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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid Fibrils03:03

Amyloid Fibrils

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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,...
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Myasthenia Gravis ll: Pathophysiology01:22

Myasthenia Gravis ll: Pathophysiology

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The disease process of myasthenia gravis begins at the neuromuscular junction, where antibodies attack key proteins needed for muscle activation. This immune reaction weakens signal transmission, leading to the characteristic muscle fatigue and weakness that define the condition.Immune-Mediated DamageIn most individuals, antibodies target acetylcholine receptors (AChRs) on the postsynaptic membrane of muscle cells. By blocking acetylcholine binding, these antibodies prevent the nerve signal...
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Alzheimer Disease l: Introduction01:29

Alzheimer Disease l: Introduction

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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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Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

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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...
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Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
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Related Experiment Video

Updated: Apr 27, 2026

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

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[Amyloid light chain amyloidosis].

Kenshi Suzuki1, Toshiko Shimizu

  • 1Department of Hematology, Japanese Red Cross Medical Center.

Brain and Nerve = Shinkei Kenkyu No Shinpo
|July 8, 2014
PubMed
Summary

Primary amyloid light chain (AL) amyloidosis is an aggressive plasma cell disorder. Early diagnosis and treatment are crucial for managing organ damage and improving survival in AL amyloidosis patients.

Area of Science:

  • Hematology
  • Oncology
  • Pathology

Context:

  • Primary amyloid light chain (AL) amyloidosis is a rare, aggressive plasma cell dyscrasia.
  • Monoclonal immunoglobulin light chains deposit in various organs, causing progressive dysfunction and failure.
  • Diagnosis relies on tissue biopsy demonstrating amyloid deposits, often via Congo red staining.

Purpose:

  • To summarize the key aspects of AL amyloidosis, including its pathophysiology, diagnosis, treatment, and prognostic factors.
  • To highlight the challenges in timely diagnosis and treatment initiation.
  • To underscore the importance of early intervention for better patient outcomes.

Summary:

  • AL amyloidosis involves the deposition of amyloid fibrils derived from monoclonal free light chains (FLCs) in multiple organs.

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  • Diagnosis requires tissue biopsy, while treatment options include autologous stem cell transplant for eligible patients or chemotherapy regimens like melphalan-dexamethasone for non-candidates.
  • Poor prognostic factors include elevated N-terminal pro-brain natriuretic peptide, cardiac troponin T, and difference in FLC levels (dFLC).

    • Impact:

    • Timely diagnosis and treatment initiation are critical for preserving organ function and improving survival in AL amyloidosis.
    • Understanding prognostic factors aids in risk stratification and personalized treatment strategies.
    • Advances in treatment, including novel agents, offer improved survival for patients ineligible for stem cell transplant.