32. Correlation in cryoinjury of mitochondrial ultrastructure with respiratory control ratio, cytochrome oxidase activity, and rate of tissue oxygen consumption

Cryobiology ◽  
1970 ◽  
Vol 6 (6) ◽  
pp. 581
1982 ◽  
Vol 2 (6) ◽  
pp. 715-719 ◽  
Author(s):  
Roland Perasso ◽  
Jean-Jacques Curgy ◽  
Nicole Stelly ◽  
Jean Andre

The effects of chloramphenicol (CAP) on mitochondrial respiratory activity in the wild strain (ST) and in a cytoplasmic CAP-resistant mutant (STR1) ofTetrahymena pyriformiswere studied by determining oxygen consumption, by spectrophotometry, and by cytochemistry. In the absence of CAP both strains had the same respiration capacity, and the low-temperature spectra of their isolated mitochondria were similar. Furthermore, the mitochondria of both strains showed a positive reaction with diaminobenzidine, denoting a similar cytochrome oxidase activity. However, when cells were grown in CAP for 24 or 48 h, the peaks of cytochrome oxidase and cytochromebwere almost absent in the wild type. In this type the oxygen consumption was greatly decreased, and the mitochondria were no longer stained by diaminobenzidine. In the mutant, the peaks of cytochrome oxidase and cytochromebwere decreased only; respiration was less affected than in the wild type, and cytochrome oxidase activity was still disclosed by the diaminobenzidine reaction. These results show that CAP inhibits the synthesis of two cytochromes (band oxidase) which are partially translated into the mitochrondria ofT. pyriformis.In the mutant, CAP reduces only the mitochondrial translation, resulting in reduced mitochondrial activity and reduced growth rate of the cell. These results are compared with the nucleo-mitochondrial regulation mechanisms discussed in our previous works.


Development ◽  
1982 ◽  
Vol 71 (1) ◽  
pp. 75-82
Author(s):  
B. Ove Nilsson ◽  
Claes Magnusson ◽  
Sibylle Widéhn ◽  
Torbjörn Hillensjö

Delayed blastocysts had an oxygen consumption of 0·24 nl/h, while only 4 h after an oestrogen injection the respiration had increased nearly two fold, remaining at this level both 8 and 18 h after activation for implantation. The mitochondria of delayed blastocysts exhibited no positive cytochrome oxidase reaction, neither in the trophoblast nor in the embryoblasts. A few mitochondria at 8 h and most of those of blastocysts activated for 18 h were positive. It is suggested that the activation of blastocysts for implantation is initiated by a surge of substrates for glycolysis into the uterine secretion causing an increased energy production by glycolysis which in turn makes possible an increase of the cytochrome oxidase activity of the mitochondria thus getting oxidative phosphorylation into action.


1959 ◽  
Vol 109 (2) ◽  
pp. 187-195 ◽  
Author(s):  
Marie M. Daly ◽  
E. Gambetta Gurpide

Oxygen consumption and cytochrome oxidase activity of aortas of rats with experimental hypertension were found to be higher than the corresponding values for aortas of normotensive animals. The higher metabolic activity of aortas of hypertensive animals appeared to be due both to an increase in the proportion of muscle cells to connective tissue fibers and to a higher activity of the intracellular portion of the tissue.


1987 ◽  
Vol 248 (1) ◽  
pp. 161-165 ◽  
Author(s):  
F Malatesta ◽  
G Antonini ◽  
P Sarti ◽  
M Brunori

The activity of cytochrome oxidase reconstituted into phospholipid vesicles has been studied as a function of orthophosphate, ATP and inositol hexakisphosphate concentrations. The respiratory-control ratio was found to be quite sensitive to these compounds and was inversely related to the anion concentration. This effect is related to a phosphate-dependent decrease in the rate constant for ferrocytochrome c oxidation observed in the presence of ionophores. The data cannot be interpreted simply on the basis of ionic strength, which is known to limit cytochrome c binding to cytochrome oxidase, since cytochrome oxidase-containing vesicles responded differently to phosphate depending on the energization state of the phospholipid membrane.


1982 ◽  
Vol 2 (6) ◽  
pp. 715-719
Author(s):  
Roland Perasso ◽  
Jean-Jacques Curgy ◽  
Nicole Stelly ◽  
Jean Andre

The effects of chloramphenicol (CAP) on mitochondrial respiratory activity in the wild strain (ST) and in a cytoplasmic CAP-resistant mutant (STR 1 ) of Tetrahymena pyriformis were studied by determining oxygen consumption, by spectrophotometry, and by cytochemistry. In the absence of CAP both strains had the same respiration capacity, and the low-temperature spectra of their isolated mitochondria were similar. Furthermore, the mitochondria of both strains showed a positive reaction with diaminobenzidine, denoting a similar cytochrome oxidase activity. However, when cells were grown in CAP for 24 or 48 h, the peaks of cytochrome oxidase and cytochrome b were almost absent in the wild type. In this type the oxygen consumption was greatly decreased, and the mitochondria were no longer stained by diaminobenzidine. In the mutant, the peaks of cytochrome oxidase and cytochrome b were decreased only; respiration was less affected than in the wild type, and cytochrome oxidase activity was still disclosed by the diaminobenzidine reaction. These results show that CAP inhibits the synthesis of two cytochromes ( b and oxidase) which are partially translated into the mitochrondria of T. pyriformis. In the mutant, CAP reduces only the mitochondrial translation, resulting in reduced mitochondrial activity and reduced growth rate of the cell. These results are compared with the nucleo-mitochondrial regulation mechanisms discussed in our previous works.


1977 ◽  
Vol 73 (1) ◽  
pp. 56-77 ◽  
Author(s):  
A Wiseman ◽  
N W Gillham ◽  
J E Boynton

Wild type cells of the green alga Chlamydomonas reinhardtii can grow in the in the dark by taking up and respiring exogenously supplied acetate. Obligate photoautotrophic (dark dier, dk) mutants of this alga have been selected which grow at near wild type rates in the light, but rapidly die when transferred to darkness because of defects in mitochondrial structure and function. In crosses of the dk mutants to wild type, the majority of the mutants are inherited in a mendelian fashion, although two have been isolated which are inherited in a clearly nonmendelian fashion. Nine mendelian dk mutants have been analyzed in detail, and belong to eight different complementation groups representing eight gene loci. These mutants have been tentatively grouped into three classes on the basis of the pleiotropic nature of their phenotypic defects. Mutants in Class I have gross alterations in the ultrastructure of their mitochondrial inner membranes together with deficiencies in cytochrome oxidase and antimycin/rotenone-sensitive NADH-cytochrome c reductase activities. Mutants in Class II have a variety of less severe alterations in mitochondrial ultrastructure and deficiencies in cytochrome oxidase activity. Mutants in Class III have normal or near normal mitochondrial ultrastructure and reduced cytochrome oxidase activity. Eight of the nine mutants show corresponding reductions in cyanide-sensitive respiration.


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