Mutant Profilin1 Aggregation in Amyotrophic Lateral Sclerosis: An in Vivo Biochemical Analysis.

ABSTRACT:

Introduction

Profilin1 (PFN1) is a ubiquitously expressed protein known for its function as a regulator of actin polymerization and dynamics. A recent discovery linked mutant PFN1 to Amyotrophic Lateral Sclerosis (ALS), which is a fatal and progressive motor neuron disease. We have also demonstrated that Gly118Val mutation in PFN1 is a cause of ALS, and the formation of aggregates containing mutant PFN1 may be a mechanism for motor neuron death. Hence, we were interested in investigating the aggregation of PFN1 further and searching for co-aggregated proteins in our mouse model overexpressing mutant PFN1.

Methods

We investigated protein aggregation in several tissues of transgenic and notransgenic mice using western blotting. To further understand the neurotoxicity of mutant

SUBMITTER: Nekouei M 

PROVIDER: S-EPMC8672666 | biostudies-literature | 2021 Mar-Apr

REPOSITORIES: biostudies-literature