Correlation between Degree of Rupture of Outer Mitochondrial Membrane and Changes of Kinetics of Regulation of Respiration by ADP in Permeabilized Heart and Liver Cells

Saks, Valdur; Belikova, Yulia; Vasilyeva, Elena; Кузнецов, А. В.; Fontaine, Éric; Kériel, Christiane; Leverve, Xavier; Saks, V.; Belikova, Y.; Vasilyeva, E.; Kuznetsov, A.; Fontaine, E.; Keriel, C.; Leverve, X.

doi:10.1006/bbrc.1995.1924

Cited by 8 publications

(14 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A similar situation was observed in permeabilized cells for NADH in yeast (28) and in hepatocytes (37). In each of these cases, it was found that closure of the voltage-dependent anion channel was responsible for restraining molecule flux to the intermembrane space (14,40). Since the voltage-dependent anionic channel is closed in permeabilized spheroplasts, it is possible that the hexose monophosphate diffusion is constrained.…”

Section: Resultssupporting

confidence: 56%

Mitochondrial Oxidative Phosphorylation Is Regulated by Fructose 1,6-Bisphosphate

Díaz-Ruiz

Avéret

Araiza

et al. 2008

Journal of Biological Chemistry

142

109

View full text Add to dashboard Cite

In numerous cell types, tumoral cells, proliferating cells, bacteria, and yeast, respiration is inhibited when high concentrations of glucose are added to the culture medium. This phenomenon has been named the "Crabtree effect." We used yeast to investigate (i) the short term event(s) associated with the Crabtree effect and (ii) a putative role of hexose phosphates in the inhibition of respiration. Indeed, yeast divide into "Crabtree-positive," where the Crabtree effect occurs, and "Crabtree-negative," where it does not. In mitochondria isolated from these two categories of yeast, we found that low, physiological concentrations of glucose 6-phosphate and fructose 6-phosphate slightly (20%) stimulated the respiratory flux and that this effect was strongly antagonized by fructose 1,6-bisphosphate (F16bP). On the other hand, F16bP by itself was able to inhibit mitochondrial respiration only in mitochondria isolated from a Crabtree-positive strain. Using permeabilized spheroplasts from Crabtree-positive yeast, we have shown that the sole effect observed at physiological concentrations of hexose phosphates is an inhibition of oxidative phosphorylation by F16bP. This F16bP-mediated inhibition was also observed in isolated rat liver mitochondria, extending this process to mammalian cells. From these results and taking into account that F16bP is able to accumulate in the cell cytoplasm, we propose that F16bP regulates oxidative phosphorylation and thus participates in the establishment of the Crabtree effect.

show abstract

Section: Resultssupporting

confidence: 56%

Mitochondrial Oxidative Phosphorylation Is Regulated by Fructose 1,6-Bisphosphate

Díaz-Ruiz

Avéret

Araiza

et al. 2008

Journal of Biological Chemistry

142

109

View full text Add to dashboard Cite

show abstract

“…As shown earlier for skinned cardiac muscles, hypoosmotic treatment of skinned fibres resulted in the appearance of a population of mitochondria with high affinity for ADP 191. This effect is related to the damage of the outer mitochondrial membrane since it correlates with the effect of exogenous cytochrome c on the respiration [9]. Table 1 shows the same result for skinned fibres from soleus, which confirms that the low affinity of mitochondria for ADP in vivo is due to the decreased permeability of the outer mitochondria1 membrane for this substrate.…”

Section: Kinetics Of Respiration Regulation By Adpsupporting

confidence: 64%

“…In KCI-containing medium, cytochrome c dissociates from the outer surface of the inner mitochondrial membrane and if the outer mitochondrial membrane is damaged it leaves the mitochondrial intermembrane space, which decreases the rate of respiration [9]. However, addition of exogenous cytochrome c completely restores respiration under these conditions [9]. The results of this test for investigation of the state of the outer mitochondrial membrane after treatment of the skinned fibres by trypsin are shown in Fig.…”

Section: Effects Of Proteolytic Enzymes (Trypsin Chymotrypsin and Elmentioning

confidence: 99%

“…Maximal oxygen-consumption rates and K:' (ADP) in different fibres. Means 2 SD are given for [6][7][8][9][10][11][12] experiments. Trypsin, chymotrypsin and elastase were used in concentration of 125 pg/ml.…”

Section: Kinetics Of Respiration Regulation By Adpmentioning

confidence: 99%

“…The cytochrome c test was used to investigate the state of the outer mitochondrial membrane before and after trypsin treatment. In KCI-containing medium, cytochrome c dissociates from the outer surface of the inner mitochondrial membrane and if the outer mitochondrial membrane is damaged it leaves the mitochondrial intermembrane space, which decreases the rate of respiration [9]. However, addition of exogenous cytochrome c completely restores respiration under these conditions [9].…”

Section: Effects Of Proteolytic Enzymes (Trypsin Chymotrypsin and Elmentioning

confidence: 99%

See 2 more Smart Citations

Striking Differences Between the Kinetics of Regulation of Respiration by ADP in Slow‐Twitch and Fast‐Twitch Muscles In Vivo

Кузнецов

Tiivel

Sikk

et al. 1996

European Journal of Biochemistry

180

209

View full text Add to dashboard Cite

The kinetics of in vivo regulation of mitochondrial respiration by ADP was studied in rat heart, slowtwitch skeletal muscle (soleus) and fast-twitch skeletal muscle (gastrocnemius, plantaris, quadriceps and tibialis anterior) by means of saponin-skinned fibres. Mitochondria1 respiratory parameters were determined in the absence and presence of creatine (20 mM), and the effect of proteolytic enzymes (trypsin, chymotrypsin or elastase) on these parameters was investigated in detail. Chem. 270, 19921 -199291, who studied muscle fibres from normal and transgenic mice, that the kinetics of respiration regulation in muscle cells is tissue specific. We found that in rat cardiac and soleus muscle fibres the apparent K,,, for respiration regulation was 300-400 pM and decreased to 50-80 pM in the presence of creatine. In contrast, in skinned fibres from gastrocnemius, plantaris, tibialis anterior and quadriceps muscles, this value was initially very low, 10-20 pM, i.e. the same as that is in isolated muscle mitochondria, and the effect of creatine was not observable under these experimental conditions. Treatment of the fibres with trypsin, chymotrypsin or elastase (0.125 pg/ml) for 15 min decreased the apparent K,,, for ADP in cardiac and soleus muscle fibres to 40-98 pM without significant alteration of V,,,, or the intactness of outer mitochondrial membrane, as assessed by the cytochrome c test. In fibres from gastrocnemius, trypsin increased the apparent K,,, for ADP transiently. The effects of trypsin and chymotrypsin were studied in detail and found to be concentration dependent and time dependent. The effects were characterised by saturation phenomenon with respect to the proteolytic enzyme concentration, saturation being observed above 1 pM enzyme. These results are taken to show that in cardiac and slow-twitch skeletal muscle, the permeability of the outer mitochondrial membrane to adenine nucleotides is low and controlled by a cytoplasmic protein that is sensitive to trypsin and chymotrypsin. This protein may participate in feedback signal transduction by a mechanism of vectorial-ligand conduction. This protein factor is not expressed in fasttwitch skeletal muscle, in which cellular mechanism of regulation of respiration is probably very different from that of slow-twitch muscles.Keywords: heart; skeletal muscle; respiration ; regulation; adenine nucleotide.The cellular mechanism of regulation of respiration in vivo is still unknown. The conventional explanation that the rate of respiration of mitochondria in intact cells is governed by the cytoplasmic ADP concentration according to a simple Michaelis-Menten type relationship is in disagreement with many experimental data [l-51. First, it has been shown in numerous experiments on isolated hearts that the increases in workload and oxygen consumption are usually observed at stable, low and sometimes even decreasing steady-state ADP levels [I -51. Second, Kushmerick et al. have found that in slow-twitch skeletal muscle, an increase of frequency of stimulation does...

show abstract

The MyMOMA domain of MYO19 encodes for distinct Miro‐dependent and Miro‐independent mechanisms of interaction with mitochondrial membranes

et al. 2019

View full text Add to dashboard Cite

MYO19 interacts with mitochondria through a C‐terminal membrane association domain (MyMOMA). Specific mechanisms for localization of MYO19 to mitochondria are poorly understood. Using promiscuous biotinylation data in combination with existing affinity‐capture databases, we have identified a number of putative MYO19‐interacting proteins. We chose to explore the interaction between MYO19 and the mitochondrial GTPase Miro2 by expressing mchr‐Miro2 in combination with GFP‐tagged fragments of the MyMOMA domain and assaying for recruitment of MYO19‐GFP to mitochondria. Coexpression of MYO19898‐970‐GFP with mchr‐Miro2 enhanced MYO19898‐970‐GFP localization to mitochondria. Mislocalizing Miro2 to filopodial tips or the cytosolic face of the nuclear envelope did not recruit MYO19898‐970‐GFP to either location. To address the kinetics of the Miro2/MYO19 interaction, we used FRAP analysis and permeabilization‐activated reduction in fluorescence analysis. MyMOMA constructs containing a putative membrane‐insertion motif but lacking the Miro2‐interacting region displayed slow exchange kinetics. MYO19898‐970‐GFP, which does not include the membrane‐insertion motif, displayed rapid exchange kinetics, suggesting that MYO19 interacting with Miro2 has higher mobility than MYO19 inserted into the mitochondrial outer membrane. Mutation of well‐conserved, charged residues within MYO19 or within the switch I and II regions of Miro2 abolished the enhancement of MYO19898‐970‐GFP localization in cells ectopically expressing mchr‐Miro2. Additionally, expressing mutant versions of Miro2 thought to represent particular nucleotide states indicated that the enhancement of MYO19898‐970‐GFP localization is dependent on Miro2 nucleotide state. Taken together, these data suggest that membrane‐inserted MYO19 is part of a larger complex, and that Miro2 plays a role in integration of actin‐ and microtubule‐based mitochondrial activities.

show abstract

Correlation between Degree of Rupture of Outer Mitochondrial Membrane and Changes of Kinetics of Regulation of Respiration by ADP in Permeabilized Heart and Liver Cells

Cited by 8 publications

References 0 publications

Mitochondrial Oxidative Phosphorylation Is Regulated by Fructose 1,6-Bisphosphate

Mitochondrial Oxidative Phosphorylation Is Regulated by Fructose 1,6-Bisphosphate

Striking Differences Between the Kinetics of Regulation of Respiration by ADP in Slow‐Twitch and Fast‐Twitch Muscles In Vivo

The MyMOMA domain of MYO19 encodes for distinct Miro‐dependent and Miro‐independent mechanisms of interaction with mitochondrial membranes

Contact Info

Product

Resources

About