Downregulation of Reactive Oxygen Species in Apoptosis

Chul-Ho Jeong1, Sang Hoon Joo2

  • 1College of Pharmacy, Keimyung University, Daegu, Gyeongsan, Korea.

Insights

Phytochemicals can modulate reactive oxygen species (ROS) to prevent cancer or induce apoptosis. This review details compounds like metformin and curcumin that regulate ROS via cellular pathways, aiding cancer therapy.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Reactive oxygen species (ROS) generation by anti-cancer drugs and phytochemicals is linked to apoptosis induction in cancer.
  • ROS downregulation by certain compounds can inhibit carcinogenesis.
  • Modulating ROS is a key mechanism for cancer prevention and therapy.

Purpose of the Study:

  • To review selected chemical compounds and cellular components that modulate ROS during apoptosis.
  • To elucidate the role of ROS modulation by phytochemicals in cancer therapy and prevention.

Main Methods:

  • Literature review of studies on chemical compounds and cellular components involved in ROS modulation.
  • Analysis of the relationship between compounds, cellular components, and ROS in apoptotic cancer cells.

Main Results:

  • Metformin, quercetin, curcumin, and vitamin C were identified as compounds that downregulate ROS.
  • Some of these compounds also induce apoptosis in cancer cells.
  • Key cellular components mediating ROS downregulation include Nrf2 pathway, thioredoxin, catalase, glutathione, HO-1, and uncoupling proteins.

Conclusions:

  • Phytochemicals and compounds like metformin play a crucial role in regulating ROS for cancer apoptosis and prevention.
  • Understanding the interplay between these compounds and cellular antioxidant pathways is vital for developing novel cancer therapies.

Related Concept Videos

Apoptosis01:30

Apoptosis

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...
14.2K
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...
8.3K
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

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...
8.2K
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
13.7K
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...
2.9K
Overview of Cell Death01:30

Overview of Cell Death

Cell death is an essential process where the body gets rid of old or damaged cells. Cell proliferation and death need to be balanced, as an imbalance between the two may lead to cancer or autoimmune diseases.
Cell death was observed in the early 19th century, but there was no experimental evidence to prove it. In 1842, Carl Vogt first discovered cell death in a metamorphic toad; however, it was not termed ‘cell death.’ Scientists discovered different cell death pathways only in the...
9.5K