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Related Concept Videos

Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
Radical Autoxidation01:20

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...
Peroxisomes and Mitochondria01:30

Peroxisomes and Mitochondria

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.
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Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide02:44

Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

Alkenes are converted to 1,2-diols or glycols through a process called dihydroxylation. It involves the addition of two hydroxyl groups across the double bond with two different stereochemical approaches, namely anti and syn. Dihydroxylation using osmium tetroxide progresses with syn stereochemistry.

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Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
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Asbestos surface provides a niche for oxidative modification.

Hirotaka Nagai1, Toshikazu Ishihara, Wen-Hua Lee

  • 1Department of Pathology and Biological Responses, Nagoya University Graduate School of Medicine, Nagoya, Japan.

Cancer Science
|September 8, 2011
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Summary

Asbestos fibers adsorb DNA and proteins, creating a site for iron-catalyzed oxidative damage. This mechanism contributes to genetic alterations and cancer risk from asbestos exposure.

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Area of Science:

  • Environmental Health Sciences
  • Toxicology
  • Molecular Biology

Background:

  • Asbestos is a known carcinogen linked to mesothelioma and lung cancer.
  • The exact mechanisms of asbestos-induced carcinogenesis are not fully understood.
  • Asbestos's surface properties facilitate biomolecule adsorption, contributing to toxicity.

Purpose of the Study:

  • To systematically identify proteins adsorbed by asbestos fibers.
  • To investigate the role of asbestos-bound hemoglobin in oxidative DNA damage.
  • To propose a novel mechanism for asbestos-induced genetic alterations.

Main Methods:

  • Matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) for protein identification.
  • Analysis of protein scission and oxidative modifications on different asbestos types.
  • Assessment of hemoglobin's catalytic activity in DNA damage.

Main Results:

  • Proteins adsorbed by asbestos include chromatin/RNA-binding proteins, ribosomal proteins, and histones.
  • Iron-rich asbestos types (crocidolite, amosite) induced more protein damage than chrysotile.
  • Chrysotile-bound hemoglobin catalyzed oxidative DNA damage, forming 8-hydroxy-2'-deoxyguanosine.

Conclusions:

  • Asbestos adsorbs DNA and proteins, creating a pro-oxidative environment via catalytic iron.
  • Iron plays a crucial role in the carcinogenicity of asbestos, particularly chrysotile.
  • A novel mechanism involving asbestos-induced genetic alterations via oxidative damage is proposed.