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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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Rapid Generation of Amyloid from Native Proteins In vitro
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Serum Amyloid A (SAA) Proteins.

George H Sack1

  • 1Departments of Biological Chemistry and Medicine, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Physiology 615, Baltimore, MD, 21205, USA. gsack@jhmi.edu.

Sub-Cellular Biochemistry
|March 20, 2020
PubMed
Summary
This summary is machine-generated.

Serum Amyloid A (SAA) proteins are vital acute phase reactants involved in host defense and cholesterol transport. Their dysregulation can lead to secondary amyloid disease and organ failure.

Keywords:
APRAcute phase reactionAmyloidosisArthritisAtherosclerosisCytokineHDLInflammationLipoproteinsMetastasisSAASerum amyloid A

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Area of Science:

  • Biochemistry
  • Immunology
  • Molecular Biology

Background:

  • Serum Amyloid A (SAA) proteins are normal blood constituents, synthesized mainly in the liver.
  • SAA fragments can form amyloid fibrils, causing secondary amyloid disease and organ dysfunction.
  • SAA proteins are key acute phase reactants, alongside C-reactive protein (CRP).

Purpose of the Study:

  • To elucidate the biological functions of SAA proteins.
  • To understand SAA's role in host defense and the acute phase response (APR).
  • To investigate SAA's involvement in various physiological and pathological processes.

Main Methods:

  • Analysis of SAA protein structure and conservation.
  • Investigation of SAA's association with high-density lipoproteins (HDL) and cholesterol transport.
  • Exploration of SAA interactions with cellular receptors and downstream effects.

Main Results:

  • SAA proteins are small, well-conserved molecules with a significant role in the APR.
  • SAA proteins are lipophilic and participate in lipid transport.
  • Emerging evidence links SAA to tissue remodeling, inflammation, and various diseases.

Conclusions:

  • SAA proteins are crucial for primordial host defense and the acute phase response.
  • SAA's multifaceted roles extend to lipid metabolism and complex disease pathways.
  • Further research into SAA's molecular mechanisms is warranted to understand its full biological significance.