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Presence of prion protein in peripheral tissues of Libyan Jews with Creutzfeldt-Jakob disease

Department of Neurology (Dr. Meiner, M. Halimi, and Dr. Gabizon), Haddssah University Hospital, Jerusalem, Israel; the Department of Virology (Dr. Polakiewicz), Hebrew University Medical School, Jerusalem, Israel; and the Departments of Neurology and Biochemistry and Biophysics (Dr. Prusiner), University of California at San Francisco, CA.

The prion protein (PrP) gene on chromosome 20 encodes a protein designated PrP^C. An abnormal, protease-resistant isoform of PrP^C, denoted PrP^CJD or PrP^Sc, is present in the brains of patients with Creutzfeldt-Jakob disease (CJD). In Libyan Jews, CJD segregates with a point mutation at codon 200 of the PrP gene, resulting in the substitution of lysine for glutamate. In the present study, we examined the presence of PrP in fibroblasts and leukocytes derived from eight CJD patients with the codon 200 mutation. In cultured fibroblasts as well as in leukocytes, there was a significant increase in PrP as judged by immunocytochemistry in addition to immunoblotting. Most of the PrP in fibroblasts and leukocytes could be released from the external surface by phosphatidylinositol-specific phospholipase C, a property characteristic of PrP^C. In leukocytes only, part of the protein was protease resistant, resembling PrP^CJD. The concentration of PrP mRNA was similar in fibroblast lines derived from controls and CJD patients. These results suggest that in CJD patients carrying a mutation at codon 200 of the PrP gene, the metabolism of PrP, rather than PrP synthesis, is abnormal.

Address correspondence and reprint requests to Dr. Ruth Gabizon, Department of Neurology, Hadassah Hospital, POB 12000, Jerusalem, Israel 91120.

Supported by research grants from the Israeli Ministry of Health, Israel USA Binational Foundation, the joint research fund of the Hebrew University and Hadassah, the American Health Assistance Foundation, and the National Institutes of Health (AG-02132, NS-14069, AG-08967, and NS-227863.

Received September 18, 1991. Accepted for publication in final form December 13, 1991.

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