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 Experiment Videos

Animal models for reactive amyloidosis

E Gruys1, F W Snel

  • 1Faculty of Veterinary Medicine, Utrecht University, The Netherlands.

Bailliere'S Clinical Rheumatology
|August 1, 1994
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Arthropathic and amyloidogenic Enterococcus faecalis infections in brown layers: A study on infection routes.

Avian pathology : journal of the W.V.P.A·2016
Same author

Morphologic Study of Homograft Valves before and after Cryopreservation and after Short-Term Implantation in Patients.

Cardiovascular pathology : the official journal of the Society for Cardiovascular Pathology·2015
Same author

Equine acquired multiple acyl-CoA dehydrogenase deficiency (MADD) in 14 horses associated with ingestion of Maple leaves (Acer pseudoplatanus) covered with European tar spot (Rhytisma acerinum).

Molecular genetics and metabolism·2010
Same author

[Subacute ruminal acidosis, claw problems and infertility in (high producing) milk cows].

Tijdschrift voor diergeneeskunde·2009
Same author

[Intestinal problems in turkeys cause by coccidiosis].

Tijdschrift voor diergeneeskunde·2009
Same author

Avian leukosis virus subtype J in ovo -infected specific pathogen free broilers harbour the virus in their feathers and show feather abnormalities.

Avian pathology : journal of the W.V.P.A·2009
Same journal

Regional soft tissue pains: alias myofascial pain?

Bailliere's clinical rheumatology·1999
Same journal

The knee

Bailliere's clinical rheumatology·1999
Same journal

The elbow, forearm, wrist and hand

Bailliere's clinical rheumatology·1999
Same journal

Shoulder disorders: a state-of-the-art review

Bailliere's clinical rheumatology·1999
Same journal

The neck

Bailliere's clinical rheumatology·1999
Same journal

Treatment options for regional musculoskeletal pain: what is the evidence?

Bailliere's clinical rheumatology·1999
See all related articles

Animal experiments reveal that serum amyloid A (SAA) protein crystallizes into fibrils, initiating reactive amyloidosis. Membrane vesicles indicate alterations during this process, with amyloid enhancing factors (AEF) potentially acting as crystallization nidi.

Area of Science:

  • Biochemistry
  • Pathology
  • Immunology

Background:

  • Reactive amyloidosis pathogenesis has been studied for over 70 years using animal models.
  • AA amyloid formation requires elevated serum amyloid A (SAA) precursor protein, an acute phase protein of hepatic origin.
  • Amyloidogenic SAA subtypes are found in mice, hamsters, and mink, but not rats, despite mRNA transcription.

Purpose of the Study:

  • To elucidate the pathogenesis of reactive amyloidosis and the general formation of beta-pleated sheet-rich amyloid fibrils.
  • To investigate the role of serum amyloid A (SAA) protein in amyloid fibril formation.
  • To explore the significance of membrane vesicles and amyloid enhancing factors (AEF) in amyloidogenesis.

Main Methods:

  • Animal experiments, primarily in rodents (mouse, hamster), involving amyloid-inducing injections.

Related Experiment Videos

  • Biochemical analysis of SAA protein, its association with high-density lipoprotein (apoSAA), and its potential crystallization into fibrils.
  • Immunoelectron microscopy to study morphological evidence of membrane alteration and SAA accumulation.
  • Characterization of amyloid enhancing factors (AEF) for their role in accelerating amyloid deposition.

    • Main Results:

    • Evidence suggests SAA crystallizes into fibrils first, with C-terminal end loss occurring post-fibrillogenesis.
    • Basement membrane heparan sulphate proteoglycans (perlecans) play a primary role, while serum amyloid P-component is a secondary phenomenon.
    • Membrane-bound, lipid-rich vesicles are observed, indicating primary membrane alteration during amyloid fibril crystallization, likely due to intramembranous SAA crystallization.
    • Amyloid enhancing factors (AEF) shorten the lag phase for amyloid deposition and possess beta-pleated sheet structure, suggesting a role as crystallization nidi.

    Conclusions:

    • SAA crystallization is a key initial step in reactive amyloidosis pathogenesis.
    • Membrane alterations and vesicle formation are indicators of early amyloid fibril crystallization.
    • Amyloid enhancing factors (AEF) may act as physical crystallization nidi, accelerating fibril formation.