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Cells for clearing amyloid polypeptide and application thereof

An amyloid polypeptide, cell technology, applied in the field of cell biology and pharmacy, can solve problems such as cell dysfunction

Inactive Publication Date: 2016-03-16
SHANGHAI INST OF BIOLOGICAL SCI CHINESE ACAD OF SCI
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Although its specific mechanism has not been studied clearly, the ApoE-mediated increase of Aβ levels in the brain at least suggests that there is a dysfunction in the clearance of Aβ cells

Method used

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  • Cells for clearing amyloid polypeptide and application thereof
  • Cells for clearing amyloid polypeptide and application thereof
  • Cells for clearing amyloid polypeptide and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0199] Example 1, NG2 cells are activated around amyloid plaques

[0200] The brain tissue sections (brain slices) of 14-month-old APPswe / PS1 transgenic mice (JacksonLab, clone number 004462) and control mice without APPswe / PS1 transgene (C57BL / 6J*C3H / HeJ) were obtained, and the NG2 cells of the cerebral cortex were analyzed. Immunohistochemical staining and plaque thioflavin-S staining. NG2-positive cells were uniformly distributed in the cerebral cortex of control mice, but gathered around amyloid plaques in APPswe / PS1 transgenic mice, as shown in figure 1 A-B are shown.

Embodiment 2

[0201] Example 2, NG2 cells are a new cell type that gathers around amyloid plaques

[0202] Immunohistochemical staining of the cerebral cortex of APPswe / PS1 transgenic mice. Such as figure 2 , Thioflavin-S staining for amyloid plaques, Iba1 for microglia, GFAP for astrocytes, and NeuN for neurons. The results showed that Iba1-positive microglia and GFAP-positive astrocytes gathered around the amyloid plaques, while there were no NeuN-positive neurons at the location of the amyloid plaques.

[0203] Immunohistochemical double labeling was performed on the cerebral cortex of APPswe / PS1 transgenic mice. The cerebral cortex was double-labeled with NG2 and GFAP, NeuN or Iba1. The result is as image 3 , showing that NG2-positive cells did not co-localize with GFAP-positive astrocytes, NeuN-positive neurons and Iba1-positive microglia. The results demonstrated that NG2 cells are a new cell type that aggregates around amyloid plaques, where they are activated.

Embodiment 3

[0204] Example 3, primary NG2 cells and oli-neu cell lines can phagocytize Aβ

[0205] The primary NG2 cells and Oli-neu cells were seeded on slides in a 24-well plate, cultured for 18 hours, and then incubated with 2 μM fluorescently-labeled (HiLyteFluor488-labeled) Aβ for 24 hours. Cell immunofluorescence staining with NG2 antibody was performed after the cells were fixed. The result is as Figure 4 A-B, showing that Aβ can be phagocytosed into the somata of primary NG2 cells and Oli-neu cells.

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Abstract

The invention relates to a cell for removing amyloid polypeptide and a use thereof. The invention first discloses that the NG2 cell can be activated by A beta and phagocytose A beta. The NG2 cell can be used as a pharmaceutical target for researching and screening a drug for activation or promotion of NG2 phagocytosis on A beta. The NG2 cell provides an effective approach for treating neurodegenerative diseases caused by excess A beta in the brain.

Description

technical field [0001] The invention belongs to the fields of cell biology and pharmacy; more specifically, the invention relates to cells for clearing amyloid polypeptides and applications thereof. Background technique [0002] Alzheimer's disease (AD) is the most common form of dementia. There are three major features in neuropathology: amyloid plaques deposited outside cells; neurofibrillary tangles inside cells; and neuronal death in specific brain regions. Amyloid β polypeptide (Aβ) is the main component of amyloid plaques, which is a natural metabolite formed by amyloid precursor protein (APP) through cleavage catalyzed by different endoproteases. There are three proteases involved in the cleavage process of APP, which are called α-secretase, β-secretase and γ-secretase according to the order of discovery of their cleavage sites. The cleavage process of APP can be divided into amyloid pathway and non-amyloid pathway. The main amyloid pathway is that β-secretase firs...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C12Q1/02A61K45/00A61P25/28
Inventor 柯尊记骆嘉李文霞唐义芬范志勤
Owner SHANGHAI INST OF BIOLOGICAL SCI CHINESE ACAD OF SCI
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