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The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

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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...
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The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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Apoptosis01:30

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Apoptosis is a combination of two Greek words, 'apo' and 'ptosis,' meaning separation and falling off, respectively. Hippocrates used this word to describe gangrene, which was caused due to bandaging of fractured bones. Apoptosis was distinguished from necrosis in 1970 when John Kerr reported observations of morphological changes occurring during apoptosis. During one experiment, he observed that the disruption of blood supply to the liver tissue resulted in a size...
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Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
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Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
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Silencing of BRCA2 to Identify Novel BRCA2-regulated Biological Functions in Cultured Human Cells
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PPARα induces cell apoptosis by destructing Bcl2.

Jiaming Gao1,2, Qian Liu1, Ying Xu2

  • 1Department of Oncology, The Affiliated Wujin People's Hospital, Jiangsu University, Changzhou, Jiangsu Province, China.

Oncotarget
|November 12, 2015
PubMed
Summary

Peroxisome-proliferator-activated receptors alpha (PPARα) acts as an E3 ubiquitin ligase, degrading the Bcl2 protein. This mechanism enhances cancer cell sensitivity to chemotherapy, offering a new therapeutic target.

Keywords:
Bcl2PPARαapoptosisdegradationubiquitination

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Area of Science:

  • Molecular Biology
  • Cancer Research
  • Biochemistry

Background:

  • Peroxisome-proliferator-activated receptors (PPARs) are crucial in regulating cell proliferation and tumorigenesis.
  • The precise molecular mechanisms underlying PPARs' role in cancer are not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanism by which PPARα influences cancer cell proliferation and chemoresistance.
  • To investigate the role of PPARα in regulating Bcl2 protein stability.

Main Methods:

  • Co-immunoprecipitation assays to confirm physical binding between PPARα and Bcl2.
  • Ubiquitination assays to detect K48-linked polyubiquitination of Bcl2 at lysine-22.
  • Cellular experiments involving PPARα overexpression and silencing to assess chemotherapy sensitivity.

Main Results:

  • PPARα directly binds to the BH3 domain of Bcl2.
  • PPARα functions as an E3 ubiquitin ligase, mediating K48-linked polyubiquitination and proteasomal degradation of Bcl2.
  • Overexpression of PPARα increases cancer cell sensitivity to chemotherapy, while silencing PPARα reduces it.

Conclusions:

  • PPARα regulates Bcl2 protein stability through ubiquitination and proteasomal degradation.
  • This novel mechanism contributes to reduced cancer cell chemoresistance.
  • PPARα represents a potential therapeutic target for enhancing cancer treatment efficacy.