Abstract
The amyloidoses are a group of protein misfolding diseases in which the precursor protein undergoes a conformational change that triggers the formation of amyloid fibrils in different tissues and organs, causing cell death and organ failure. Amyloidoses can be either localized or systemic. In localized amyloidosis, amyloid deposits form at the site of precursor protein synthesis, whereas in systemic amyloidosis, amyloid deposition occurs distant from the site of precursor protein secretion. We review the type of proteins and cells involved and what is known about the complex pathophysiology of these diseases. We focus on light chain amyloidosis to illustrate how biochemical and biophysical studies have led to a deeper understanding of the pathogenesis of this devastating disease. We also review current cellular, tissue, and animal models and discuss the challenges and opportunities for future studies of the systemic amyloidoses.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 745-774 |
| Number of pages | 30 |
| Journal | Annual Review of Biochemistry |
| Volume | 82 |
| DOIs | |
| State | Published - Jun 2013 |
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Keywords
- Amyloid fibril formation
- Amyloid precursor proteins
- Light chain amyloidosis
- Protein aggregation
- Protein misfolding
- Transthyretin amyloidosis
ASJC Scopus subject areas
- Biochemistry
Cite this
Systemic amyloidoses. / Blancas-Mejía, Luis M.; Ramirez-Alvarado, Marina.
In: Annual Review of Biochemistry, Vol. 82, 06.2013, p. 745-774.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Systemic amyloidoses
AU - Blancas-Mejía, Luis M.
AU - Ramirez-Alvarado, Marina
PY - 2013/6
Y1 - 2013/6
N2 - The amyloidoses are a group of protein misfolding diseases in which the precursor protein undergoes a conformational change that triggers the formation of amyloid fibrils in different tissues and organs, causing cell death and organ failure. Amyloidoses can be either localized or systemic. In localized amyloidosis, amyloid deposits form at the site of precursor protein synthesis, whereas in systemic amyloidosis, amyloid deposition occurs distant from the site of precursor protein secretion. We review the type of proteins and cells involved and what is known about the complex pathophysiology of these diseases. We focus on light chain amyloidosis to illustrate how biochemical and biophysical studies have led to a deeper understanding of the pathogenesis of this devastating disease. We also review current cellular, tissue, and animal models and discuss the challenges and opportunities for future studies of the systemic amyloidoses.
AB - The amyloidoses are a group of protein misfolding diseases in which the precursor protein undergoes a conformational change that triggers the formation of amyloid fibrils in different tissues and organs, causing cell death and organ failure. Amyloidoses can be either localized or systemic. In localized amyloidosis, amyloid deposits form at the site of precursor protein synthesis, whereas in systemic amyloidosis, amyloid deposition occurs distant from the site of precursor protein secretion. We review the type of proteins and cells involved and what is known about the complex pathophysiology of these diseases. We focus on light chain amyloidosis to illustrate how biochemical and biophysical studies have led to a deeper understanding of the pathogenesis of this devastating disease. We also review current cellular, tissue, and animal models and discuss the challenges and opportunities for future studies of the systemic amyloidoses.
KW - Amyloid fibril formation
KW - Amyloid precursor proteins
KW - Light chain amyloidosis
KW - Protein aggregation
KW - Protein misfolding
KW - Transthyretin amyloidosis
UR - http://www.scopus.com/inward/record.url?scp=84878629549&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84878629549&partnerID=8YFLogxK
U2 - 10.1146/annurev-biochem-072611-130030
DO - 10.1146/annurev-biochem-072611-130030
M3 - Article
C2 - 23451869
AN - SCOPUS:84878629549
VL - 82
SP - 745
EP - 774
JO - Annual Review of Biochemistry
JF - Annual Review of Biochemistry
SN - 0066-4154
ER -