Related Experiment Video

Updated: May 27, 2026

Gene-environment Interaction Models to Unmask Susceptibility Mechanisms in Parkinson's Disease
08:09

Gene-environment Interaction Models to Unmask Susceptibility Mechanisms in Parkinson's Disease

Published on: January 7, 2014

The mPTP and its regulatory proteins: final common targets of signalling pathways for protection against necrosis

Tetsuji Miura1, Masaya Tanno

  • 1Second Department of Internal Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan. miura@sapmed.ac.jp

Cardiovascular Research
|November 11, 2011
PubMed

Insights

The mitochondrial permeability transition pore (mPTP) opening causes cell death during ischemia/reperfusion. Inhibiting mPTP opening protects the heart by targeting key regulatory proteins.

Area of Science:

  • Cardiovascular Biology
  • Mitochondrial Medicine
  • Cell Death Mechanisms

Background:

  • The mitochondrial permeability transition pore (mPTP) is a channel crucial for cell survival.
  • mPTP opening leads to mitochondrial dysfunction and myocyte necrosis during ischemia/reperfusion injury.
  • Inhibiting mPTP opening is a therapeutic strategy to limit infarct size.

Purpose of the Study:

  • To review the regulation of mPTP opening.
  • To describe the interaction of mPTP with key regulatory proteins.
  • To highlight the role of these interactions in protection against ischemia/reperfusion injury.

Main Methods:

  • Literature review of studies on mPTP structure, function, and regulation.
  • Analysis of signaling pathways targeting mPTP.
  • Characterization of proteins interacting with mPTP subunits.

Main Results:

  • mPTP opening is a critical determinant of cell death in ischemia/reperfusion.
  • Pro-survival signaling pathways converge on mPTP to inhibit its opening.
  • Four proteins—hexokinase II, GSK-3β, STAT3, and SIRT3—interact with mPTP and mediate protective effects.

Conclusions:

  • Understanding mPTP regulation by interacting proteins offers therapeutic targets for ischemia/reperfusion injury.
  • Targeting these interactions may limit infarct size and preserve cardiac function.
  • Further research into mPTP structure and its regulatory network is warranted.

More Related Videos

Mechanism of Kemeng Fang's Inhibition of Podocyte Apoptosis in Rats with Membranous Nephropathy through the PI3K/AKT Signaling Pathway07:15

Mechanism of Kemeng Fang's Inhibition of Podocyte Apoptosis in Rats with Membranous Nephropathy through the PI3K/AKT Signaling Pathway

Published on: August 23, 2024

Related Concept Videos

PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...