Therapeutic protein degradation and relationship between p62 and ubiquilin 2, new proteins causative for neurodegenerative diseases

2015 Fiscal Year Final Research Report

• Project/Area Number: 25461297
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Neurology
• Research Institution: Kinki University
• Principal Investigator: HIRANO Makito 近畿大学, 医学部附属病院, 准教授 (50347548)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: p62

Outline of Final Research Achievements

This study was conducted to clarify ubiquilin 2, a novel amyotrophic lateral sclerosis (ALS)-related protein that the research manager helped to identify, and p62 of which mutations in the first Japanese patients were found by the manager. We used pluripotent stem (iPS) cells of patients with ALS and controls. We found neurons derived from iPS cells of a patient with a p62 mutation had aggregations of p62, a pathological hallmark of ALS. However, the aggregates were not positive for ubiquilin 2 or valosin-containing protein (VCP). Control neurons were negative for p62. Cells of a p62-negative patient had mild aggregations. Treatment of an autophagy-inducer and an antioxidant reduced aggregation.

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