Gerstmann-straussler-scheinker disease (Prnp p102l)

Amyloid deposits are best recognized by antibodies directed to epitopes in prp region 90-165

Pedro Piccardo, Bernardino Ghetti, Dennis W. Dickson, Harry V. Vinters, Giorgio Giaccone, Orso Bugiani, Fabrizio Tagliavini, Katherine Young, Stephen Dlouhy, Charles Seiler, Carrie K. Jones, Alice Lazzarini, Lawrence I. Golbe, Thomas R. Zimmerman, Susan L. Perlman, Donald C. McLachlan, Peter H St George-Hyslop, Anne Lennox

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Gerstmann-Straussler-Scheinker (GSS) disease is a familial neurological disorder pathologically characterized by accumulation of prion protein (PrP) in the form of fibrillary and non-fibrillary deposits within the cerebrum and cerebellum. We have studied two patients in whom the disease is caused by a leucine for proline amino acid substitution at residue 102 of PrP. In both patients, the neuropathologic findings are similar, consisting of spongiform changes, amyloid deposits, and gliosis. To investigate the antigenic profile of PrP deposits, we used antibodies raised against several peptides that correspond to segments of the N-terminus, repeat region, midregion, and C-terminus of PrP. By immunohistochemistry, PrP amyloid cores are best labeled by antibodies directed to epitopes spanning PrP residues 90-165. In GSS disease caused by a substitution of thymine to cytosine at PRNP codon 198 (Indiana kindred), the major amyloidogenic peptide spans residues 58-150; therefore, in these two genetic forms of GSS disease, amyloid may be composed of different peptides. 1995 by the American Association of Neuropathologists.

Original languageEnglish
Pages (from-to)790-801
Number of pages12
JournalJournal of Neuropathology and Experimental Neurology
Volume54
Issue number6
StatePublished - 1995

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Gerstmann-Straussler-Scheinker Disease
Amyloid Plaques
Epitopes
Antibodies
Amyloid
Peptides
Gliosis
Thymine
Cytosine
Cerebrum
Amino Acid Substitution
Nervous System Diseases
Proline
Codon
Leucine
Cerebellum
Prion Proteins
Immunohistochemistry

Keywords

  • Amyloid
  • Antibodies
  • Gerstmann-Straussler-Scheinker disease
  • Immunohistochemistry
  • Prion protein (PrP)
  • PrP peptides

ASJC Scopus subject areas

  • Clinical Neurology
  • Pathology and Forensic Medicine
  • Cellular and Molecular Neuroscience
  • Neurology
  • Neuroscience(all)

Cite this

Gerstmann-straussler-scheinker disease (Prnp p102l) : Amyloid deposits are best recognized by antibodies directed to epitopes in prp region 90-165. / Piccardo, Pedro; Ghetti, Bernardino; Dickson, Dennis W.; Vinters, Harry V.; Giaccone, Giorgio; Bugiani, Orso; Tagliavini, Fabrizio; Young, Katherine; Dlouhy, Stephen; Seiler, Charles; Jones, Carrie K.; Lazzarini, Alice; Golbe, Lawrence I.; Zimmerman, Thomas R.; Perlman, Susan L.; McLachlan, Donald C.; George-Hyslop, Peter H St; Lennox, Anne.

In: Journal of Neuropathology and Experimental Neurology, Vol. 54, No. 6, 1995, p. 790-801.

Research output: Contribution to journalArticle

Piccardo, P, Ghetti, B, Dickson, DW, Vinters, HV, Giaccone, G, Bugiani, O, Tagliavini, F, Young, K, Dlouhy, S, Seiler, C, Jones, CK, Lazzarini, A, Golbe, LI, Zimmerman, TR, Perlman, SL, McLachlan, DC, George-Hyslop, PHS & Lennox, A 1995, 'Gerstmann-straussler-scheinker disease (Prnp p102l): Amyloid deposits are best recognized by antibodies directed to epitopes in prp region 90-165', Journal of Neuropathology and Experimental Neurology, vol. 54, no. 6, pp. 790-801.
Piccardo, Pedro ; Ghetti, Bernardino ; Dickson, Dennis W. ; Vinters, Harry V. ; Giaccone, Giorgio ; Bugiani, Orso ; Tagliavini, Fabrizio ; Young, Katherine ; Dlouhy, Stephen ; Seiler, Charles ; Jones, Carrie K. ; Lazzarini, Alice ; Golbe, Lawrence I. ; Zimmerman, Thomas R. ; Perlman, Susan L. ; McLachlan, Donald C. ; George-Hyslop, Peter H St ; Lennox, Anne. / Gerstmann-straussler-scheinker disease (Prnp p102l) : Amyloid deposits are best recognized by antibodies directed to epitopes in prp region 90-165. In: Journal of Neuropathology and Experimental Neurology. 1995 ; Vol. 54, No. 6. pp. 790-801.
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abstract = "Gerstmann-Straussler-Scheinker (GSS) disease is a familial neurological disorder pathologically characterized by accumulation of prion protein (PrP) in the form of fibrillary and non-fibrillary deposits within the cerebrum and cerebellum. We have studied two patients in whom the disease is caused by a leucine for proline amino acid substitution at residue 102 of PrP. In both patients, the neuropathologic findings are similar, consisting of spongiform changes, amyloid deposits, and gliosis. To investigate the antigenic profile of PrP deposits, we used antibodies raised against several peptides that correspond to segments of the N-terminus, repeat region, midregion, and C-terminus of PrP. By immunohistochemistry, PrP amyloid cores are best labeled by antibodies directed to epitopes spanning PrP residues 90-165. In GSS disease caused by a substitution of thymine to cytosine at PRNP codon 198 (Indiana kindred), the major amyloidogenic peptide spans residues 58-150; therefore, in these two genetic forms of GSS disease, amyloid may be composed of different peptides. 1995 by the American Association of Neuropathologists.",
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AU - Vinters, Harry V.

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AU - Bugiani, Orso

AU - Tagliavini, Fabrizio

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AU - Dlouhy, Stephen

AU - Seiler, Charles

AU - Jones, Carrie K.

AU - Lazzarini, Alice

AU - Golbe, Lawrence I.

AU - Zimmerman, Thomas R.

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AU - McLachlan, Donald C.

AU - George-Hyslop, Peter H St

AU - Lennox, Anne

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