Influence of human amylin on the membrane stability of rat primary hippocampal neurons.

Abstract:

:The two most common aging-related diseases, Alzheimer's disease and type 2 diabetes mellitus, are associated with accumulation of amyloid proteins (β-amyloid and amylin, respectively). This amylin aggregation is reportedly cytotoxic to neurons. We found that aggregation of human amylin (hAmylin) induced neuronal apoptosis without obvious microglial infiltration in vivo. High concentrations of hAmylin irreversibly aggregated on the surface of the neuronal plasma membrane. Long-term incubation with hAmylin induced morphological changes in neurons. Moreover, hAmylin permeabilized the neuronal membrane within 1 min in a manner similar to Triton X-100, allowing impermeable fluorescent antibodies to enter the neurons and stain intracellular antigens. hAmylin also permeabilized the cell membrane of astrocytes, though more slowly. Under scanning electron microscopy, we observed that hAmylin destroyed the integrity of the cell membranes of both neurons and astrocytes. Additionally, it increased intracellular reactive oxygen species generation and reduced the mitochondrial membrane potential. Thus, by aggregating on the surface of neurons, hAmylin impaired the cell membrane integrity, induced reactive oxygen species production, reduced the mitochondrial membrane potential, and ultimately induced neuronal apoptosis.

journal_name

Aging (Albany NY)

journal_title

Aging

authors

Zhang N,Xing Y,Yu Y,Liu C,Jin B,Huo L,Kong D,Yang Z,Zhang X,Zheng R,Jia Z,Kang L,Zhang W

doi

10.18632/aging.103105

subject

Has Abstract

pub_date

2020-05-28 00:00:00

pages

8923-8938

issue

10

issn

1945-4589

pii

103105

journal_volume

12

pub_type

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