scholarly journals Gender- and region-specific changes in estrogen signaling in aging rat brain mitochondria

Aging ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 2148-2169 ◽  
Author(s):  
Christopher M. Evola ◽  
Tanner L. Hudson ◽  
Luping Huang ◽  
Adrian M. Corbett ◽  
Debra A. Mayes
Keyword(s):  
Rat Brain ◽  
Brain Mitochondria ◽  
Estrogen Signaling ◽  
Rat Brain Mitochondria ◽  
Aging Rat

Acyl-CoA: sn-Glycerol-3-Phosphate O-Acyltransferase in Rat Brain Mitochondria and Microsomes

1982 ◽  
Vol 39 (1) ◽  
pp. 286-289 ◽  
Author(s):  
Susan M. Fitzpatrick ◽  
Giovanna Sorresso ◽  
Dipak Haldar
Keyword(s):  
Rat Brain ◽  
Brain Mitochondria ◽  
Rat Brain Mitochondria

scholarly journals The role of ADP in the modulation of the calcium-efflux pathway in rat brain mitochondria

1985 ◽  
Vol 225 (1) ◽  
pp. 41-49 ◽  
Author(s):  
J Vitorica ◽  
J Satrústegui
Keyword(s):  
Rat Brain ◽  
Binding Sites ◽  
Tricarboxylic Acid Cycle ◽  
Brain Mitochondria ◽  
Ruthenium Red ◽  
Calcium Efflux ◽  
Rat Brain Mitochondria ◽  
Pi Complex ◽  
Efflux Pathway

The role of ADP in the regulation of Ca2+ efflux in rat brain mitochondria was investigated. ADP was shown to inhibit Ruthenium-Red-insensitive H+- and Na+-dependent Ca2+-efflux rates if Pi was present, but had no effect in the absence of Pi. The primary effect of ADP is an inhibition of Pi efflux, and therefore it allows the formation of a matrix Ca2+-Pi complex at concentrations above 0.2 mM-Pi and 25 nmol of Ca2+/mg of protein, which maintains a constant free matrix Ca2+ concentration. ADP inhibition of Pi and Ca2+ efflux is nucleotide-specific, since in the presence of oligomycin and an inhibitor of adenylate kinase ATP does not substitute for ADP, is dependent on the amount of ADP present, and requires ADP concentrations in excess of the concentrations of translocase binding sites. Brain mitochondria incubated with 0.2 mM-Pi and ADP showed Ca2+-efflux rates dependent on Ca2+ loads at Ca2+ concentrations below those required for the formation of a Pi-Ca2+ complex, and behaved as perfect cytosolic buffers exclusively at high Ca2+ loads. The possible role of brain mitochondrial Ca2+ in the regulation of the tricarboxylic acid-cycle enzymes and in buffering cytosolic Ca2+ is discussed.

scholarly journals Effect of phenylpyruvate on pyruvate dehydrogenase activity in rat brain mitochondria

1973 ◽  
Vol 134 (2) ◽  
pp. 539-544 ◽  
Author(s):  
John M. Land ◽  
John B. Clark
Keyword(s):  
Rat Brain ◽  
Dehydrogenase Activity ◽  
Pyruvate Dehydrogenase ◽  
Pyruvate Dehydrogenase Complex ◽  
Competitive Inhibitor ◽  
Brain Mitochondria ◽  
Significant Inhibition ◽  
Complex Activity ◽  
Rat Brain Mitochondria ◽  
Dehydrogenase Complex

1. The effects of phenylpyruvate, a metabolite produced in phenylketonuria, on the pyruvate dehydrogenase-complex activity were investigated in rat brain mitochondria. 2. Pyruvate dehydrogenase activity was measured by two methods, one measuring the release of 14CO2 from [1-14C]pyruvate and the other measuring the acetyl-CoA formed by means of the coupling enzyme, pigeon liver arylamine acetyltransferase (EC 2.3.1.5). In neither case was there significant inhibition of the pyruvate dehydrogenase complex by phenylpyruvate at concentrations below 2mm. 3. However, phenylpyruvate acted as a classical competitive inhibitor of the coupling enzyme arylamine acetyltransferase, with a Ki of 100μm. 4. It was concluded that the inhibition of pyruvate dehydrogenase by phenylpyruvate is unlikely to be a primary enzyme defect in phenylketonuria.

Arginine Transport in Rat Brain Mitochondria

1987 ◽  
Vol 494 (1 Third Colloqu) ◽  
pp. 291-293 ◽  
Author(s):  
JAMES WATROUS ◽  
ELLEN KEELEY
Keyword(s):  
Rat Brain ◽  
Brain Mitochondria ◽  
Rat Brain Mitochondria ◽  
Arginine Transport
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