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Alpha synuclein processing by MMP-3 - implications for synucleinopathies.

Alexandra Bluhm¹, Sarah Schrempel¹, Sandra Moceri²

¹Paul Flechsig Institute for Brain Research, University of Leipzig, 04103 Leipzig, Germany.

Behavioural Brain Research

|July 23, 2022

Summary

Pyroglutamate modification of alpha-synuclein (aSyn) is linked to synucleinopathies. Matrix metalloproteinase-3 (MMP-3) and glutaminyl cyclase (QC) enzymes are implicated in generating this toxic pGlu79-aSyn form in mouse models.

Keywords:

Glutaminyl cyclase Matrix metalloproteinase-3 Pyroglutamate modification Substantia nigra Transgenic mouse models α-synuclein

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Alpha-synuclein (aSyn) aggregation is central to synucleinopathies.
A novel pyroglutamate (pGlu) modification at Gln79 of N-truncated aSyn (pGlu79-aSyn) promotes neurotoxicity.
Matrix metalloproteinase-3 (MMP-3) and glutaminyl cyclase (QC) are candidate enzymes for pGlu79-aSyn formation.

Purpose of the Study:

To investigate the expression and co-localization of aSyn, MMP-3, QC, and pGlu79-aSyn in transgenic mouse models of synucleinopathies.
To analyze the age-dependent changes in these proteins in the context of aSyn pathology.

Main Methods:

Triple immunofluorescent labeling and confocal laser scanning microscopy.
Western blot analysis.
Immunohistochemistry in BAC-SNCA and ASO transgenic mouse models.

Main Results:

MMP-3, QC, and pGlu79-aSyn co-localized in brain regions affected by aSyn pathology (hippocampus, substantia nigra).
Regional differences in aSyn, MMP-3, and QC abundance were observed.
Aging ASO mice showed increased QC and pGlu79-aSyn in the substantia nigra.

Conclusions:

Data support a role for MMP-3 and QC in the in vivo generation of pGlu79-aSyn.
This modification is a key event in the pathogenesis of synucleinopathies.