Reduced cytochrome oxidase activity and increased protein tyrosine phosphorylation of mitochondria-rich fractions of buffalo (Bubalus bubalis) spermatozoa after a cycle of freezing and thawing

2019 ◽  
Vol 31 (10) ◽  
pp. 1567 ◽  
Author(s):  
Arya P. Panda ◽  
Sudhir C. Roy ◽  
Deepak T. Sakhare ◽  
Sharanabasav Badami ◽  
Bannur C. Divyashree ◽  
...  
Keyword(s):  
Cytochrome Oxidase ◽  
Tyrosine Phosphorylation ◽  
Oxidase Activity ◽  
Mitochondrial Protein ◽  
Sucrose Density Gradient ◽  
Vital Role ◽  
Mitochondrial Proteins ◽  
Freezing And Thawing ◽  
Cytochrome Oxidase Activity ◽  
Cryopreserved Sperm

The motility and fertility of mammalian spermatozoa are compromised when they are cryopreserved. Sperm mitochondrial proteins play a vital role in conferring motility. However, the effects of cryopreservation on mitochondria-specific proteins remain primarily unexplored in domestic animals, including buffaloes, so the present study aimed to evaluate this issue. Mitochondria were isolated from both non-cryopreserved and cryopreserved buffalo spermatozoa by sonication followed by sucrose density gradient ultracentrifugation. The purity of the mitochondrial preparation was assessed by cytochrome oxidase assay and electron microscopy. Mitochondria separated from cryopreserved buffalo spermatozoa were associated with significantly lower (P ≤ 0.05) cytochrome oxidase activity as compared with non-cryopreserved spermatozoa. The intensities of two low-molecular-mass mitochondrial proteins (30.1 kDa and 26.1 kDa) were significantly reduced as compared with the non-cryopreserved group. In addition, in cryopreserved buffalo sperm mitochondria, the intensities of three tyrosine phosphorylated proteins (126.6, 106.7 and 26 kDa) increased significantly compared with the non-cryopreserved group. Of these, tyrosine phosphorylation of the 26-kDa mitochondrial protein of cryopreserved sperm was very intense and unique because it could not be detected in the mitochondria of non-cryopreserved sperm. Thus, the study confirmed that both cytochrome oxidase activity and the proteins of buffalo sperm mitochondria undergo significant cryogenic changes in terms of quantity and quality after a cycle of freezing and thawing and this may be one of the important causes of reduced post-thaw motility and fertility of cryopreserved buffalo spermatozoa.

Changes in concentrations of respiratory components and cytochrome oxidase activity in mitochondria obtained from carbon tetrachloride-induced cirrhotic rat liver

1988 ◽  
Vol 74 (5) ◽  
pp. 485-489 ◽  
Author(s):  
Taisuke Morimoto ◽  
Akira Tanaka ◽  
Yoshiro Taki ◽  
Masashi Noguchi ◽  
Naoki Yokoo ◽  
...  
Keyword(s):  
Carbon Tetrachloride ◽  
Cytochrome Oxidase ◽  
Cytochrome B ◽  
Rat Liver ◽  
Coenzyme Q10 ◽  
Oxidase Activity ◽  
Energy Charge ◽  
Mitochondrial Protein ◽  
Cirrhotic Liver ◽  
Cytochrome Oxidase Activity

1. Changes in the concentrations of respiratory components, phosphorylative activity, the cytochrome oxidase activity of mitochondria and the hepatic adenylate energy charge level (in situ) were studied in cirrhotic rat liver induced by carbon tetrachloride (CCl4). 2. In the cirrhotic liver mitochondria, concentrations of cytochrome a(+ a3), cytochrome b, coenzyme Q9 and coenzyme Q10 increased significantly to 2.44 ± 0.02 × 10−10 (mean ± se), 1.37 ± 0.05 × 10−10, 25.57 ± 0.47 × 10−10 and 5.39 ± 0.26 × 10−10 mol/mg of mitochondrial protein, respectively, compared with 1.83 ± 0.03 × 10−10, 1.22 ± 0.02 × 10−10, 16.24 ± 0.39 × 10−10 and 1·81 ± 0.07 × 10−10 in normal rats [P < 0.001 for cytochrome a(+ a3), coenzyme Q9 and coenzyme Q10, and P < 0.01 for cytochrome b]. 3. Concentrations of flavoprotein and pyridine nucleotides decreased significantly to 13.33 ± 0.14 × 10−10 and 45.68 ± 1.59 × 10−10 mol/mg of mitochondrial protein, respectively, compared with 14.79 ± 0.33 × 10−10 and 86.26 ± 1.83 × 10−10 in normal rats (P < 0.001). There was no significant difference in the concentration of cytochrome c(+ c1). 4. Cytochrome oxidase activity per unit of cytochrome a(+ a3) increased significantly to 67.43 ± 1.71 atoms O s−1 mol−1, compared with 55.77 ± 1.16 in normal rats (P < 0.001). By contrast, phosphorylative activity per unit of cytochrome a(+ a3) decreased significantly in the cirrhotic liver to 10.40 ± 0.36 s−1 compared with 13.43 ± 0.49 in normal rats (P < 0.001). The total adenine nucleotide concentration and the hepatic energy charge level decreased significantly in the cirrhotic liver to 3.420 ± 0.075 μmol/g of wet liver and 0.806 ± 0.003, respectively, compared with 3·854 ± 0.088 and 0.841 ± 0.004 in normal rats (P < 0.001). 5. It is concluded that in mitochondria obtained from CCl4-induced cirrhotic rat liver in which the energy charge level is decreased, cytochrome oxidase activity per unit of cytochrome a(+ a3) is increased in association with an increase in cytochrome a(+ a3) concentration.

Loose-coupled mitochondria in chronic glucagon-treated hyperthermic ducklings

1989 ◽  
Vol 256 (6) ◽  
pp. R1192-R1199 ◽  
Author(s):  
H. Barre ◽  
G. Berne ◽  
P. Brebion ◽  
F. Cohen-Adad ◽  
J. L. Rouanet
Keyword(s):  
Creatine Kinase ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Kinase Activity ◽  
Mitochondrial Protein ◽  
Creatine Kinase Activity ◽  
Strong Increase ◽  
Muscle Mitochondria ◽  
Glucagon Test ◽  
Cytochrome Oxidase Activity

In chronic glucagon-treated ducklings (GT) showing thermogenic and hyperthermic responses without shivering to glucagon test injection and in control ducklings (TN; both aged 44 +/- 1 days and reared at thermoneutrality), subsarcolemmal (S) and intermyofibrillar (I) mitochondria from gastrocnemius muscle and mitochondria from liver were isolated. Respiration and cytochrome oxidase activity were determined in these isolated mitochondria by polarography and creatine kinase activity by spectrophotometry, both at 25 degrees C. In GT ducklings, the powerful thermogenesis observed in vivo after a glucagon test injection may be due to the uncoupling effect of released free fatty acids (FFA) in loose-coupled mitochondria because their respiration increased as a function of FFA concentration, and the loose coupling of these mitochondria was reversed by addition of albumin. In all types of mitochondria from GT ducklings, the increase in respiration because of FFA was about double that in mitochondria from controls. There was no change in creatine kinase activity from liver and I mitochondria, but a 16% decrease in this enzyme activity (expressed per mg mitochondrial protein) from S mitochondria was shown despite a strong increase in cytochrome oxidase activity from liver mitochondria (+114% if expressed per g tissue) and from muscle mitochondria (I, +53 or +48%; S, +41 or +97% if expressed per mg mitochondrial protein or per g tissue, respectively). These results support a coupling defect in liver and skeletal muscle mitochondria from the GT hyperthermic ducklings and an uncoupling reinforcement by FFA.

Effect of 3,3′-di-iodothyronine and 3,5-di-iodothyronine on rat liver mitochondria

1993 ◽  
Vol 136 (1) ◽  
pp. 59-64 ◽  
Author(s):  
A. Lanni ◽  
M. Moreno ◽  
M. Cioffi ◽  
F. Goglia
Keyword(s):  
Cytochrome Oxidase ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Mitochondrial Protein ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Activity ◽  
Mitochondrial Mass ◽  
Cytochrome Oxidase Activity ◽  
Other Hand

ABSTRACT In the present study we report that 3,3′,5-tri-iodothyronine (T3) as well as two iodothyronines (3,5-diiodothyronine (3,5-T2) and 3,3′-di-iodothyronine (3,3′-T2)) significantly influence rat liver mitochondrial activity. Liver oxidative capacity (measured as cytochrome oxidase activity/g wet tissue) in hypothyroid compared with normal rats was significantly reduced (21%, P > 0·01) and the administration of T3 and both iodothyronines restored normal values. At the mitochondrial level, treatment with T3 stimulated respiratory activity (state 4 and state 3) and did not influence cytochrome oxidase activity. On the other hand, both the mitochondrial respiratory rate and specific cytochrome oxidase activity significantly increased in hypothyroid animals after treatment with 3,3′-T2 or 3,5-T2 (about 50 and 40% respectively). The actions of both iodothyronines were rapid and evident by 1 h after the injection. The hepatic mitochondrial protein content which decreased in hypothyroid rats (9·6 mg/g liver compared with 14·1 in normal controls, P < 0·05) was restored by T3 injection, while neither T2 was able to restore it. Our results suggest that T3 and both iodothyronines have different mechanisms of action. T3 acts on both mitochondrial mass and activity; the action on mitochondrial activity was not exerted at the cytochrome oxidase complex level. The action of the iodothyronines, on the other hand, is exerted directly on the cytochrome oxidase complex without any noticeable action on the mitochondrial mass. Journal of Endocrinology (1993) 136, 59–64

Cytochrome Oxidase Activity at The Hepatic Parenchyma Different Periods of Ischemia and Obstructive Jaundice

2019 ◽  
Vol 9 (5) ◽  
pp. p8944
Author(s):  
Askarov Tahir Askarovich ◽  
Akhmedov Mirhalil Dzhalilovich ◽  
Fayziev Yokub Nishanovic ◽  
Ashurmetov Ahmadjon Makhamadjonovich ◽  
Dalimov Kenjabek Sabutaevich ◽  
...  
Keyword(s):  
Obstructive Jaundice ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Hepatic Parenchyma ◽  
Cytochrome Oxidase Activity

Histochemical assessment of cytochrome oxidase activity for monitoring ischemic muscle injury

1985 ◽  
Vol 88 (2) ◽  
pp. 265-276 ◽  
Author(s):  
Richard M. Millis ◽  
Theodore A. Stephens ◽  
Gerard Harris ◽  
Columbus Anonye ◽  
Michael Reynolds
Keyword(s):  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Muscle Injury ◽  
Cytochrome Oxidase Activity ◽  
Ischemic Muscle

scholarly journals TISSUE CYTOCHROME OXIDASE ACTIVITY AND BODY WEIGHT

1952 ◽  
Vol 198 (1) ◽  
pp. 229-236
Author(s):  
H.O. Kunkel ◽  
J.E. Campbell
Keyword(s):  
Body Weight ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Cytochrome Oxidase Activity

Changes in Cytochrome Oxidase Activity of the Isolated Perfused Rabbit Kidney

1967 ◽  
Vol 8 (3) ◽  
pp. 235-240
Author(s):  
H.H. Mazarean ◽  
G. Domján ◽  
Ö. Takács
Keyword(s):  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Rabbit Kidney ◽  
Cytochrome Oxidase Activity

scholarly journals Cytochrome Oxidase Activity and Confocal Laser Scanning Microscopic Analysis of the Hamster Submandibular Gland Using Microwave Irradiated Fixation

Scanning ◽  
2006 ◽  
Vol 24 (6) ◽  
pp. 314-320 ◽  
Author(s):  
K. Moriguchi ◽  
M. Utsumi ◽  
H. Maeda ◽  
Y. Kameyama ◽  
N. Ohno
Keyword(s):  
Cytochrome Oxidase ◽  
Submandibular Gland ◽  
Oxidase Activity ◽  
Laser Scanning ◽  
Microscopic Analysis ◽  
Confocal Laser Scanning ◽  
Confocal Laser ◽  
Cytochrome Oxidase Activity
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