Gender dimorphism in rat liver mitochondrial oxidative metabolism and biogenesis

2005 ◽  
Vol 289 (2) ◽  
pp. C372-C378 ◽  
Author(s):  
Roberto Justo ◽  
Jordi Boada ◽  
Margalida Frontera ◽  
Jordi Oliver ◽  
Jordi Bermúdez ◽  
...  
Keyword(s):  
Gender Differences ◽  
Protein Content ◽  
Rat Liver ◽  
Oxidative Metabolism ◽  
Mitochondrial Protein ◽  
Electron Microscopic ◽  
Gender Dimorphism ◽  
Protein Levels ◽  
Mitochondrial Fractions ◽  
Mitochondrial Oxidative Metabolism

In the present study, we have investigated gender differences in rat liver mitochondrial oxidative metabolism. Total mitochondrial population (M) as well as the heavy (M1), medium (M3), and light (M8) mitochondrial fractions obtained by means of differential centrifugation steps at 1,000, 3,000, and 8,000 g, respectively, were isolated. Electron microscopic analysis was performed and mitochondrial protein content and cardiolipin levels, mitochondrial O2 flux, ATP synthase activity, mitochondrial membrane potential, and mitochondrial transcription factor A (TFAM) protein levels were measured in each sample. Our results indicate that mitochondria from females have higher protein content and higher cardiolipin levels, greater respiratory and phosphorylative capacities, and more-energized mitochondria in respiratory state 3. Moreover, protein levels of TFAM were four times greater in females than in males. Gender differences in the aforementioned parameters were more patent in the isolated heavy M1 and M3 mitochondrial fractions. The present study demonstrates that gender-related differences in liver mitochondrial function are due mainly to a higher capacity and efficiency of substrate oxidation, likely related to greater mitochondrial machinery in females than in males, which is in accord with greater mitochondrial differentiation in females.

Effect of thyroid state and cold exposure on rat liver mitochondrial protein mass and function

1991 ◽  
Vol 131 (1) ◽  
pp. 67-73 ◽  
Author(s):  
S. Iossa ◽  
G. Liverini ◽  
A. Barletta
Keyword(s):  
Oxidative Phosphorylation ◽  
Rat Liver ◽  
Cold Exposure ◽  
Oxidative Metabolism ◽  
Mitochondrial Protein ◽  
The Other ◽  
Thyroid State ◽  
Protein Mass ◽  
Palmitoyl Carnitine ◽  
And Function

ABSTRACT The effects of thyroid state on liver mitochondrial protein mass was investigated in rats at 24 and 4 °C, as was oxidative phosphorylation using substrates which represent the final catabolic products of the metabolic fuels. In rats at 24 °C, a significant increase in mitochondrial protein mass (about +40%) was observed only in hyperthyroid animals, while a significant increase due to cold exposure was found in hypothyroid (+ 45%) and euthyroid (+ 35%) rats. In rats at 24 °C, hypothyroidism significantly decreased the oxidation of glutamate and palmitoyl carnitine but not of pyruvate, while hyperthyroidism only increased the oxidation of palmitoyl carnitine. On the other hand, exposure to cold significantly increased the oxidation of glutamate and pyruvate only in the presence of tri-iodothyronine. Our results underline not only the fact that a simple and single hypothesis for thyroid effects cannot be adopted, but also that any study concerning oxidative metabolism should be carried out using different substrates and involving different pathways of oxidation. Journal of Endocrinology (1991) 131, 67–73

Nonshivering thermogenesis in king penguin chicks. II. Effect of fasting

1991 ◽  
Vol 261 (6) ◽  
pp. R1446-R1454 ◽  
Author(s):  
C. Duchamp ◽  
H. Barre ◽  
J. L. Rouanet ◽  
A. Lanni ◽  
F. Cohen-Adad ◽  
...  
Keyword(s):  
Protein Content ◽  
Mitochondrial Protein ◽  
Respiratory Control ◽  
King Penguin ◽  
Nonshivering Thermogenesis ◽  
Protein Loss ◽  
Electron Microscopic ◽  
Muscle Mitochondria ◽  
Fat Deposits ◽  
Brown Adipose

The effect of fasting on the energy metabolism of skeletal muscle and liver was investigated in cold-acclimatized short-term fasting (STF) (3 wk) and naturally long-term fasting (LTF) (4-5 mo) king penguin chicks, both groups exhibiting nonshivering thermogenesis (NST). A comparison was made with nourished cold-acclimatized controls. In these chicks, no brown adipose tissue deposits could be found on electron-microscopic observations of fat deposits. Protein content and cytochrome oxidase (CO) activity of tissue homogenates were measured in liver and pectoralis and gastrocnemius muscles, as were protein content, CO activity, and respiration rates of mitochondria isolated from these organs. Fasting-induced protein loss affected the pectoralis more than the gastrocnemius muscle, thus preserving locomotor function. In STF chicks, specific mitochondrial protein content and specific tissue CO activity were preserved but total organ CO capacity was reduced by half in pectoralis and liver following the fall in organ mass. In LTF chicks, both specific and total CO activity were drastically reduced in muscles, whereas specific CO activity was preserved in liver. In these LTF chicks, muscle mitochondria showed an energized configuration associated with an increased area of inner membrane in gastrocnemius. A reduction of respiratory control ratio (RCR) was observed in subsarcolemmal muscle mitochondria of STF chicks, whereas intermyofibrillar and liver mitochondria kept high RCR values.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Mitochondrial Alterations (Inhibition of Mitochondrial Protein Expression, Oxidative Metabolism, and Ultrastructure) Induced by Linezolid and Tedizolid at Clinically Relevant Concentrations in Cultured Human HL-60 Promyelocytes and THP-1 Monocytes

2017 ◽  
Vol 62 (3) ◽  
Author(s):  
Tamara V. Milosevic ◽  
Valéry L. Payen ◽  
Pierre Sonveaux ◽  
Giulio G. Muccioli ◽  
Paul M. Tulkens ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Oxidative Metabolism ◽  
Oxidase Activity ◽  
Potent Inhibitor ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Synthesis ◽  
Once Daily ◽  
Content Type ◽  
Mitochondrial Alterations ◽  
Mitochondrial Oxidative Metabolism

ABSTRACTLinezolid, the first clinically available oxazolidinone antibiotic, causes potentially severe toxicities (myelosuppression, lactic acidosis, and neuropathies) ascribed to impairment of mitochondrial protein synthesis and consecutive mitochondrial dysfunction. Tedizolid, a newly approved oxazolidinone, shows an enhanced activity compared to linezolid but is also a more potent inhibitor of mitochondrial protein synthesis. We compared linezolid and tedizolid for (i) inhibition of the expression of subunit I of cytochromec-oxidase (CYTox I; Western blot analysis), (ii) cytochromec-oxidase activity (biochemical assay), (iii) mitochondrial oxidative metabolism (Seahorse technology), and (iv) alteration of mitochondrial ultrastructure (electron microscopy) using HL-60 promyelocytes and THP-1 monocytes exposed to microbiologically (multiples of modal MIC againstStaphylococcus aureus) and therapeutically (Cmin−Cmax) pertinent concentrations. Both drugs caused a rapid and complete (48 to 72 h) inhibition of CYTox I expression, cytochromec-oxidase activity, and spare respiratory capacity, with conspicuous swelling of the mitochondrial matrix and loss of their cristae. Globally, tedizolid was a more potent inhibitor than linezolid. For both drugs, all effects were quickly (48 to 72 h) and fully reversible upon drug withdrawal. Using an alternation of exposure to and withdrawal from drug mimicking their approved schedule of administration (twice daily and once daily [qD] for linezolid and tedizolid, respectively), only partial inhibition of CYTox I expression was noted for up to 96 h. Thus, rapid reversal of toxic effects upon discontinuous administration may mitigate oxazolidinone toxicity. Since tedizolid is given qD, this may help to explain its reported lower preclinical and clinical toxicity.

Glucocorticoid effects on respiration and metabolism by rat liver homogenates

1962 ◽  
Vol 202 (2) ◽  
pp. 343-346 ◽  
Author(s):  
Dennis D. Goetsch ◽  
L. E. McDonald
Keyword(s):  
Lactic Acid ◽  
Oxygen Uptake ◽  
Rat Liver ◽  
Inorganic Phosphate ◽  
Chronic Administration ◽  
Glucocorticoid Treatment ◽  
Carbohydrate Utilization ◽  
Protein Levels ◽  
Liver Homogenates ◽  
And Control

The effects of glucocorticoid administration on oxygen uptake, glucose and glycogen disappearance, lactic acid formation, and inorganic phosphate and protein levels in rat liver homogenates have been studied. A single injection of hydrocortisone, prednisolone, or 9 α-fluoroprednisolone 5 hr before sacrifice resulted in a highly significant increase in oxygen uptake by rat liver homogenates, whereas chronic administration of prednisolone daily for 7 days caused a marked inhibition in homogenate respiration. Glycolytic rate did not appear to be affected by single injections since endogenous carbohydrate utilization was similar in liver homogenates prepared from control and treated animals. Incubation of liver homogenates under aerobic conditions disclosed that inorganic phosphate levels were decreased in homogenates from corticoid-treated rats, whereas these levels were similar in treated and control liver homogenates incubated under nitrogen. Under anaerobic conditions, liver homogenates from treated rats accumulated lactic acid more rapidly than untreated liver homogenates. Glucocorticoid treatment did not appear to affect protein disappearance since no differences between protein levels in treated and untreated rat liver homogenates were detected following incubation.

scholarly journals Induction of carnitine acetyltransferase by clofibrate in rat liver

1981 ◽  
Vol 194 (1) ◽  
pp. 249-255 ◽  
Author(s):  
B Mittal ◽  
C K R Kurup
Keyword(s):  
Protein Synthesis ◽  
Enzyme Activity ◽  
Rat Liver ◽  
Time Lag ◽  
Mitochondrial Protein ◽  
Carnitine Acetyltransferase ◽  
Enzyme Protein ◽  
General Protein Synthesis ◽  
Liver And Kidney ◽  
General Protein

Administration of the anti-hypercholesterolaemic drug clofibrate to the rat increases the activity of carnitine acetyltransferase (acetyl-CoA-carnitine O-acetyltransferase, EC 2.3.1.7) in liver and kidney. The drug-mediated increase in enzyme activity in hepatic mitochondria shows a time lag during which the activity increases in the microsomal and peroxisomal fractions. The enzyme induced in the particulate fractions is identical with one normally present in mitochondria. The increase in enzyme activity is prevented by inhibitors of RNA and general protein synthesis. Mitochondrial protein-synthetic machinery does not appear to be involved in the process. Immunoprecipitation shows increased concentration of the enzyme protein in hepatic mitochondria isolated from drug-treated animals. In these animals, the rate of synthesis of the enzyme is increased 7-fold.

Effects of variations in dietary protein levels on hair growth and pelt quality in mink (Mustela vison)

2000 ◽  
Vol 80 (4) ◽  
pp. 633-642 ◽  
Author(s):  
Palle V. Rasmussen ◽  
Christian F. Børsting
Keyword(s):  
Protein Content ◽  
Dietary Protein ◽  
Protein Level ◽  
Hair Growth ◽  
Fibre Length ◽  
Hair Follicles ◽  
Protein Levels ◽  
Low Protein ◽  
Pregnancy And Lactation ◽  
Hair Fibre

The effect of different and shifting dietary protein levels on hair growth and the resulting pelt quality in mink was studied. Two groups of pastel female mink were fed either 59% (high protein, HP) or 40% (low protein, LP) of metabolisable energy (ME) from protein during pregnancy and lactation. Shortly after weaning, kits from females fed the LP diet were put on a new LP diet (21% protein of ME). Kits from females fed HP were randomly distributed to four experimental groups fed a new HP diet (34% protein of ME) and three of these groups were shifted to diets with 21% protein at different times during June until September. Skin biopsies were taken at 4, 6, 23 and, 29 wk of age. Histological techniques and computer-assisted light microscopy were used to determine the ratio of activity (ROA) of underfur and guard hairs, respectively, defined as the number of growing hairs as a percentage of the total number of hairs. The hair fibre length and thickness were determined by morphometric methods and correlated with fur properties of dried pelts judged by sensory methods. It was documented that 40% of ME from protein during pregnancy and lactation was sufficient for mink kits to express their genetic capacity to produce hair follicles. In males, a reduced protein level from the age of 15 wk or 22 wk until pelting disturbed moulting, indicated by a low ROA of underfur hairs at 23 wk, and consequently reduced the growth and development of the winter coat. A constantly low protein level from conception until the age of 29 wk did not disturb moulting, but led to a reduction of primeness and especially of the underfur length and fibre thickness of the winter coat. A low protein level from the age of 9 wk only reduced the thickness of the underfur fibres. Hair growth, final fur volume, and general quality of the winter coat of males were influenced negatively and to the same degree in all groups fed the LP diet in part of the growth period. The number of underfur hairs per area (hair density) of the winter coat was not influenced by the dietary treatment meaning that the protein content of 21% of ME in the LP diet was high enough for the mink to express its genetic capacity to develop hair follicles. However, this low protein content led to a reduction of hair fibre length and hair fibre thickness of the underfur. Overall, this study demonstrated that hair growth and hair properties in pelts are very dependent on the dietary protein supply in the period from 22 wk of age until pelting, irrespective of the supply in the preceding periods. Key words: Fur properties, hair fibres, nutrition, pelage, protein requirement

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