Study on mechanisms of cutaneous amyloid fibril formating

2015 Fiscal Year Final Research Report

• Project/Area Number: 26860885
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Dermatology
• Research Institution: Nagasaki University
• Principal Investigator: MINE Yoshiko 長崎大学, 病院(医学系), 助教 (90381235)
• Project Period (FY): 2014-04-01 – 2016-03-31
• Keywords: アミロイド / ケラチン / 弾性線維

Outline of Final Research Achievements

Amyloidosis is a group of disease that destroys cells or tissues by accumulating insoluble materials with beta-sheet structure in cells. The precise mechanisms are not fully understood yet. Using cutaneous amyloidosis, we immunohistochemically demonstrated that cytokeratin(CK) 5 was collocated with amyloid fibrils (AF) in the dermis. We succeeded to show that one of synthetic peptides covering c-terminus of CK5 could form AF. Furthermore, we found a member of extracellular matrix (ECM-X) codistributed with AF in the dermis. By in vitro AF assay with ThT, we demonstrated that recombinant ECM-X accelerated F formation of CK5-derived peptide. Taken these, cutaneous AF formation proceeds with a help of special bystander such as ECM-X. The results of this unique points of AF formation may help drug development to amyloidosis in any organs.

Free Research Field

皮膚科学