Establish the diagnostic system for amyloidosis using modified proteomic method.

2016 Fiscal Year Final Research Report

• Project/Area Number: 26860372
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Laboratory medicine
• Research Institution: Kumamoto University
• Principal Investigator: Tasaki Masayoshi 熊本大学, 大学院生命科学研究部(保), 助教 (50613402)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: アミロイドーシス / 質量分析 / 診断

Outline of Final Research Achievements

There are 36 kinds of amyloid precursor proteins that make amyloid　fibrils. Amyloidosis is classified as each disease according to type of amyloid precursor protein, and the treatment is different. For this reason, it is extremely important to accurately identify the amyloid precursor protein for typing of amyloidosis. In this study, we developed a new extraction method for amyloid and establish a system that can accurately identify amyloid precursor protein. In addition, we tried to pick up candidates as prognostic markers using mass spectrometry for AL amyloidosis.
It revealed that the analytical method using proteinase K increased the detection rate of amyloid precursor protein. In AL amyloidosis, many type of peptides derived from L chain could be detected by using mass spectrometry. In addition, candidate peptides may become a prognostic marker for AL amyloidosis.

Free Research Field

医歯薬学