Light chain amyloidosis - current findings and future prospects
Elizabeth M Baden1, Laura A Sikkink1, Marina Ramirez-Alvarado1
1Department of Biochemistry and Molecular Biology, College of Medicine, Mayo Clinic, 200 First Street SW, Rochester, MN 55905.
Current Protein & Peptide Science
|June 23, 2009
Summary
Systemic light chain amyloidosis (AL) involves abnormal immunoglobulin light chain (LC) deposition. Research into protein misfolding and fibril formation, including work from the Fink laboratory, aims to improve therapies for this fatal disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Pathology
Background:
- Systemic light chain amyloidosis (AL) is a protein misfolding disease.
- Extracellular deposition of immunoglobulin light chains forms amyloid fibrils.
- Monoclonal plasma cells produce excess pathogenic light chains, leading to instability and misfolding.
Purpose of the Study:
- To review the current state of AL research.
- To highlight recent findings from the Fink laboratory on amyloidogenesis.
- To explore molecular factors in light chain amyloidogenicity and fibril formation.
Main Methods:
- Review of existing literature on AL amyloidosis.
- Analysis of protein misfolding and fibril formation pathways.
- Incorporation of research findings from the Fink laboratory.
Main Results:
- Identified key molecular factors contributing to light chain amyloidogenicity.
- Elucidated mechanisms of amyloid fibril formation, including the role of intermediates.
- Highlighted the impact of somatic mutations on protein stability.
Conclusions:
- Understanding protein pathogenesis is crucial for developing better AL therapies.
- Fink laboratory's research provides significant insights into amyloid fibril formation.
- Improved therapies could enhance patient survival in systemic light chain amyloidosis.
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...
02:57Targeted Cancer Therapies
The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
There are several types of targeted therapies against specific...
There are several types of targeted therapies against specific...