Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Extranodal natural killer/T-cell lymphoma: From fatal to curable.

CA: a cancer journal for clinicians·2026
Same author

Factor X colocalizes with amyloid light chain deposits in AL amyloidosis: evidence from three patients.

Haematologica·2026
Same author

Daratumumab-Bortezomib-Cyclophosphamide-Dexamethasone in Newly Diagnosed Amyloidosis: ANDROMEDA Final Survival Analysis.

Blood·2026
Same author

Accelerated apolipoprotein A-II senile amyloidosis in a plasminogen activator inhibitor-1 knock-out model.

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis·2026
Same author

Comparison of the biocompatibility profiles of synthetic polysulfone and polyethersulfone dialysis membranes.

Clinical kidney journal·2026
Same author

Health-related quality of life and mental health in autoimmune thrombotic thrombocytopenic purpura patients in the caplacizumab era.

Research and practice in thrombosis and haemostasis·2026

Related Experiment Video

Updated: May 19, 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

Al amyloidosis.

Estelle Desport1, Frank Bridoux, Christophe Sirac

  • 1Service d'Hématologie et de Thérapie Cellulaire, Cedex, France.

Orphanet Journal of Rare Diseases
|August 23, 2012
PubMed
Summary
This summary is machine-generated.

AL amyloidosis is caused by abnormal immunoglobulin light chains. Treatment focuses on the plasma cell clone, with chemotherapy improving outcomes, but organ involvement significantly impacts survival.

More Related Videos

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Related Experiment Videos

Last Updated: May 19, 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

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Area of Science:

  • AL amyloidosis is a systemic disease caused by extracellular deposition of abnormal immunoglobulin light chains (LC).
  • The disease arises from conformational changes in monoclonal LC, leading to misfolding and amyloid fibril formation.
  • It is the most common type of systemic amyloidosis in developed countries.

Background:

  • AL amyloidosis affects approximately 9 in a million inhabitants annually, with a median age of diagnosis around 65.
  • The condition is linked to monoclonal gammopathy or smoldering myeloma, rarely occurring with symptomatic multiple myeloma.
  • While most patients are older, less than 10% are diagnosed before age 50.

Purpose of the Study:

  • To define AL amyloidosis, its epidemiology, clinical presentation, diagnostic methods, differential diagnosis, management, and prognosis.
  • To provide a comprehensive overview of AL amyloidosis for healthcare professionals and researchers.
  • To highlight key factors influencing patient survival and treatment strategies.

Main Methods:

  • Diagnosis involves pathological examination of amyloid deposits using Congo red staining and immunohistochemistry for light chains.
  • Non-invasive biopsies like abdominal fat aspiration are recommended to minimize complication risks.
  • Distinguishing AL amyloidosis from other systemic amyloidoses and monoclonal LC-related diseases is crucial.

Main Results:

  • Renal and cardiac involvement are frequent at diagnosis, with heart disease being the most critical prognostic factor.
  • Chemotherapy targeting the underlying plasma cell clone is the primary treatment, with alkylating agents and dexamethasone showing efficacy.
  • Newer agents are being investigated to improve hematologic response rates.
  • Supportive care for organ failure is essential, with specific management for cardiac amyloidosis (diuretics, not standard heart failure drugs).

Conclusions:

  • Patient survival is primarily determined by the extent of organ involvement, particularly cardiac disease, and the hematologic response to treatment.
  • Effective management requires a multi-faceted approach, including chemotherapy for the underlying clone and supportive care for organ dysfunction.
  • Further research into novel therapeutic agents holds promise for improving outcomes in AL amyloidosis.