Functional and structural changes in liver mitochondria of rats due to CCl4 intoxication—I

1971 ◽  
Vol 20 (7) ◽  
pp. 1437-1441 ◽  
Author(s):  
V.V. Lyachovich ◽  
V.M. Mishin ◽  
A.V. Dolgov ◽  
I.B. Tsyrlov
Keyword(s):  
Structural Changes ◽  
Liver Mitochondria ◽  
Ccl4 Intoxication

Functional and structural changes in liver mitochondria of rats due to CCl4 intoxication—II

1971 ◽  
Vol 20 (7) ◽  
pp. 1443-1451 ◽  
Author(s):  
V.V. Lyachovich ◽  
V.M. Mishin ◽  
A.V. Dolgov ◽  
G.S. Jakobson ◽  
A.V. Panov ◽  
...  
Keyword(s):  
Structural Changes ◽  
Liver Mitochondria ◽  
Ccl4 Intoxication

scholarly journals STRUCTURAL CHANGES IN ISOLATED LIVER MITOCHONDRIA OF RATS DURING ESSENTIAL FATTY ACID DEFICIENCY

1964 ◽  
Vol 21 (1) ◽  
pp. 15-26 ◽  
Author(s):  
Janet A. Smith ◽  
Hector F. DeLuca
Keyword(s):  
Atpase Activity ◽  
Structural Damage ◽  
Structural Changes ◽  
Essential Fatty Acids ◽  
Saturated Fat ◽  
Respiratory Control ◽  
Liver Mitochondria ◽  
Structural Defects ◽  
Thin Sections ◽  
Fatty Acid Deficiency

Liver mitochondria isolated in 0.44 M sucrose from rats deficient in essential fatty acids (EFA) oxidized citrate, succinate, α-ketoglutarate, glutamate, and pyruvate at a faster rate than did mitochondria isolated from normal rats; however, the oxidation of malate, caprylate, and ß-hydroxybutyrate was not significantly increased. The mitochondria from deficient rats exhibited an increased ATPase activity and extensive structural damage as revealed by electron microscope examination of thin sections. An increase in citrate oxidation and ATPase activity, together with some structural damage, could be demonstrated as early as the 4th week in rats on a fat-free diet. Saturated fat in the diet did not prevent the change in mitochondrial structure but accelerated its appearance. Both the biochemical and structural defects could be reversed within three weeks after feeding deficient rats a source of EFA. In the presence of a phosphate acceptor the effect of EFA deficiency on substrate oxidation was largely eliminated. A trend toward a reduced efficiency of oxidative phosphorylation was noted in mitochondria from EFA-deficient rats, but significant uncoupling was found only in the case of citrate, ß-hydroxybutyrate, and glutamate in the presence of malonate. Together with the increased ATPase activity, the uncoupling of phosphorylation could account for the poor respiratory control found with the deficient preparation. However, EFA deficiency was without effect on the respiration of liver slices, which supports the belief that the observed changes in oxidation and phosphorylation are an artifact resulting from damage sustained by the deficient mitochondria during their isolation.

STRUCTURAL CHANGES ASSOCIATED WITH THE RELEASE OF ENZYMES FROM RAT-LIVER MITOCHONDRIA BY FREEZING

1966 ◽  
Vol 44 (6) ◽  
pp. 775-781 ◽  
Author(s):  
C. V. Lusena ◽  
C. M. S. Dass
Keyword(s):  
Rat Liver ◽  
Structural Modification ◽  
Structural Changes ◽  
Sodium Deoxycholate ◽  
Liver Mitochondria ◽  
Maximum Activity ◽  
Supernatant Fraction ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Disruption ◽  
Partial Release

Suspensions of rat-liver mitochondria in 0.44 M sucrose, after they were frozen and thawed under defined conditions, were partitioned into three sedimentable and one supernatant fraction by differential centrifugation. These were analyzed for optical density, protein content, and for activities of glutamate dehydrogenase (GD) and 3-hydroxybutyrate dehydrogenase (BD) with exogenous nicotinamide–adenine dinucleotide (NAD) both as maximum activity after sodium deoxycholate treatment and as activity released by freezing. Pellets of the three sedimentable fractions were also examined in the electron microscope. When dehydrogenases were not released by a freezing treatment, no structural changes were detected. Release of BD, which was accompanied by release of GD as well, was associated with mitochondrial disruption and drastic rearrangement of mitochondrial membranes. On the other hand, release of GD without BD occurred from swollen and emptied mitochondria. The partial release of enzymes in a preparation was not associated with a partial structural modification of all of the mitochondria, but rather with drastic structural changes in only some of them.

The Effect of Insulin on Mitochondrial Particles

1967 ◽  
Vol 25 ◽  
pp. 160-161 ◽  
Author(s):  
Burton B. Silver ◽  
James C. Hall
Keyword(s):  
Bovine Serum Albumin ◽  
Structural Changes ◽  
Normal Values ◽  
Liver Mitochondria ◽  
Synergistic Action ◽  
Diabetic Rat ◽  
Rat Liver Mitochondria ◽  
Structural Studies

Correlative biochemical and structural studies have shown that insulin and Mg++ may act to alter the configuration and also enhance the efficiency of coupled phosphorylation in sonicated fragments of diabetic rat liver mitochondria. The diabetic preparations had consistently lowered P:O ratios which returned to normal values with addition of insulin in vivo or in vitro. Optimum coupling and structural changes with insulin required a Mg++ concentration of 5 × 10−5 M. Insulin remained effective diluted to a concentration of 2 × 10−4 I.U. per ml. Glutathione, bovine serum albumin, and Zn++ were ineffective in producing either coupling or structural changes. There seems to be a synergistic action of insulin and Mg++ in restoring P:O ratios in diabetic particles while simultaneously altering the structure toward normal control appearances. Fragments negatively stained with phosphotungstate indicated that the normal particles had well defined cristae with numerous evenly distributed, stalked subunits, 90 Å in diameter.

scholarly journals Structural changes in mitochondria induced by uncoupling reagents. The response to proteolytic enzymes

1968 ◽  
Vol 106 (3) ◽  
pp. 711-717 ◽  
Author(s):  
Eugene C. Weinbach ◽  
Joel Garbus
Keyword(s):  
Structural Changes ◽  
Proteolytic Enzymes ◽  
Free Acid ◽  
Liver Mitochondria ◽  
Mitochondrial Proteins ◽  
Rat Liver Mitochondria ◽  
Phospholipid Complex ◽  
Structural Alterations ◽  
Uncoupling Of Oxidative Phosphorylation ◽  
Contrast Interaction

Interaction of uncoupling reagents with bovine serum albumin markedly inhibited its hydrolysis by proteolytic enzymes. The inhibition presumably is due to conformational transitions in the protein substrate induced by the binding of the ligand–uncoupling reagents. The proteolysis of casein, a protein that does not bind these reagents, was not affected, indicating that the proteinases themselves were not inactivated. In contrast, interaction of uncoupling reagents with freshly isolated rat liver mitochondria enhanced their susceptibility to proteolytic enzymes. This was shown by an increase in the release of ninhydrin-reacting material, by an increase in free acid groups and by a decrease in the turbidity of the mitochondrial suspensions. These effects, although opposite in direction to those obtained with albumin, are also presumed to indicate structural changes in the mitochondrial proteins and a disorganization of the protein–phospholipid complex. It is suggested that such structural alterations are expressed functionally as the uncoupling of oxidative phosphorylation.

Oral Contraceptives: Long-Term Use Produces Fine Structural Changes in Liver Mitochondria

Science ◽  
1969 ◽  
Vol 165 (3895) ◽  
pp. 805-807 ◽  
Author(s):  
V. Perez ◽  
S. Gorosdisch ◽  
J. de Martire ◽  
R. Nicholson ◽  
G. di Paola
Keyword(s):  
Oral Contraceptives ◽  
Structural Changes ◽  
Liver Mitochondria

scholarly journals Morphological changes of mitochondria and mammalian cells, induced by hypochlorous acid

2019 ◽  
Vol 64 (2) ◽  
pp. 156-168
Author(s):  
I. B. Zavodnik ◽  
R. I. Kravchuk ◽  
T. V. Ilyich ◽  
E. A. Lapshina ◽  
A. G. Vejko ◽  
...  
Keyword(s):  
Rat Liver ◽  
Mammalian Cells ◽  
Structural Changes ◽  
Hypochlorous Acid ◽  
Morphological Changes ◽  
Liver Mitochondria ◽  
Hill Coefficient ◽  
Rat Liver Mitochondria ◽  
Apparent Dissociation Constant ◽  
Functional Changes

Hypochlorous acid, HOCl, is one of the most powerful biological oxidants and the most important mediator of inflammatory damage of cells and tissues. The purpose of this study was to characterize the morphological features of HOCl – induced oxidative impairment in rat liver mitochondria in vitro and to compare the processes of HOCl-induced oxidation in mitochondria, erythrocytes and B14 cells.HOCl addition (300 μM) to mitochondrial suspension resulted in mitochondrial structural changes with a decrease in the mean total length of the crista and the average number of cristae in one mitochondria with no change in the length of one crista. There was shown a slight decrease in the average cross-sectional area of one mitochondria, mitochondrial profile elongation, an increase in the number of altered mitochondria and the heterogeneity of the population. Simultaneously we observed depolarization of the mitochondrial membrane, the rate and degree of which were determined by the concentration of HOCl. HOCl addition (25–150 μМ) induced lysis of erythrocytes for 60–180 s, which was preceded by a change in the shape and size of cells. The apparent dissociation constant for the HOCl – membrane complex was estimated to be Kd = 140 ± 25 μМ, and the Hill coefficient was to be 2.1. The B14 cell exposure to HOCl (100 μМ) led to a loss of ability to sorb on the substrate, to form associates, and to subsequent shrinkage of cells.Therefore, HOCl caused some morphological (and functional) changes in rat liver mitochondria, which may serve as one of the causes of cell death in inflammatory foci. At the level of the whole cells, the HOCl addition induced lysis of red blood cells and deep damage to B14 cells.

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