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Amyloid Fibrils

Amyloid Fibrils

Amyloid Fibrils

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,...

Antibody Structure

Antibody Structure

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

Antibody Structure and Classes

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

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Related Experiment Video

Updated: Mar 14, 2026

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

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

Published on: October 20, 2017

Immunoglobulin Light Chain Systemic Amyloidosis.

Angela Dispenzieri^1,2, Giampaolo Merlini³

¹Division of Hematology, Mayo Clinic, Rochester, MN, USA.

Cancer Treatment and Research

|October 4, 2016

Summary

Immunoglobulin light chain amyloidosis (AL) is a rare plasma cell disorder. Early diagnosis and risk-adapted therapy are crucial for effective management and improved patient outcomes.

Keywords:

Biomarkers Cardiac amyloidosis Chemotherapy Immunoglobulin light chain amyloidosis Immunotherapy

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Area of Science:

Hematology
Oncology
Nephrology

Background:

Immunoglobulin light chain amyloidosis (AL) is a rare, complex plasma cell dyscrasia.
It results from misfolded free light chains produced by an indolent plasma cell clone.
Early intervention is critical to prevent irreversible organ damage.

Purpose of the Study:

To outline the cornerstones of AL amyloidosis management.
To highlight the importance of early diagnosis and risk-adapted therapy.
To discuss emerging therapeutic strategies.

Main Methods:

The review emphasizes early diagnosis and accurate typing of AL amyloidosis.
It focuses on risk-adapted chemotherapy guided by cardiac biomarkers.
Supportive care and close follow-up are highlighted.

Main Results:

Effective treatments can alter the disease's natural history if initiated promptly.
Suppression of amyloidogenic light chains remains the primary therapeutic goal.
Cardiac biomarkers guide chemotherapy selection.

Conclusions:

Cornerstones of AL amyloidosis management include early diagnosis, accurate typing, risk-adapted therapy, and supportive care.
Emerging therapies like oral proteasome inhibitors and targeted antibodies offer new hope.
These advancements present unprecedented opportunities to improve patient care and outcomes.