Identification of Candidate Proteins Binding to Prion Protein

Fruma Yehiely; Paul Bamborough; Maria Da Costa; Billie J. Perry; Gopal Thinakaran; Fred E. Cohen; George A. Carlson; Stanley B. Prusiner

Neurobiology of Disease (Jan 1997)

Identification of Candidate Proteins Binding to Prion Protein

Fruma Yehiely,
Paul Bamborough,
Maria Da Costa,
Billie J. Perry,
Gopal Thinakaran,
Fred E. Cohen,
George A. Carlson,
Stanley B. Prusiner

Affiliations

Fruma Yehiely: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205
Paul Bamborough: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205
Maria Da Costa: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205
Billie J. Perry: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205
Gopal Thinakaran: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205
Fred E. Cohen: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205
George A. Carlson: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205
Stanley B. Prusiner: Department of Neurology, University of California, San Francisco, California, 94143; Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, 94143; McLaughlin Research Institute, Great Falls, Montana, 59405; Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205

Journal volume & issue: Vol. 3, no. 4
pp. 339 – 355

Abstract

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Prion diseases are disorders of protein conformation that produce neurodegeneration in humans and animals. Studies of transgenic (Tg) mice indicate that a factor designated protein X is involved in the conversion of the normal cellular prion protein (PrPC) into the scrapie isoform (PrPSc); protein X appears to interact with PrPCbut not with PrPSc. To search for PrPCbinding proteins, we fused PrP with alkaline phosphatase (AP) to produce a soluble, secreted probe. PrP–AP was used to screen a λgt11 mouse brain cDNA library, and six clones were isolated. Four cDNAs are novel while two clones are fragments of Nrf2 (NF-E2 related factor 2) transcription factor and Aplp1 (amyloid precursor-like protein 1). The observation that PrP binds to a member of the APP (amyloid precursor protein) gene family is intriguing, in light of possible relevance to Alzheimer's disease. Four of the isolated clones are expressed preferentially in the mouse brain and encode a similar motif.

Published in Neurobiology of Disease

ISSN: 0969-9961 (Print); 1095-953X (Online)
Publisher: Elsevier
Country of publisher: United States
LCC subjects: Medicine: Internal medicine: Neurosciences. Biological psychiatry. Neuropsychiatry
Website: https://www.journals.elsevier.com/neurobiology-of-disease

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