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Updated: Jun 22, 2026
10:56
Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
Proteomics in protein misfolding diseases.
Monica Stoppini1, Laura Obici, Francesca Lavatelli
1Department of Biochemistry, University of Pavia, Pavia, Italy.
Clinical Chemistry and Laboratory Medicine
|June 17, 2009
Summary
Proteomics aids in understanding systemic amyloidoses by analyzing protein misfolding and deposition. This approach helps identify disease markers and understand organ dysfunction caused by amyloid fibrils.
Area of Science:
- Biochemistry
- Molecular Biology
- Medical Research
Background:
- Systemic amyloidoses are characterized by widespread amyloid deposition, leading to severe organ dysfunction and tissue damage.
- Understanding the molecular mechanisms of protein misfolding and aggregation is crucial for disease pathogenesis.
Purpose of the Study:
- To review the advancements in proteomics for studying systemic amyloidoses.
- To highlight the utility of proteomics in characterizing amyloidogenic precursors and affected tissues.
- To discuss the diagnostic and research perspectives offered by proteomics in this disease group.
Main Methods:
- Proteomic analysis of circulating amyloidogenic precursors.
- Proteomic analysis of tissues affected by amyloid deposition.
- Characterization of fibril components and protein expression changes.
Main Results:
- Proteomics has proven effective in identifying amyloid fibril components.
- Proteomics enables the characterization of disease-related protein expression alterations.
- The versatility of proteomics facilitates comprehensive analysis of systemic amyloidoses.
Conclusions:
- Proteomics is an invaluable tool for the comprehensive study of systemic amyloidoses.
- Continued development in proteomics offers promising avenues for diagnosis and understanding of these diseases.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:13The 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...
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...
02:18The 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...
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...
01:33Proteomics
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
02:11Proteins: From Genes to Degradation
Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick. Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Transcription is the synthesis of RNA molecules by RNA...