Molecular Association of Glia Maturation Factor with the Autophagic Machinery in Rat Dopaminergic Neurons: a Role for Endoplasmic Reticulum Stress and MAPK Activation

Mol Neurobiol. 2019 Jun;56(6):3865-3881. doi: 10.1007/s12035-018-1340-1. Epub 2018 Sep 14.

Abstract

Parkinson's disease (PD) is one of the several neurodegenerative diseases where accumulation of aggregated proteins like α-synuclein occurs. Dysfunction in autophagy leading to this protein build-up and subsequent dopaminergic neurodegeneration may be one of the causes of PD. The mechanisms that impair autophagy remain poorly understood. 1-Methyl-4-phenylpiridium ion (MPP+) is a neurotoxin that induces experimental PD in vitro. Our studies have shown that glia maturation factor (GMF), a brain-localized inflammatory protein, induces dopaminergic neurodegeneration in PD and that suppression of GMF prevents MPP+-induced loss of dopaminergic neurons. In the present study, we demonstrate a molecular action of GMF on the autophagic machinery resulting in dopaminergic neuronal loss and propose GMF-mediated autophagic dysfunction as one of the contributing factors in PD progression. Using dopaminergic N27 neurons, primary neurons from wild type (WT), and GMF-deficient (GMF-KO) mice, we show that GMF and MPP+ enhanced expression of MAPKs increased the mammalian target of rapamycin (mTOR) activation and endoplasmic reticulum stress markers such as phospho-eukaryotic translation initiation factor 2 alpha kinase 3 (p-PERK) and inositol-requiring enzyme 1α (IRE1α). Further, GMF and MPP+ reduced Beclin 1, focal adhesion kinase (FAK) family-interacting protein of 200 kD (FIP200), and autophagy-related proteins (ATGs) 3, 5, 7, 16L, and 12. The combined results demonstrate that GMF affects autophagy through autophagosome formation with significantly reduced lysosomal-associated membrane protein 1/2, and the number of autophagic acidic vesicles. Using primary neurons, we show that MPP+ treatment leads to differential expression and localization of p62/sequestosome and in GMF-KO neurons, there was a marked increase in p62 staining implying autophagy deficiency with very little co-localization of α-synuclein and p62 as compared with WT neurons. Collectively, this study provides a bidirectional role for GMF in executing dopaminergic neuronal death mediated by autophagy that is relevant to PD.

Keywords: Autophagy dysfunction; Glia maturation factor; Parkinson’s disease; Protein aggregation.

MeSH terms

  • Animals
  • Autophagosomes / drug effects
  • Autophagosomes / metabolism
  • Autophagy* / drug effects
  • Beclin-1 / metabolism
  • Biomarkers / metabolism
  • Cell Nucleus / drug effects
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Dopaminergic Neurons / drug effects
  • Dopaminergic Neurons / enzymology
  • Dopaminergic Neurons / metabolism*
  • Endoplasmic Reticulum Stress*
  • Enzyme Activation / drug effects
  • Glia Maturation Factor / metabolism*
  • Glia Maturation Factor / pharmacology
  • Lysosomes / drug effects
  • Lysosomes / metabolism
  • Mice
  • Mitogen-Activated Protein Kinases / metabolism*
  • Protein Aggregates / drug effects
  • Protein Transport / drug effects
  • Rats
  • Sequestosome-1 Protein / metabolism
  • TOR Serine-Threonine Kinases / metabolism
  • alpha-Synuclein / metabolism

Substances

  • Beclin-1
  • Biomarkers
  • Glia Maturation Factor
  • Protein Aggregates
  • Sequestosome-1 Protein
  • Sqstm1 protein, mouse
  • alpha-Synuclein
  • TOR Serine-Threonine Kinases
  • Mitogen-Activated Protein Kinases