Publication Detail

The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in PubMed. This abstract is what is used to create the fingerprint of the publication. If any grants are referenced by the publication, they will be listed here as well.

PrP27-30 is a normal soluble prion protein fragment released by human platelets.

F Perini; R Vidal; B Ghetti; F Tagliavini; B Frangione; F Prelli (Profiled Author: Frangione, Blas)

Department of Pathology, New York University Medical Center, New York 10016, USA.
Biochemical and biophysical research communications 1996;223(3):572-7.

Prion diseases are neurodegenerative disorders characterized by the accumulation of abnormal isoforms of prion protein (PrPSc) in the central nervous system. PrPSc isoforms differ from their normal homologue (PrPC), in that they possess increased beta-sheet conformation, are partially protease resistant and may be associated with amyloid deposition. Amyloid proteins are thought to derive from soluble precursors or fragments thereof, present in biological fluids, which in the disease state undergo conformational change leading to aggregation and deposition in target tissues. We report here that platelets carry PrP mRNA and release PrPC, a sialoglycoprotein bound to the cell surface by a glycosylphosphatidylinositol (GPI) anchor. Soluble PrPC, and a N-terminal truncated PrPC isoform starting at position 90 are secreted by resting and agonist-stimulated platelets and are detectable after partial deglycosylation of releasates. N-terminal sequence analysis of the soluble 27-30 kDa isoform, GQGGGTHSQ(W)NKP, revealed homology to scrapie PrP27-30, the protease resistant core derived from PrPSc. These findings indicate that in addition to PrPC, platelets process a soluble PrP27-30 isoform. Whether this isoform can be converted in scrapie PrP27-30 remains to be determined.

5 Originating Grant

• 1.

  FRANGIONE, BLAS

  BIOCHEMISTRY OF LEWY BODIES AND GELSOLIN AMYLOID

  30 September 1991 - 29 September 1997

  NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE

  Total Funding: $ 898,861

• 2.

  FRANGIONE, BLAS

  AMYLOIDOSIS AND ALZHEIMERS DISEASE

  1 July 1985 - 30 June 1997

  NATIONAL INSTITUTE ON AGING

  Total Funding: $ 3,049,140

• 3.

  Frangione, Blas

  Amyloidosis and Alzheimer's Disease

  1 July 1985 - 30 June 2007

  NATIONAL INSTITUTE ON AGING

  Total Funding: $ 4,467,436

• 4.

  Frangione, Blas

  CONFORMATIONAL DISORDERS--AMYLOID AND PRION PROTEINS

  1 September 1978 - 31 March 2006

  NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES

  Total Funding: $ 3,600,812

• 5.

  FRANGIONE, BLAS

  STRUCTURE OF IMMUNOGLOBULINS AND RELATED PROTEINS

  1 September 1978 - 31 March 1999

  NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES

  Total Funding: $ 2,819,853

Scientific Context

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