Abnormal isoform of prion proteins accumulates in the synaptic structures of the central nervous system in patients with Creutzfeldt-Jakob disease

T. Kitamoto, R. W. Shin, K. Doh-ura, N. Tomokane, M. Miyazono, T. Muramoto, J. Tateishi

Research output: Contribution to journalArticlepeer-review

248 Citations (Scopus)

Abstract

A new method, which enabled the first immunohistochemical documentation of abnormal prion protein (PrP) in all patients with Creutzfeldt-Jakob disease (CJD), was established. This method designated as 'hydrolytic autoclaving' revealed punctate PrP(CJD) stainings around the neuronal cell bodies and dendrites in CJD brains. These punctate stainings were almost identical with that of synaptophysin, suggesting PrP(CJD) accumulations in the synaptic structures. Subcellular fractionation revealed that prion protein in Creutzfeldt-Jakob disease (PrP(CJD)) was most concentrated in the synaptosomal fraction. In CJD patients with a long clinical course, synaptophysin immunoreactivity decreased, and synaptic PrP(CJD) accumulated with a wider distribution. These results suggest that synaptic PrP(CJD) accumulations might be responsible for the neuronal dysfunction and degeneration in CJD.

Original languageEnglish
Pages (from-to)1285-1294
Number of pages10
JournalAmerican Journal of Pathology
Volume140
Issue number6
Publication statusPublished - 1992 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

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