scholarly journals Uptake and processing of the precursor for rat liver ornithine transcarbamylase by isolated mitochondria. Inhibition by uncouplers.

1981 ◽  
Vol 256 (16) ◽  
pp. 8263-8266 ◽  
Author(s):  
M. Mori ◽  
T. Morita ◽  
S. Miura ◽  
M. Tatibana
1988 ◽  
Vol 14 (5) ◽  
pp. 477-482 ◽  
Author(s):  
P. Cantatore ◽  
P. Loguercio Polosa ◽  
A. Mustich ◽  
V. Petruzzella ◽  
M. N. Gadaleta

1994 ◽  
Vol 22 (10) ◽  
pp. 1861-1865 ◽  
Author(s):  
José A. Enríquez ◽  
Javier Ramos ◽  
Acisclo Pérez-Martos ◽  
Manuel J. López-Pérez ◽  
Julio Montoya

1960 ◽  
Vol 199 (4) ◽  
pp. 653-656
Author(s):  
Leonard Share

A study was made of the effects of certain agents, which inhibit potassium transport in intact cells, on the potassium, sodium and water metabolism of isolated mitochondria. Protamine (4 mg/100 ml) induced swelling in rat liver and kidney mitochondria and impaired the ability of these mitochondria to concentrate potassium. These actions appeared to be associated with the uncoupling of oxidative phosphorylation. Protamine was without effect on the mitochondrial sodium concentration. Strophanthin at extremely high concentrations (1 gm/100 ml) was also found to induce swelling of rat liver, kidney and heart mitochondria and to interfere with the ability of the mitochondria to concentrate potassium. There was a tendency for mitochondrial sodium concentration to be elevated. It is concluded that the actions of protamine and strophanthin on mitochondria are qualitatively and quantitatively different from the actions of these substances on intact cells and that there are basic differences between the potassium concentrating mechanisms in mitochondria and in intact cells.


Blood ◽  
1976 ◽  
Vol 47 (6) ◽  
pp. 923-930 ◽  
Author(s):  
RA Gams ◽  
EM Ryel ◽  
F Ostroy

Abstract Protein-mediated B12 uptake by isolated rat liver mitochondria has been shown to be enhanced by plasma transcobalamin (TC-II) but not by salivary R binder in vitro. The process is enhanced by calcium and depends on active mitochondrial respiration. Following uptake, cyanocobalamin is converted to adenosyl and methylcobalamins and released from the mitochondria. TC-II appears to be required for both cellular and mitochondrial uptake of vitamin B12.


1990 ◽  
Vol 259 (3) ◽  
pp. G340-G347 ◽  
Author(s):  
J. Milland ◽  
A. Tsykin ◽  
T. Thomas ◽  
A. R. Aldred ◽  
T. Cole ◽  
...  

The integration of growth and the acute-phase response is investigated by comparing the mRNA levels in rat liver during acute inflammation with those after partial hepatectomy. Northern analysis is carried out for the mRNAs for thiostatin, alpha 2-macroglobulin, alpha 1-antitrypsin, inter-alpha-trypsin inhibitor subunit 1, haptoglobin, ceruloplasmin, transferrin, vitamin D-binding protein, alpha 1-acid glycoprotein, beta-fibrinogen, apolipoproteins A-IV and E, albumin, transthyretin, alpha 2-HS-glycoprotein, retinol-binding protein, beta-tubulin, c-myc protooncogene, glyceraldehyde-3-phosphate dehydrogenase, phosphoenolpyruvate carboxykinase, ornithine transcarbamylase, and alcohol dehydrogenase. The acute-phase response dominates during the first 18 h. Changes in mRNA levels related to growth of the liver become important thereafter, and the capacity for an acute-phase response of plasma protein synthesis becomes greatly reduced. The early increase in the level of ceruloplasmin mRNA observed during inflammation is abolished during regeneration, and that of vitamin D-binding protein mRNA is converted into a decrease. The mRNAs levels of glyceraldehyde-3-phosphate dehydrogenase increase, and those for phosphoenolpyruvate carboxykinase decrease during regeneration. Ornithine transcarbamylase mRNA levels are found to exhibit negative acute-phase regulation. The pattern of transcriptional regulation is similar during inflammation and regeneration.


FEBS Letters ◽  
1984 ◽  
Vol 177 (1) ◽  
pp. 41-46 ◽  
Author(s):  
Peter Mclntyre ◽  
Lynda Graf ◽  
Julian Mercer ◽  
Gregory Peterson ◽  
Peter Hudson ◽  
...  

1974 ◽  
Vol 52 (10) ◽  
pp. 936-939 ◽  
Author(s):  
J. B. Davidson ◽  
N. Z. Stanacev

The enzymatic activities of marker enzymes (NADPH – cytochrome c reductase and glucose-6-phosphatase) and synthetic enzymes (acyl-CoA:sn-glycero-3-phosphate acyltransferase, CTP:sn-3-phosphatidic acid cytidyltransferase, and CDP-diglyceride:sn-glycero-3-phosphate phosphatidyltransferase) were measured in both isolated mitochondria and microsomes from liver of guinea pig and rat. Results thus obtained show a significant difference in activities of these enzymes between subcellular particles within species and between two examined species. The activity of acyl-CoA:glycero-3-phosphate acyltransferase in guinea-pig mitochondria parallels the activity of microsomal marker enzymes in this fraction, while in rat liver mitochondria the activity is relatively higher and cannot be accounted for by the microsomal content as determined by marker enzymes. Implications of these results regarding mitochondrial autonomy in the biosynthesis of polyglycero-phosphatides and their precursors are discussed.


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