What does this research mean for the field?

Continuous release of heparan sulfate from glypican-1 moderates alpha-synuclein aggregation and supports the differentiation of neural progenitor cells into dopaminergic neurons. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

To investigate the functional interplay between amyloid precursor protein, glypican-1 processing, and α-synuclein aggregation in undifferentiated and differentiated human neural progenitor cells.

February 13, 2023GlycobiologyOpen Access

Interplay between APP and glypican-1 processing and α-synuclein aggregation in undifferentiated and differentiated human neural progenitor cells

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Authors

FCFang ChengSun Yat-sen University LFLars‐Âke FranssonLund University KMKatrin ManiLund University

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Implication

In vitro study demonstrates that APP and glypican-1 processing modulates alpha-synuclein aggregation in neural progenitor cells, indicating a protective mechanism in dopaminergic differentiation.

Key Points

To investigate the functional interplay between amyloid precursor protein, glypican-1 processing, and α-synuclein aggregation in undifferentiated and differentiated human neural progenitor cells.
Modulated APP and GPC1 processing in human neural progenitor cells using β-secretase inhibition, nitric oxide deprivation, interleukin-6, and ascorbate.
Evaluated APP degradation fragments, heparan sulfate release, tyrosine hydroxylase expression, and filamentous α-synuclein aggregates using immunofluorescence microscopy and slot immunoblotting.
Interleukin-6 stimulated APP and GPC1 processing alongside filamentous α-synuclein formation, which was decreased by β-secretase inhibition or nitric oxide deprivation.
Inhibition of β-secretase markedly disrupted ascorbate-dependent differentiation of neural progenitors into tyrosine hydroxylase-positive neurons.
Interleukin-6 induced coclustering of APP degradation fragments, tyrosine hydroxylase, heparan sulfate, and filamentous α-synuclein, which was reversed by ascorbate-stimulated heparan sulfate release.

Cite This Study

Cheng et al. (2023) studied this question.

synapsesocial.com/papers/6aaa5d69b6ecf18e3783150a https://doi.org/10.1093/glycob/cwad013

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Implication

In vitro study demonstrates that APP and glypican-1 processing modulates alpha-synuclein aggregation in neural progenitor cells, indicating a protective mechanism in dopaminergic differentiation.

Interplay between APP and glypican-1 processing and α-synuclein aggregation in undifferentiated and differentiated human neural progenitor cells

Discussion

Member takes

Implication

Key Points

Cite This Study

Interplay between APP and glypican-1 processing and α-synuclein aggregation in undifferentiated and differentiated human neural progenitor cells

Discussion

Member takes

Implication

Key Points

Cite This Study

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