Related Experiment Video
Updated: Aug 4, 2026
10:33
A Caenorhabditis elegans Model System for Amylopathy Study
Published on: May 17, 2013
The changing concepts of amyloid
1Department of Pathology, Loyola University Medical Center, Maywood, Ill 60153, USA. mpicken@lumc.edu
Archives of Pathology & Laboratory Medicine
|January 11, 2001
Summary
Amyloidosis research has evolved over 75 years, revealing it as a family of diseases caused by abnormal protein folding. Current understanding encompasses classification, syndromes, and diagnosis of these complex conditions.
Area of Science:
- Pathology
- Biochemistry
- Genetics
Background:
- The concept of amyloidosis has evolved since Virchow's initial description over a century ago.
- Early experimental induction of amyloidosis in mice by Richard Jaffé marked a significant milestone.
- Advancements in techniques like biochemical analysis, electron microscopy, and molecular genetics have expanded understanding.
Discussion:
- Amyloidosis is now recognized as a diverse group of diseases, including sporadic, familial, inherited, degenerative, and infectious forms.
- A common characteristic of all amyloidoses is the abnormal folding and subsequent deposition of proteins.
- This article provides a synopsis of current knowledge on amyloidosis.
Key Insights:
- Amyloidogenesis involves abnormal protein folding and deposition.
- Amyloidoses represent a spectrum of disease processes.
- Modern techniques have been crucial in unraveling the complexities of amyloidosis.
Outlook:
- This review covers current terminology and classification of amyloidosis.
- It details major clinical syndromes associated with protein misfolding disorders.
- Diagnostic approaches for amyloidosis are also discussed.
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...
01:26Type I Diabetes II: Pathophysiology
Type 1 diabetes mellitus arises from an immune-mediated destruction of pancreatic β-cells, resulting in an absolute deficiency of insulin. This process develops in genetically susceptible individuals when autoimmunity, environmental exposures, and immunologic dysregulation converge to trigger a targeted attack on the insulin-producing cells of the pancreas. The β-cells are located within the islets of Langerhans and are essential for regulating blood glucose by facilitating cellular uptake of...
01:19Type I Diabetes III: Clinical Manifestations
Type 1 diabetes mellitus typically presents with rapid-onset symptoms due to the body’s inability to utilize glucose in the absence of insulin. Since insulin is required for glucose uptake into cells, its deficiency leads to hyperglycemia and cellular energy deprivation, resulting in characteristic clinical features.Polyuria and PolydipsiaOne of the earliest, most prominent symptoms is polyuria (excessive urination). When blood glucose concentrations rise above the renal threshold, the kidneys...
01:22Diabetic Ketoacidosis ll: Pathophysiology
Diabetic ketoacidosis (DKA) is a metabolic emergency characterized by hyperglycemia, ketonemia, and metabolic acidosis. It results from severe insulin deficiency and an excess of counterregulatory hormones, leading to uncontrolled lipolysis, ketogenesis, and widespread electrolyte and fluid disturbances.Pathophysiology The central event in DKA is a profound loss of insulin action. Without insulin, glucose uptake in insulin-dependent tissues is impaired, while hepatic glucose production...
01:23Alzheimer Disease ll: Pathophysiology
Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...