Prion diseases: contribution of high‐resolution immunomorphology | Zendy

Fournier JG. | Zendy; Grigoriev V. | Zendy

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Prion diseases: contribution of high‐resolution immunomorphology

Author(s) -

Fournier JG.,

Grigoriev V.

Publication year - 2001

Publication title -

journal of cellular and molecular medicine

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.44

H-Index - 130

eISSN - 1582-4934

pISSN - 1582-1838

DOI - 10.1111/j.1582-4934.2001.tb00171.x

Subject(s) - prion protein , biogenesis , prion proteins , biology , scrapie , amyloid (mycology) , microbiology and biotechnology , virology , pathology , disease , biochemistry , medicine , botany , gene

The transmisible spongiform encephalopathies or prion diseases are fatal neurological diseases that occur in animals and humans. They are characterized by the accumulation in the cerebral tissue of the abnormal form of prion protein (PrP sc ) produced by a post‐translational event involving conformational change of its normal cellular counterpart (PrP c ). In this short review, we present some results on the biology of prion proteins which have benefited from morphological approaches combining the electron microscopy techniques and the immunodetection methods. We discuss data concerning in particular the physiological function of the normal cellular prion prion (PrP c ) which have allowed to open up new vistas on prion diseases, the biogenesis of amyloid plaque and the cellular site involved in the prion protein conversion process.

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