Evolution of mammalian endothermic metabolism: mitochondrial activity and cell composition

1989 ◽  
Vol 256 (1) ◽  
pp. R63-R69 ◽  
Author(s):  
A. J. Hulbert ◽  
P. L. Else

Body composition was measured and compared in Amphibolurus vitticeps and Rattus norvegicus (a reptile and a mammal with the same weight and body temperature). Homogenates were prepared from liver, kidney, brain, heart, lung, and skeletal (gastrocnemius) muscle, and mitochondria were isolated. Cytochrome oxidase activities of both tissue homogenates and isolated mitochondria were measured (at 37 degrees C) as was protein content. Phospholipids were extracted from liver and kidney, and the fatty acid composition was determined. The brain, liver, kidney, heart, and skeletal muscle were significantly larger in the mammal, whereas the skin, reproductive organs, lung, and digestive tract showed no significant difference in size. All mammalian tissues examined contained approximately 50% more protein and phospholipid than the respective reptilian tissue. Although the mammalian phospholipids contained significantly less total unsaturated fatty acids, these unsaturated fatty acids were significantly more polyunsaturated than in the reptilian tissues. Tissue cytochrome oxidase activity was significantly greater in mammals when expressed on a wet weight basis but not when expressed on a tissue protein basis. Mitochondrial cytochrome oxidase activity (on a protein basis) was the same in both species in liver, kidney, and brain, but in heart, lung, and skeletal muscle mammalian mitochondria were twice as active as reptilian mitochondria. The implications of these differences in tissue composition were discussed relative to the evolution of mammalian endothermy.

1971 ◽  
Vol 49 (6) ◽  
pp. 545-553 ◽  
Author(s):  
Jean Himms–Hagen

The aim of these experiments was to depress the increased metabolic activity of the brown adipose tissue in the intact rat during acclimation to cold in order to elucidate further the possible thermogenic and endocrine functions of this tissue. The antibiotic oxytetracycline was administered twice daily for 2 weeks to rats living at 4 °C in an attempt to inhibit the proliferation of mitochondria and of mitochondrial inner membrane known to occur in the brown adipose tissue in response to cold; control rats received saline during the same period. Total cytochrome oxidase activity served as an index of the amount of mitochondrial inner membrane in brown adipose tissue, liver, and skeletal muscle. The development of an enhanced calorigenic response to intravenously infused noradrenaline served as an index of the extent of acclimation to cold.Treatment with oxytetracycline inhibited both the cold-induced increase in cytochrome oxidase activity in brown adipose tissue and the cold-induced development of an enhanced calorigenic response to noradrenaline in the intact rats; a direct correlation was noted between the amount of cytochrome oxidase in brown adipose tissue and the size of the metabolic response to noradrenaline of the intact animals. However, the amount of oxygen that could be consumed by the total cytochrome oxidase in the brown adipose tissue was itself too small to account for the increase in oxygen consumption by the rat. Treatment of the rats with oxytetracycline did not alter the cold-induced growth of brown adipose tissue (as judged by the increase in wet weight and the increase in total protein); it also did not alter the cytochrome oxidase activities of liver or skeletal muscle. The effect of oxytetracycline seems, therefore, to be fairly specific for the mitochondria of the most rapidly dividing tissue, the brown adipose tissue. The conclusion is drawn that a protein synthesized in the mitochondria of the brown adipose tissue in response to cold is essential for adaptation to cold.


1965 ◽  
Vol 48 (5) ◽  
pp. 737-752 ◽  
Author(s):  
H. Schuel ◽  
L. Lorand ◽  
R. Schuel ◽  
N. G. Anderson

Supernatants of rat skeletal muscle homogenates were fractionated by differential centrifugation and by zonal centrifugation in sucrose density gradients. Cytochrome oxidase was employed as an enzymatic marker for locating mitochondria. The subcellular fractions were also assayed for their ability to prevent the ATP-induced contraction of myofibrils. Both the mitochondrial and microsomal fractions obtained by differential fractionation were found to be rich in such relaxing activity, and the microsomal fraction was appreciably contaminated by mitochondria. In contrast to this, when fractionation was carried out by means of zonal centrifugation (4200 RPM x 205 min. to 40,000 RPM x 60 min.), relaxing activity was found to be associated only with particles having the sedimentation characteristics of microsomes (s20,w estimated to be between 370 and 1880S). Relaxing activity was not detected in the regions of the gradient containing either the starting sample zone (soluble phase) or the mitochondrial peak. The microsomal relaxing particles showed negligible cytochrome oxidase activity.


1993 ◽  
Vol 136 (1) ◽  
pp. 59-64 ◽  
Author(s):  
A. Lanni ◽  
M. Moreno ◽  
M. Cioffi ◽  
F. Goglia

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


Author(s):  
Askarov Tahir Askarovich ◽  
Akhmedov Mirhalil Dzhalilovich ◽  
Fayziev Yokub Nishanovic ◽  
Ashurmetov Ahmadjon Makhamadjonovich ◽  
Dalimov Kenjabek Sabutaevich ◽  
...  

1985 ◽  
Vol 88 (2) ◽  
pp. 265-276 ◽  
Author(s):  
Richard M. Millis ◽  
Theodore A. Stephens ◽  
Gerard Harris ◽  
Columbus Anonye ◽  
Michael Reynolds

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