Abstract:
:DJ-1 plays roles in transcriptional regulation and anti-oxidative stress, and loss of its function is thought to result in the onset of Parkinson's disease. DJ-1 has a protease-like structure and transthyretin (TTR), a protein causing familial amyloidotic polyneuropathy (FAP), was identified as a substrate for DJ-1 protease in this study. Both TTR and DJ-1 were secreted into the culture medium under normal conditions, and secreted TTR was not aggregated. Under oxidative conditions, TTR but not DJ-1 was secreted into the culture medium, resulting in aggregation. Mirror images of both the expression patterns and solubility of DJ-1 and TTR were observed in tissues of FAP patients, and an unoxidized form of DJ-1, an inactive form, was secreted into the serum of FAP patients. These results suggest that oxidative stress to cells abrogates secretion of DJ-1 and that secreted DJ-1 degrades aggregated TTR to protect against the onset of FAP.
journal_name
Int J Mol Medjournal_title
International journal of molecular medicineauthors
Koide-Yoshida S,Niki T,Ueda M,Himeno S,Taira T,Iguchi-Ariga SM,Ando Y,Ariga Hsubject
Has Abstractpub_date
2007-06-01 00:00:00pages
885-93issue
6eissn
1107-3756issn
1791-244Xjournal_volume
19pub_type
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