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J.Health Sci., 49(4), 267-272, 2003
-Minireview-
Therapeutic Approaches in Prion Disease
Naomi S. Hachiya,a, b Yuji
Sakasegawa,a, b and Kiyotoshi
Kaneko*, a, b
aDepartment of Cortical Function Disorders, National Institute of Neuroscience, National Center of Neurology and Psychiatry,
4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan and
bCore Research for Evolutional Science and Technology (CREST) of
Japan Science and Technology Corporation, 4-1-8 Honcho, Kawaguchi-shi, Saitama 332-0012, Japan
Prion protein (PrP) exists in two different isoforms; a normal cellular isoform
(PrPC) and an abnormal infectious isoform
(PrPSc), the latter is a causative agent of prion disease such as Bovine Spongiform
Encephalopathy (BSE, mad cow disease) and Creutzfeldt-Jakob disease (CJD). Great concern about variant CJD, which
is caused by ingesting BSE-contaminated products, is also emerging and spreading over Japan since the first
BSE-affected cattle was identified in September, 2001. The amino acid sequences of
PrPC and PrPSc are identical, but their conformations are rather different;
PrPC is rich in the non beta-sheet isoform while
PrPSc is rich in the beta-sheet isoform. Our prion research focuses on further understanding such an unprecedented mechanism by
identifying auxiliary factor(s) other than
PrPC and PrPSc. These studies also help us to develop "therapeutics and
prevention methods" for prion disease. Three major trials; genetic manipulation with dominant negative mutant
PrPC gene working against a hypothetical host-specific factor, antibody therapy with anti-PrP antibodies which
block PrPC-PrPSc binding, and
PrPSc unfolding therapy with a novel-class molecular chaperone, are currently
underway.
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