Burst of succinate dehydrogenase and α-ketoglutarate dehydrogenase activity in concert with the expression of genes coding for respiratory chain proteins underlies short-term beneficial physiological stress in mitochondria.
Conditions for the realization in rats of moderate physiological stress (PHS) (30-120 min) were selected, which preferentially increase adaptive restorative processes without adverse responses typical of harmful stress (HST). The succinate dehydrogenase (SDH) and α-ketoglutarate dehydrogenase (KDH) activity and the formation of reactive oxygen species (ROS) in mitochondria were measured in lymphocytes by the cytobiochemical method, which detects the regulation of mitochondria in the organism with high sensitivity. These mitochondrial markers undergo an initial 10-20-fold burst of activity followed by a decrease to a level exceeding the quiescent state 2-3-fold by 120 min of PHS. By 30-60 min, the rise in SDH activity was greater than in KDH activity, while the activity of KDH prevailed over that of SDH by 120 min. The attenuation of SDH hyperactivity during PHS occurs by a mechanism other than oxaloacetate inhibition developed under HST. The dynamics of SDH and KDH activity corresponds to the known physiological replacement of adrenergic regulation by cholinergic during PHS, which is confirmed here by mitochondrial markers because their activity reflects these two types of nerve regulation, respectively. The domination of cholinergic regulation provides the overrestoration of expenditures for activity. In essence, this phenomenon corresponds to the training of the organism. It was first revealed in mitochondria after a single short-time stress episode. The burst of ROS formation was congruous with changes in SDH and KDH activity, as well as in ucp2 and cox3 expression, while the activity of SDH was inversely dependent on the expression of the gene of its catalytic subunit in the spleen. As the SDH activity enhanced, the expression of the succinate receptor decreased with subsequent dramatic rise when the activity was becoming lower. This article is part of a Directed Issue entitled: Bioenergetic dysfunction, adaption and therapy.
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Russia.
Marina V
MV
Zakharchenko
A V
AV
Zakharchenko
N V
NV
Khunderyakova
M N
MN
Tutukina
M A
MA
Simonova
A A
AA
Vasilieva
O I
OI
Romanova
N I
NI
Fedotcheva
E G
EG
Litvinova
E I
EI
Maevsky
V P
VP
Zinchenko
A V
AV
Berezhnov
I G
IG
Morgunov
A A
AA
Gulayev
M N
MN
Kondrashova
D000818:Animals; D004579:Electron Transport; D005786:Gene Expression Regulation; D007655:Ketoglutarate Dehydrogenase Complex / Q000235:genetics / Q000378:metabolism*; D008297:Male; D008928:Mitochondria / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D013312:Stress, Physiological / Q000235:genetics; D013385:Succinate Dehydrogenase / Q000235:genetics / Q000378:metabolism*
D007655:Ketoglutarate Dehydrogenase Complex; D013385:Succinate Dehydrogenase