirubin accumulated within the microsomes and the acid hydrolase-rich fraction (lysosomes) but not in the mitochondrial or nuclear fractions.

scholarly journals Determination of the intracellular distribution and pool sizes of apolipoprotein B in rabbit liver

1992 ◽  
Vol 288 (2) ◽  
pp. 413-419 ◽  
Author(s):  
J Wilkinson ◽  
J A Higgins ◽  
P H E Groot ◽  
E Gherardi ◽  
D E Bowyer
Keyword(s):  
Endoplasmic Reticulum ◽  
Apolipoprotein B ◽  
Intracellular Distribution ◽  
Subcellular Fractions ◽  
Rabbit Liver ◽  
Very Low Density Lipoproteins ◽  
Apo B ◽  
Golgi Region ◽  
Membrane Bound ◽  
Vldl Assembly

We have investigated the intracellular distribution of apolipoprotein B (apo B) in rabbit liver by immunoblotting, radioimmunoassay (r.i.a.) and enzyme-linked immunoassay (e.l.i.s.a.). Apo B100 was detected in total microsomes, rough microsomes, smooth microsomes, trans-enriched Golgi and cis-enriched Golgi and membrane and cisternal-content subfractions prepared from these fractions. There was also evidence of degradation of apo B100 in the Golgi membrane fractions. The amount of apo B in the subcellular fractions detected by competitive r.i.a. or e.l.i.s.a. ranged from 1.5 micrograms/mg of protein in the rough endoplasmic reticulum to 13 micrograms/mg of protein in the trans-Golgi fraction. Using internal standards (NADPH-cytochrome c reductase for the endoplasmic reticulum and galactosyltransferase for the Golgi membranes) it was calculated that all the apo B of liver is recovered within the secretory compartment, with 63% of the total apo B in the endoplasmic reticulum and the remainder in the Golgi. When the subcellular fractions were separated into membranes and cisternal contents, 60%, 50%, 60% and 30% of the total apo B was recovered in the membrane of the rough microsomes, smooth microsomes, cis-Golgi and trans-Golgi respectively. Using competitive e.l.i.s.a. we found that the membrane-bound form of the apo B was exposed at the cytosolic surface of the intact subcellular fractions. These observations are consistent with a model for assembly of very-low-density lipoproteins (VLDL) in which newly synthesized apo B is incorporated into a membrane-bound pool and a lumenal pool. The membrane-bound pool not used for VLDL assembly may be degraded, possibly in the Golgi region.

Characteristics of Phytochrome in Glutaraldehyde-Treated Maize Coleoptiles

1975 ◽  
Vol 2 (3) ◽  
pp. 281 ◽  
Author(s):  
R Yu
Keyword(s):  
Soluble Fraction ◽  
Red Light ◽  
Intracellular Distribution ◽  
Subcellular Fractions ◽  
Particulate Fraction ◽  
Cell Fractionation

Glutaraldehyde treatment was used to stabilize the in situ distribution of phytochrome at intervals during the course of phytochrome dark reactions. Total cellular phytochrome decreased in maize coleoptiles when they were returned to darkness and incubated after red irradiation. Photoreversibility was lost in both the soluble and particulate fractions, being faster in the particulate fraction. Glutaraldehyde treatment of coleoptiles immediately after irradiation inhibited loss of particulate phytochrome in the dark. When coleoptiles were irradiated with R/FR, i.e, red light (R, 660 nm) followed by far-red light (FR, 737 nm), and then incubated in the dark, the loss of particulate phytochrome was compensated for by an increase of phytochrome in the soluble fraction, resulting in negligible loss of total phytochrome. The phytochrome dark reactions in subcellular fractions of coleoptiles irradiated in vivo with R and R/FR and extracted in Mg2+-containing buffer were similar to those in corresponding subcellular fractions of coleoptiles treated with glutaraldehyde before cell fractionation. If the pattern of phytochrome dark reactions in subcellular fractions of R- and R/FR-irradiated coleoptiles treated with glutaraldehyde before cell fractionation truly reffects the in situ situation, this similarity suggests that the phytochrome distribution in subcellular fractions obtained by extraction in Mg2+-containing buffer of coleoptiles irradiated in vivo (without ghtaraldehyde treatment) also represents the intracellular distribution. This conclusion however cannot be extended to the distribution obtained following irradiation of Mg2+-containing non-cellular extracts.

INTRACELLULAR DISTRIBUTION OF COPPER IN THE LIVER OF THE RAT

1967 ◽  
Vol 45 (12) ◽  
pp. 1841-1851 ◽  
Author(s):  
G. Gregoriadis ◽  
T. L. Sourkes
Keyword(s):  
Copper Content ◽  
Copper Deficiency ◽  
Physiological State ◽  
Intracellular Distribution ◽  
Subcellular Fractions ◽  
Absolute Amount ◽  
Newborn Rat ◽  
Adult Rat ◽  
Total Copper ◽  
Minor Losses

The absolute amount of copper in whole liver and its subcellular fractions decreases as the rat matures. The decrease in mitochondrial and nuclear fractions, which contain most of the copper in the liver of the newborn rat, is much greater than the decrease in the soluble and microsomal fractions. This results in a redistribution of the copper, in favor of the supernatant. In the adult rat, this fraction is about one-half the total copper content of the liver, with the content of nuclei, mitochondria, and microsomes following in that order. The intraperitoneal injection of copper sulfate or the feeding of a diet low in copper brings the copper content of the liver above and below normal levels, respectively, and affects the intracellular distribution as follows. In copper loading, mitochondria and nuclei hold most of the excess and the cytoplasm and microsomes accumulate much less. In copper deficiency, there is a greater loss of soluble and mitochondrial copper and there are minor losses in microsomes and nuclei. The copper concentration in subcellular fractions of the liver seems to be related to the total copper content of the organ rather than to the physiological state of the animal.

The effect of chloroquine on the binding, intracellular distribution, and action of insulin on isolated mouse pancreatic acini

Diabetes ◽  
1983 ◽  
Vol 32 (12) ◽  
pp. 1102-1109
Author(s):  
Y. Iwamoto ◽  
E. Roach ◽  
A. Bailey ◽  
J. A. Williams ◽  
I. D. Goldfine
Keyword(s):  
Intracellular Distribution ◽  
Pancreatic Acini

Biomass Characterization in a Nitrification-Denitrification Biological Enhanced Phosphorus Removal (NDBEPR) Plant during Start-Up and Subsequent Periods of Good and Poor Phosphorus Removal

1994 ◽  
Vol 29 (7) ◽  
pp. 91-100 ◽  
Author(s):  
K. C. Lindrea ◽  
S. P. Pigdon ◽  
B. Boyd ◽  
G. A. Lockwood
Keyword(s):  
Phosphorus Removal ◽  
Poor Performance ◽  
Intracellular Distribution ◽  
Full Scale ◽  
Laboratory Scale ◽  
Plant Operation ◽  
The Poor ◽  
Start Up ◽  
Biomass Characterization

During commissioning and process stabilization of a NDBEPR plant at Bendigo intracellular distribution and movement of phosphorus, K+, Mg2+ and Ca2+ was followed to establish the nature of biomass development. The system was also monitored at the end of a period of breakdown of the BEPR process and during its return to phosphorus removal. Phosphorus (P) and Mg2+ distribution in the biomass were closely related during all phases of plant operation, and laboratory trials indicated that the poor performance of the full-scale plant was associated with seasonal reduction in influent Mg2+. Laboratory scale trials produced a similar effect when the influent Mg2+ was limited to concentrations much lower than those experienced in the full scale plant, but only after the Mg2+ and P reserves in the biomass were depleted. The distribution of P, K+, Mg2+ and Ca2+ in the biomass from the full scale plant was similar to that seen in the laboratory trials when cations in the feed were severely limited and recovery of the full scale plant also closely matched that of the laboratory scale system.

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