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Related Concept Videos

Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
Bioactivation and Tissue Toxicity01:25

Bioactivation and Tissue Toxicity

Bioactivation is a metabolic process that transforms less reactive substances into highly reactive metabolites, initiating tissue toxicity. This transformation can lead to various toxic effects, including carcinogenesis and teratogenesis. Reactive metabolites are classified into two main types: electrophiles and free radicals.Electrophiles are electron-deficient species and are produced primarily by the enzyme cytochrome P-450 during the metabolism of compounds containing carbon, nitrogen, or...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Nucleotide Excision Repair01:38

Nucleotide Excision Repair

DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
Nucleotide Excision Repair01:08

Nucleotide Excision Repair

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Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications
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Protein damage by reactive electrophiles: targets and consequences.

Daniel C Liebler1

  • 1Department of Biochemistry, Vanderbilt University School of Medicine,, Nashville, Tennessee 37232, USA. daniel.liebler@vanderbilt.edu

Chemical Research in Toxicology
|December 7, 2007
PubMed
Summary

Protein covalent binding, once overlooked, is now a key focus in understanding chemical toxicity. Advanced proteomics techniques allow scientists to identify protein targets of electrophiles and link this damage to health effects.

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Area of Science:

  • Toxicology and Molecular Biology
  • Chemical Carcinogenesis and Drug Toxicity

Background:

  • Protein covalent binding by carcinogens was first described 60 years ago.
  • Initially overshadowed by DNA adducts, protein binding re-emerged as crucial for drug and chemical toxicity in the 1970s.
  • Technological limitations in characterizing protein adducts were overcome by mass spectrometry-based proteomics in the late 1990s.

Purpose of the Study:

  • To review the progress in characterizing protein targets of electrophiles and the consequences of protein damage.
  • To highlight the current technological capabilities for mapping electrophile damage.
  • To emphasize the link between protein adducts and clinically relevant health effects.

Main Methods:

  • Integration of novel affinity chemistries for electrophile probes.
  • Application of shotgun proteomics methods.
  • Utilization of systems modeling tools for analysis.

Main Results:

  • Identification of hundreds of protein targets for electrophiles in mammalian systems.
  • Capability to map damage to critical signaling pathways and metabolic networks.
  • Understanding of damage mechanisms at a systems level.

Conclusions:

  • Sensitive and specific analyses for protein adducts are now available.
  • These analyses can link damage from xenobiotic and endogenous electrophiles to health outcomes.
  • This approach offers a means to connect chemical exposures and disease processes to clinical health effects.