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...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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...
Myasthenia Gravis ll: Pathophysiology01:22

Myasthenia Gravis ll: Pathophysiology

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...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

You might also read

Related Articles

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

Sort by
Same author

Exploration of Arrhythmia Burden in Cardiac Amyloidosis Using Implantable Loop Recorders: The EXCALIBUR Study.

Journal of the American College of Cardiology·2026
Same author

Sustained innovation in ATTR-CM - Twenty years of innovation in transthyretin amyloidosis.

European journal of internal medicine·2026
Same author

Limited Contribution of Fibrosis to Myocardial Interstitial Expansion in End-Stage Cardiac Amyloidosis: Insights From Explanted Whole Hearts.

Journal of the American College of Cardiology·2026
Same author

Biochemical triple testing to exclude monoclonal gammopathy for non-biopsy diagnosis of transthyretin amyloid cardiomyopathy.

European journal of heart failure·2026
Same author

Monoclonal gammopathy exclusion in transthyretin amyloid cardiomyopathy: iStopMM estimated glomerular filtration rate-adjusted serum-free light chain ratio cut-offs.

European heart journal·2026
Same author

Atrial Mechanical Contraction Predicts Cerebrovascular Risk in Patients With Transthyretin Amyloid Cardiomyopathy and Sinus Rhythm.

Journal of the American College of Cardiology·2026
Same journal

Limitations of spectrophotometry in the analysis of cerebrospinal fluid bilirubin.

Annals of clinical biochemistry·2026
Same journal

Commentary on the impact of lithium heparin vacutainer tubes on daily cerebrospinal fluid analysis.

Annals of clinical biochemistry·2026
Same journal

Routine laboratory triage for NT-proBNP elevation may reflect cardiorenal frailty as much as heart failure specificity.

Annals of clinical biochemistry·2026
Same journal

From interpretable NT-proBNP prediction to equitable laboratory stewardship.

Annals of clinical biochemistry·2026
Same journal

Serum Sclerostin Levels in Children with Osteogenesis Imperfecta.

Annals of clinical biochemistry·2026
Same journal

Population-Specific HOMA-IR Reference Ranges in Iraq: Defining Insulin Sensitivity in a Middle Eastern Cohort.

Annals of clinical biochemistry·2026
See all related articles

Related Experiment Video

Updated: May 24, 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

Amyloidosis.

Jennifer H Pinney1, Philip N Hawkins

  • 1UCL Centre for Nephrology, UCL Medical School, Royal Free Hampstead NHS Trust, Rowland Hill Street, London NW3 2PF, UK. j.pinney@ucl.ac.uk

Annals of Clinical Biochemistry
|March 10, 2012
PubMed
Summary
This summary is machine-generated.

Amyloidosis involves protein deposits causing organ damage. Current treatments reduce precursor proteins and offer supportive care, improving survival, with new therapies in development.

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 24, 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:

  • Biochemistry
  • Pathology
  • Medicine

Background:

  • Amyloid refers to extracellular protein deposits in an insoluble fibrillar form.
  • Amyloidosis encompasses clinical syndromes resulting from amyloid deposit-induced tissue and organ damage.
  • The clinical impact of amyloidosis ranges from asymptomatic to rapidly fatal systemic forms.

Purpose of the Study:

  • To provide an overview of amyloidosis, its clinical significance, and current/emerging therapeutic strategies.

Main Methods:

  • Literature review of amyloidosis pathogenesis, clinical manifestations, and treatment modalities.
  • Analysis of current therapeutic approaches including precursor protein reduction and supportive care.
  • Examination of novel therapeutic agents in development, such as RNA interference, protein stabilizers, and monoclonal antibodies.

Main Results:

  • Current therapies focus on reducing amyloid precursor protein supply and supportive care, significantly improving survival.
  • Chemotherapy and anti-inflammatory treatments for AL and AA amyloidosis are guided by monitoring specific circulating precursor proteins.
  • Organ transplantation can enhance quality of life and prognosis for certain hereditary systemic amyloidosis forms.

Conclusions:

  • Amyloidosis presents a spectrum of clinical severity, necessitating tailored treatment strategies.
  • Established therapies have improved patient outcomes, with promising new treatments under investigation.
  • Ongoing research into novel agents targeting fibril formation and deposition holds potential for future amyloidosis management.