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Related Concept Videos

Amyloid Fibrils03:03

Amyloid 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 Fibrils03:03

Amyloid 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...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer 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...
Cardiomyopathy IV: Restrictive Cardiomyopathy01:29

Cardiomyopathy IV: Restrictive Cardiomyopathy

Restrictive cardiomyopathy (RCM) is a rare heart muscle disease characterized by impaired ventricular filling due to stiffened ventricular walls, leading to significant diastolic dysfunction.EtiologyRestrictive cardiomyopathy can arise from both inherited and acquired diseases, many of which are systemic. It is categorized into four main types: infiltrative, storage, non-infiltrative, and endomyocardial diseases.Infiltrative diseases, such as amyloidosis, lead to RCM by depositing amyloid...
Alzheimer's Disease: Overview01:26

Alzheimer's Disease: Overview

Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ and tau...
Alzheimer Disease l: Introduction01:29

Alzheimer Disease l: Introduction

Alzheimer disease is a chronic, progressive, and irreversible neurodegenerative disorder and the most common cause of dementia in older adults. It leads to gradual neuronal loss, causing cognitive decline, behavioral changes, and loss of functional independence.Risk Factors and EtiologyThe disease is multifactorial. Age is the strongest risk factor, with prevalence doubling every 5 years after age 65. Genetic factors include mutations in genes such as APP, PSEN1, and PSEN2, which are associated...

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Updated: May 16, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Systemic AA amyloidosis.

Jennifer H Pinney1, Helen J Lachmann

  • 1National Amyloidosis Centre and Centre for Nephrology, Division of Medicine, UCL Medical School, Rowland Hill Street, NW3 2PF, London, UK, j.pinney@ucl.ac.uk.

Sub-Cellular Biochemistry
|December 11, 2012
PubMed
Summary
This summary is machine-generated.

Systemic AA amyloidosis, a complication of inflammatory diseases, involves amyloid deposits from serum amyloid A protein. Effective management of the underlying inflammation can lead to regression of amyloid deposits and improved renal function.

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Last Updated: May 16, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
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Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
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Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis
06:33

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis

Published on: June 9, 2018

Area of Science:

  • Nephrology
  • Rheumatology
  • Internal Medicine

Background:

  • Systemic AA amyloidosis is a rare but serious complication of chronic inflammatory disorders.
  • Amyloid fibrils originate from serum amyloid A (SAA) protein, an acute-phase reactant synthesized by the liver.
  • Renal involvement is the most common clinical manifestation, often leading to proteinuria and progressive decline in kidney function, frequently culminating in end-stage renal failure.

Purpose of the Study:

  • To highlight the significance of monitoring serum amyloid A (SAA) protein levels in managing systemic AA amyloidosis.
  • To emphasize the link between SAA protein levels, patient survival, and renal outcomes.
  • To demonstrate the potential for amyloid deposit regression and renal function improvement with effective disease suppression.

Main Methods:

  • Clinical observation and monitoring of patients with systemic AA amyloidosis.
  • Assessment of serum amyloid A (SAA) protein levels as a biomarker.
  • Evaluation of renal function and clinical outcomes in relation to SAA suppression and treatment of underlying inflammatory conditions.

Main Results:

  • Serum amyloid A (SAA) protein level is a critical predictor of patient survival and renal prognosis.
  • Adequate suppression of SAA protein levels through management of the underlying inflammatory disease is associated with positive outcomes.
  • Regression of amyloid deposits and stabilization or improvement of renal function can be achieved in patients with effectively controlled SAA levels.

Conclusions:

  • Effective management of the underlying inflammatory condition is paramount in treating systemic AA amyloidosis.
  • Monitoring serum amyloid A (SAA) protein levels is vital for assessing treatment efficacy and predicting patient outcomes.
  • Targeting SAA protein reduction offers a therapeutic strategy for stabilizing or improving renal function and enhancing survival in systemic AA amyloidosis.