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• Vol.43 No.11
• CLINICA NEUROL, 43: 817−819, 2003
• Vol.43 No.11 contents

The 44th Annual Meeting of the Japanese Society of Neurology

Symposium 3-4: Unfolding chaperone as a prion protein relating molecule

Naomi S. Hachiya, M.D. Yuji Sakasegawa M.D. and Kiyotoshi Kaneko M.D.

Department of Cortical Function Disorders, National Institute of Neuroscience, National Center of Neurology and Psychiatry

Prion protein exists in two different isoforms, a normal cellular isoform (PrP^C) and an abnormal infectious isoform (PrP^Sc), the latter is a causative agent of prion disease such as mad cow disease and Creutzfeldt-Jakob disease. Amino acid sequences of PrP^C and PrP^Sc are identical, but their conformations are rather different; PrP^C rich in non β -sheet vs. PrP^Sc rich in β -sheet isoform. Since the two isoforms have quite different conformation, this host factor might be a molecular chaperone, which enables to override an energy barrier between PrP^C and PrP^Sc.
To examine the protein unfolding activities against collectly folded structure exist or not, we constructed an assay system and purified a novel molecular chaperone, Unfoldin, from S. cerevisiae. Unfoldin consists of oligomeric ring-like structure with the central cavity and has an ATP-dependent protein unfolding activity with broad specificity in vitro, of which targets included PrP in β -sheet form, α -synuclein, and Aβ protein.
We have also found that mouse neuroblastoma N2a cells contained the activity. Treatment of this factor with an ATP-hydrolyzing enzyme, apyrase, caused the decrease in its protein unfolding activity. It was suggested that the purified protein probably formed homo-oligomer consisting of 4-5 subunits and its activity was ATP-dependent.

(CLINICA NEUROL, 43: 817−819, 2003)
key words: prion disease, prion protein, Unfoldin, molecular chaperone

(Received: 16-May-03)