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Role of perivascular cells and myocytes in vascular amyloidosis

H M Wisniewski1, J Wegiel, A W Vorbrodt

  • 1New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314, USA.

Annals of the New York Academy of Sciences
|May 20, 2000
PubMed

Insights

Alzheimer's disease involves amyloid-beta (A beta) production by brain cells. Different cell types generate A beta, impacting brain vasculature and leading to neuronal damage and hemorrhages.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Pathology

Background:

  • Alzheimer's disease (AD) pathology is characterized by amyloidogenic processing of amyloid-beta precursor protein (APP).
  • Amyloid-beta (A beta) originates from diverse cellular sources within the brain.

Purpose of the Study:

  • To elucidate the cellular origins and pathogenic mechanisms of amyloid-beta (A beta) deposition in the brain.
  • To understand the role of different cell types in the development of Alzheimer's disease (AD) pathology.

Main Methods:

  • Investigated the cellular sources of fibrillar A beta in brain capillaries and parenchyma.
  • Examined the role of smooth muscle cells in A beta deposition in cerebral blood vessels.
  • Analyzed the impact of A beta deposition on vascular integrity and neuronal survival.

Main Results:

  • Perivascular cells (monocyte-macrophage-microglial lineage) produce fibrillar A beta in capillaries, causing endothelial cell death and vascular network reduction.
  • Parenchymal microglial cells generate fibrillar A beta in gray matter parenchyma.
  • Smooth muscle cells in arteries and veins contribute to A beta deposition, leading to smooth muscle cell necrosis and cortical hemorrhages.
  • Isolated smooth muscle cells secrete A beta and accumulate it intracellularly.

Conclusions:

  • Heterogeneous cellular origins of A beta contribute to distinct pathological features in Alzheimer's disease (AD).
  • Vascular A beta deposition by perivascular and smooth muscle cells drives critical pathologies including ischemia and hemorrhage.
  • Amyloidogenic APP processing is influenced by factors like apolipoprotein E, transthyretin, and cytokines.

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