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Are mitochondria dead?

Are mitochondria dead?


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In the video "What is Life? Is Death Real?", the subject of mitochondria is raised at 2:58. At 3:12, the narrator says "[mitochondria] are not alive any more: they are dead."

What currents of thought lead to this affirmation?

When I search for mitochondria are dead on Google, I get many links about the role of mitochondria in cell death, but I don't see anywhere that the assertion in this video is discussed.


SolarLunix posted an excellent answer detailing the criteria for being classified as "alive", and showed that by those criteria, mitochondria could be considered as "dead".

However, I would argue that the narrator's statement in your video does not make any sense. The currently-accepted theory of the evolution of mitochondria (and possibly other organelles) from free-living prokaryotes is called symbiogenesis and postulates that the mitochondrial progenitors began living symbiotically with the precursors to eukaryotes some 1.5 billion years ago. Life originated on Earth about 3.5 billion years ago, so eukaryotic cells (carrying mitochondria) have been around for a little less than half of that time.

In that incredibly large span of time (if you counted 1 number per second, you'd reach 1.5 billion in about 47.5 years), what used to be an independent organism (we assume) has become an organelle - an integral part of the eukaryotic cell. It absolutely could not survive outside the cell on its own, and relies on signals from the cell (mainly, the cell's energy needs as detected by "sensor" proteins to key molecules like glucose and ATP) to reproduce.

Therefore, it is most appropriate to think of mitochondria simply as another organelle, just like the endoplasmic reticulum, lysosomes, or the nucleus. It doesn't make sense to think of those other structures as "alive" or "dead", just as it doesn't make sense to think of mitochondria in the same way. Yes, they used to be independent, but are no longer; instead they are a well-integrated part of the whole cell.


Short answer: According to the definition of life, yes, Mitochondria are "dead".


To be considered alive an organism must meet the following criteria:

  • organized structure performing a specific function
  • an ability to sustain existence, e.g. by nourishment
  • an ability to respond to stimuli or to its environment
  • capable of adapting
  • an ability to germinate or reproduce

Are Mitochondria organised?

Yes, they have a structure that allows them to metabolise energy brought to it by the cell.

Can Mitochondria sustain their own existence?

No, many of the genes that mitochondria need to function are no longer in the mitochondria. They need the host cell to provide much of what they need for them.

Note that I am pointing to the Mitochondria's genetics. They used to be included in the Mitochondria itself and have been moved into the cell host DNA. This is why I consider them to be "dead" because they are no longer their own organism, they are an organelle that helps the cell stay alive.

We can stop here since this disqualifies Mitochondria from being considered alive. However, for completion, I will continue.

Can Mitochondria respond to stimuli?

Yes, in order for it to divide it receives signalling from the cell. I would consider this a response to its environment.

Can Mitochondria reproduce?

Yes, their reproduction is much like a bacteria reproduces - through a process called fission.


Conclusion: Since Mitochondria cannot sustain existence, alone (thanks to no longer holding their full genome) they are dead.


I would like to expand a bit on SolarLunix's post, because the logic used in the conclusion would also mean that endosymbionts, such as https://en.wikipedia.org/wiki/Buchnera_(bacterium), who cannot survive outside their host are also "dead".

I think many of us disagree with that notion, so instead I would say that it's the fact that so many of their genes have been relocated to the nucleus that makes them organelles and thus substructures of the eukaryotic cell and thus "dead".

Ultimately though, I think it's more a matter of semantics, since you could argue that they represent an advanced stage of endosymbiosis.


What a brilliant question for promoting a discussion. Mitochondria definitely reproduce, they maintain a better energy flow than any other part of the cell, and they maintain a very low entropy state by exploiting that energy flow. It may not be a textbook answer but being alive really is about decreasing your local entropy by exploiting a flow of energy. I suspect that mitochondria have ceased to change under the pressures of natural selection, but so what - they have been practically perfect for a billion years.


Are mitochondria dead? - Biology

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Mitochondria Definition

Mitochondria are cellular organelles that produce energy through aerobic respiration. Although mitochondria have many vital functions, they’re best known as the power plants of the cell.

They’re supremely important for your brain and your muscles as they use more energy than the rest of your organs.

Mitochondria are like cellular batteries that need to be constantly charged through respiration. They supply every cell, tissue, and organ in your body with energy. For example, your brain burns more energy than any other organ. Therefore your brain cells have a large number of mitochondria.

The health and strength of your body at any given time depends on the health of your mitochondria. If you want to increase your strength and energy potential you need to protect your mitochondria.


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Are mitochondria dead? - Biology

Pioneering biochemical studies have long forged the concept that the mitochondria are the ‘energy powerhouse of the cell’. These studies, combined with the unique evolutionary origin of the mitochondria, led the way to decades of research focusing on the organelle as an essential, yet independent, functional component of the cell. Recently, however, our conceptual view of this isolated organelle has been profoundly altered with the discovery that mitochondria function within an integrated reticulum that is continually remodeled by both fusion and fission events. The identification of a number of proteins that regulate these activities is beginning to provide mechanistic details of mitochondrial membrane remodeling. However, the broader question remains regarding the underlying purpose of mitochondrial dynamics and the translation of these morphological transitions into altered functional output. One hypothesis has been that mitochondrial respiration and metabolism may be spatially and temporally regulated by the architecture and positioning of the organelle. Recent evidence supports and expands this idea by demonstrating that mitochondria are an integral part of multiple cell signaling cascades. Interestingly, proteins such as GTPases, kinases and phosphatases are involved in bi-directional communication between the mitochondrial reticulum and the rest of the cell. These proteins link mitochondrial function and dynamics to the regulation of metabolism, cell-cycle control, development, antiviral responses and cell death. In this review we will highlight the emerging evidence that provides molecular definition to mitochondria as a central platform in the execution of diverse cellular events.


Results

H2O2-Induced Zygotic Cell Death Characterized by Morphology and TUNEL Stain

In control culture, B6C3F1 mouse zygotes cleaved normally (95%) at Day 2 and developed to blastocysts (92%) by Day 4 ( Fig. 2). In developed blastocysts, an average of 2 apoptotic cells were observed by TUNEL stain ( Fig. 3D), a result similar to that shown previously [ 43]. As it has been recognized that blastocysts exhibit PCD [ 32, 33, 43, 50], TUNEL-positive staining from blastocysts treated with H2O2 for 1 h were used as a positive control to confirm the effectiveness of this apoptotic assay applied in zygotes. Twenty-four hours after treatments, the total cell number (55 ± 19) was significantly (P < 0.05) reduced and percentage (25 ± 34%) of apoptotic cells significantly increased in blastocysts (n = 11) treated with 200 μM H2O2, compared to values for control, untreated blastocysts (106 ± 14 and 2 ± 2%, respectively, n = 14). However, 100 μM H2O2 treatment did not affect total as well as apoptotic cells in the blastocysts (112 ± 23 and 2 ± 3%, respectively, n = 11). In preliminary experiments, the effects of H2O2 on cleavage and development of zygotes or two-cell mouse embryos showed concentration and time dependence (data not shown).

Effects of H2O2 on development of mouse zygotes collected at Day 1. In untreated control culture, an average of 95% zygotes (n = 95) cleaved at Day 2, and 92% developed to blastocysts. Treatment of zygotes (n = 90) with 200 μM H2O2 inhibited cleavage and development, causing morphological hallmarks of apoptotic cell death, including cell shrinkage and membrane blebbing or cytoplasmic vacuoles

Effects of H2O2 on development of mouse zygotes collected at Day 1. In untreated control culture, an average of 95% zygotes (n = 95) cleaved at Day 2, and 92% developed to blastocysts. Treatment of zygotes (n = 90) with 200 μM H2O2 inhibited cleavage and development, causing morphological hallmarks of apoptotic cell death, including cell shrinkage and membrane blebbing or cytoplasmic vacuoles

TUNEL stain of cell death in mouse zygotes. In the negative control, the enzyme terminal deoxynucleotidyl transferase was not added. Top panels show negative control without enzyme added (A), TUNEL-negative stain in 200 μM H2O2-treated (15 min) zygotes (B), but positive stain (green fluorescence with fluorescein isothiocyanate filter) in 1 mM H2O2-treated (1.5 h) zygotes (C) within 24 h after treatment. Lower panels: TUNEL stain at Day 4 in a developed blastocyst as in control group (D) and 200 μM H2O2-arrested one-cell (E). Arrowhead indicates positive TUNEL nuclei, and arrow indicates polar body

TUNEL stain of cell death in mouse zygotes. In the negative control, the enzyme terminal deoxynucleotidyl transferase was not added. Top panels show negative control without enzyme added (A), TUNEL-negative stain in 200 μM H2O2-treated (15 min) zygotes (B), but positive stain (green fluorescence with fluorescein isothiocyanate filter) in 1 mM H2O2-treated (1.5 h) zygotes (C) within 24 h after treatment. Lower panels: TUNEL stain at Day 4 in a developed blastocyst as in control group (D) and 200 μM H2O2-arrested one-cell (E). Arrowhead indicates positive TUNEL nuclei, and arrow indicates polar body

Mild treatment of zygotes with 200 μM H2O2 for 15 min completely inhibited cleavage, and zygotes arrested at the one-cell stage thereafter ( Fig. 2). Treated zygotes exhibited shrunken morphology, but failed to display PI-positive staining 24 h after treatment, when pronuclei were not condensed. Only 31% zygotes showed PI-positive stain at 48 h after treatment. TUNEL assay did not reveal DNA fragmentation in pronuclei over 48 h ( Table 1). By 72 h after treatment, pronuclei were positively stained with PI, and 46% of zygotes showed weak TUNEL staining. In contrast, intensive treatment of zygotes with 1 mM H2O2 for 1.5 h induced shrunken pronuclei and fragmented DNA detected by TUNEL stain as early as 5 h, and more evidently by 24 h after treatment ( Fig. 3, C, C′, C″). At 5 h, zygotes underwent degeneration characterized by shrinkage of cytoplasm, membrane permeability to PI, and condensation of pronuclei ( Fig. 4). Table 1 shows that cell death occurred in zygotes as early as 5 h after intensive oxidative stress (1 mM H2O2 for 1.5 h), while obvious cell death did not occur until 48 h later in zygotes exposed to mild oxidative stress (200 μM H2O2 for 15 min). Moreover, the disruption of development and induction of cell death resulted from H2O2 itself because catalase, a decomposer of H2O2, could completely reverse this effect (data not shown).

H2O2-Induced cell death In mouse zygotes.

Treatment . Hours after treatment . % Dead a (no. examined) . % TUNEL-positive b (no. examined) .
Control 5 0 (50) 0 (30)
H2O2 (1 mM) 5-24 96 (67) 89 (3 7)
H2O2 (200 μM) c 24 0 (88) 0 (33)
48 31 (83) 0 (24)
72 88 (48) 46 (22)
Treatment . Hours after treatment . % Dead a (no. examined) . % TUNEL-positive b (no. examined) .
Control 5 0 (50) 0 (30)
H2O2 (1 mM) 5-24 96 (67) 89 (3 7)
H2O2 (200 μM) c 24 0 (88) 0 (33)
48 31 (83) 0 (24)
72 88 (48) 46 (22)

Live and dead stain Includes both PI and Hoechst stain, and Live and Dead Kit pooled data from at least 4 replicates.

Pooled data from 3 replicates.

Prior to 24 h after treatment, all zygotes were PI negative and did not exhibitTUNEL-positive staining (data not shown in this table) polar bodies showed FITC positive at 24-48 h (3 7%, n = 27) and 72 h (100%, n = 22).

H2O2-Induced cell death In mouse zygotes.

Treatment . Hours after treatment . % Dead a (no. examined) . % TUNEL-positive b (no. examined) .
Control 5 0 (50) 0 (30)
H2O2 (1 mM) 5-24 96 (67) 89 (3 7)
H2O2 (200 μM) c 24 0 (88) 0 (33)
48 31 (83) 0 (24)
72 88 (48) 46 (22)
Treatment . Hours after treatment . % Dead a (no. examined) . % TUNEL-positive b (no. examined) .
Control 5 0 (50) 0 (30)
H2O2 (1 mM) 5-24 96 (67) 89 (3 7)
H2O2 (200 μM) c 24 0 (88) 0 (33)
48 31 (83) 0 (24)
72 88 (48) 46 (22)

Live and dead stain Includes both PI and Hoechst stain, and Live and Dead Kit pooled data from at least 4 replicates.

Pooled data from 3 replicates.

Prior to 24 h after treatment, all zygotes were PI negative and did not exhibitTUNEL-positive staining (data not shown in this table) polar bodies showed FITC positive at 24-48 h (3 7%, n = 27) and 72 h (100%, n = 22).

Zygotes at 5 h after treatment with 1 mM H2O2 for 1.5 h displayed cell shrinkage (A) and membrane permeability to PI (B). PN, Pronucleus PB, polar body

Zygotes at 5 h after treatment with 1 mM H2O2 for 1.5 h displayed cell shrinkage (A) and membrane permeability to PI (B). PN, Pronucleus PB, polar body

Cytochrome c Release and Caspase Activation

We further sought to determine whether cell death of zygotes induced by mild and intense oxidative stress differed in critical biochemical hallmarks, including cytochrome c release and caspase activation. Experiments were replicated three times, with at least 50 embryos observed in each treatment. H2O2 treatment of 200 μM for 15 min or 1 mM for 1.5 h induced different dynamics of cytochrome c release and caspase activation. Immunostaining showed that normal zygotes displayed reticulate and punctate staining for cytochrome c ( Fig. 5B), coincident with localization of mitochondria ([ 45, 46], unpublished results). Zygotes treated with 1 mM H2O2 for 1.5 h almost invariably exhibited a diffuse distribution of cytochrome c staining, indicative of its release from mitochondria, from 1, 2, 4, and 6 h after treatment until the end of the observation period at 24 h ( Fig. 5A). Treatment with 200 μM H2O2 for 15 min did not induce cytochrome c release until 72 h after treatment, when clumps of mitochondria and some degree of homogenous cytochrome c distribution appeared in the cytoplasm. Prior to 48 h, there were no detectable changes in cytochrome c localization, although some clumping of mitochondria was noted by JC-1 staining and by ultrastructural observation, as shown below.

Fluorescence micrograph showing homogenous distribution of cytochrome c staining, indicating cytochrome c release in zygotes treated with 1 mM H2O2 for 1.5 h (A), and punctuate localization of cytochrome c in mitochondria in control zygotes (B)

Fluorescence micrograph showing homogenous distribution of cytochrome c staining, indicating cytochrome c release in zygotes treated with 1 mM H2O2 for 1.5 h (A), and punctuate localization of cytochrome c in mitochondria in control zygotes (B)

Similarly, 200 μM H2O2 did not induce caspase activation in zygotes within 48 h after treatment. However, 1 mM H2O2 triggered caspase activation as early as 3 h, and active caspase was detected over 24 h. In control, untreated zygotes, low caspase activity was characterized by light yellow-brownish staining, shown in a homogeneous gray appearance ( Fig. 6A). The brown or dark brown stain of cytoplasm (early stage) or pronuclei (late stage) indicated active caspase after apoptotic treatment, shown in black in Figure 6, B and C. Similarly, active caspase in the cytoplasm and later in the nuclei was detected in apoptotic oocytes by fluorescence analysis [ 30]. Treatment with 1 mM H2O2 also has been demonstrated to induce activation of caspase 3-like protease in PC 12 cells [ 41]. Figure 6D shows active caspase stain in blastocysts as a positive control. Indeed, expression of caspase was detected in blastocysts [ 32, 51]. The active caspase seemed to be correlated with DNA fragmentation in blastocysts.

Caspase activity assay. A) Normal zygotes with only slight background staining, indicating absence of caspase activation. B and C) Brown staining suggestion of active caspase in 1 mM H2O2-treated zygotes very dark brown staining in pronuclei, indicated by two arrows. D) Control staining in a blastocyst (two arrowheads indicate active caspase stain in two cells)

Caspase activity assay. A) Normal zygotes with only slight background staining, indicating absence of caspase activation. B and C) Brown staining suggestion of active caspase in 1 mM H2O2-treated zygotes very dark brown staining in pronuclei, indicated by two arrows. D) Control staining in a blastocyst (two arrowheads indicate active caspase stain in two cells)

Changes in MMP and Distribution of Active Mitochondria

Mild oxidative stress-induced zygotic death appeared more interesting because the prolonged cell cycle arrest mimics cell death of senescent human eggs and because aging is associated with mild oxidation, rather than acute intense stress. We sought to determine whether MMP, distribution, and structure also were affected by mild H2O2 treatment, as has been reported in PCD in many somatic cell types. Changes in MMP, assessed by the shift in fluorescence emission and intensity of the dye JC-1, were compared between control untreated zygotes and zygotes treated with 200 μM H2O2 1, 2, 3, 4, and 6 h after treatment. In control, normal zygotes preloaded with JC-1, mitochondrial populations with high energy were distributed evenly throughout the cytoplasm, appearing as red fluorescence ( Fig. 7, A and B). Living zygotes, like other cells, exhibit both depolarized and hyperpolarized mitochondria [ 13, 48]. After exposure to 200 μM H2O2 for 15 min, the MMP depolarized rapidly, as shown by the dominant green fluorescence in the intermediate region of the cytoplasm, as well as disappearance of red fluorescence and appearance of orange aggregates around cortical regions. Beginning at 2 h after treatment, the pixel ratio intensity, which reflects the MMP, was lower in the intermediate region of H2O2-treated embryos than in that of control embryos ( Fig. 7C). Perinuclear distribution of active mitochondria was observed in control zygotes, but not in H2O2-treated zygotes ( Fig. 8).

Confocal microscopy imaging of mitochondria in mouse zygotes stained with JC-1. A) Channel 1 with red (hyperpolarized, J aggregates), channel 2 with green (monomer form of JC-1), and merged fluorescence (for ratio image analysis) in control cultured zygotes and 200 μM H2O2-treated zygotes at 4 h. B) Higher magnification in the central cytoplasm of zygotes. PN, Pronucleus. C) The ratio imaging analysis collected from the confocal images. The average of relative MMP from control zygotes at each time point was set at 100%, and the MMP in treated zygotes were expressed relative to control for that time point. MMP in zygotes declined from 2 h after treatment of 200 μM H2O2 for 15 min and continued to drop over the subsequent hours. Data are presented as means ± SD in three replicates

Confocal microscopy imaging of mitochondria in mouse zygotes stained with JC-1. A) Channel 1 with red (hyperpolarized, J aggregates), channel 2 with green (monomer form of JC-1), and merged fluorescence (for ratio image analysis) in control cultured zygotes and 200 μM H2O2-treated zygotes at 4 h. B) Higher magnification in the central cytoplasm of zygotes. PN, Pronucleus. C) The ratio imaging analysis collected from the confocal images. The average of relative MMP from control zygotes at each time point was set at 100%, and the MMP in treated zygotes were expressed relative to control for that time point. MMP in zygotes declined from 2 h after treatment of 200 μM H2O2 for 15 min and continued to drop over the subsequent hours. Data are presented as means ± SD in three replicates

MitoTracker staining of active mitochondria in zygotes. Peripronuclear distribution of mitochondria was seen (arrow) in control zygotes but absent (arrowhead) around the pronuclei (PN) in zygotes treated with 200 μM H2O2. Under differential interference contrast imaging, the pronuclei could be seen intact in both group zygotes. Different embryos were visualized under differential interference contrast and fluorescence

MitoTracker staining of active mitochondria in zygotes. Peripronuclear distribution of mitochondria was seen (arrow) in control zygotes but absent (arrowhead) around the pronuclei (PN) in zygotes treated with 200 μM H2O2. Under differential interference contrast imaging, the pronuclei could be seen intact in both group zygotes. Different embryos were visualized under differential interference contrast and fluorescence

Ultrastructural Observation of Mitochondria

In untreated, control zygotes ( Fig. 9), the sphere-shaped, vacuolated, immature mitochondria exhibited electron-dense matrices without obvious cristae. Mitochondria were scattered throughout the intermediate region of the cytoplasm ( Fig. 9, upper panels). In zygotes treated with 200 μM H2O2, alterations of mitochondrial structure, including disruption of the matrix, were noted at 2 h. By 4 h after treatment, further loss of matrix and increased vacuole size were found ( Fig. 9, B and D). It appeared that the membrane was damaged in some mitochondria. Furthermore, mitochondria aggregated within the cytoplasm ( Fig. 9, upper panel). We did not see obvious structural changes in other organelles, including nuclear envelope and nucleoli.

Electron micrographs of mitochondrial ultrastructure of mouse zygotes treated with 200 μM H2O2. Top: Mitochondrial homogenous distribution in the intermediate region of control zygotes and aggregation of mitochondria in the cytoplasm in H2O2-treated zygotes. ×4000. A, C) Control zygotes B, D) H2O2-treated zygotes showing alteration of mitochondria ultrastructure in matrix or membrane. ×34 000

Electron micrographs of mitochondrial ultrastructure of mouse zygotes treated with 200 μM H2O2. Top: Mitochondrial homogenous distribution in the intermediate region of control zygotes and aggregation of mitochondria in the cytoplasm in H2O2-treated zygotes. ×4000. A, C) Control zygotes B, D) H2O2-treated zygotes showing alteration of mitochondria ultrastructure in matrix or membrane. ×34 000


Mitochondrial membrane potential (MMP), as a key indicator of mitochondrial function, can reflect the cellular health status. The dysfunction of MMP, even the subtle unusual changes, can greatly affect the intracellular bioactivities, causing various diseases, such as keratitis, diabetes, Alzheimer’s disease and even cancer. Thus, detecting the variation of MMP has great significance for biological research and medical diagnosis. Due to the advantages of real-time and in-situ monitoring, a variety of organic fluorescent probes have been developed in recent years for the detection of MMP. However, this interesting and frontier topic has not been reviewed so far. In this review, we will focus on several kinds of recent organic fluorescent probes that have provided insights into MMP detection, including design concepts, responding mechanisms and applications of the representative examples. In addition, there are still some shortcomings and limitations of existing fluorescent probes on MMP detection, such as susceptible to interference, unquantifiable detection, and lack of clinical application. This critical review may promote the development of more robust MMP fluorescent probes, providing more powerful tools for researching basic biology to improve cancer diagnoses and treatments in clinics in the future.

The recent developments of organic fluorescence probes for detecting mitochondrial membrane potential (MMP) have been reviewed for the first time.


Antioxidants in mitochondria

Chemicals present in some fruits and vegetables have been shown to have antioxidant activity. This means that, in laboratory tests, they can neutralise free radicals. It was thought that consuming these foods, or extracts made from them, would help the body to remove damaging free radicals.

Recent research suggests that antioxidants work differently in the body than in the laboratory. It is now thought that some antioxidants, in particular, a class of plant chemicals known as polyphenols, have a direct effect on the mitochondria. It appears that they stimulate the mitochondria to become more efficient in generating energy from food, so they generate fewer free radicals and neutralise them more quickly. It is as if the functioning of the mitochondria is being ‘tuned up’ by these polyphenols – an effect similar to that induced in the mitochondria by exercise.


CONCLUSION

As outlined in this review, numerous mitochondrial regulatory mechanisms from differential gene networks to enzymatic controls feature prominently in facilitating MRD and allowing organisms to survive extreme environmental stresses. Indeed, the central metabolic themes and unique adaptations highlighted, as well as the novel questions discussed represent relevant future directions that will better our understanding of the molecular underpinnings of extreme mitochondrial adaptations.


Conclusions and Perspectives

We have introduced the types and regulation mechanisms of pyroptosis briefly and discussed the significant effect of mitochondria on apoptosis in this review. In addition to the discussion of the mechanism between the well-known cell death type apoptosis and mitochondria, the MOMP-mediated apoptotic cell death in different signaling pathways was also be emphasized. According to recent findings, the association between MOMP and inflammasome-mediated pyroptosis was further highlighted, and the interplay between pyroptosis and apoptosis was also revealed. Although mitochondria are involved in a variety of regulatory cell death types, the molecular mechanisms involved are not completely exacted. Moreover, there are actually therapeutic drugs or molecules that target the mitochondria to regulate the pathological processes that involved mitochondria. Previous studie have ever reported that the permeability transition pore complex (PTPC), a multi-protein complex, is participated in the metabolism of mitochondrial stability and also in mitochondria-related intrinsic apoptotic pathways (Deniaud et al., 2006). This targeted intervention, which integrates multiple death signals, may be a promising therapeutic strategy for clinical application. Survivin, a member of the IAP5 gene family, has also been shown to act as a regulatory factor for mitochondrial apoptosis and to inhibit mitochondrial apoptosis by using adenovirus transduction technology in both animal and cell studies (Blanc-Brude et al., 2003). In addition, one homology domain of BCL-2 homology regions (BH3) Peptidomimetics can inhibit apoptosis and thus intervene in the progression of certain related diseases, although the development of targeted interventions is still limited (Nemec and Khaled, 2008). In summary, the targeted regulation of mitochondria and their related pathological processes has gradually aroused great interest. While further research and exploration are needed, this does not prevent the targeting of mitochondria as a new promising strategy to regulate cell death to achieve disease control or treatment of purposes.