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Ultrastructural localization of prion proteins: Physiological and pathological implications
Author(s) -
Fournier JeanGuy,
EscaigHaye Françoise,
Grigoriev Vladimir
Publication year - 2000
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/1097-0029(20000701)50:1<76::aid-jemt11>3.0.co;2-#
Subject(s) - ultrastructure , pathological , biology , prion protein , pathology , microbiology and biotechnology , disease , medicine , anatomy
The transmissible spongiform encephalopathies (TSE) or prion diseases are fatal neurodegenerative disorders in which the central event is the conversion of a normal host‐encoded protein (PrP c ) into an abnormal isoform (PrP sc ) which accumulates as amyloid in TSE brain. The two PrP c and PrP sc prion protein isoforms are membrane sialoglycoproteins synthesized in the central nervous system and various peripheral organ tissues. In this review, we describe the ultrastructural localization of prion proteins in human and animal cerebral and non‐cerebral tissues whether or not infected by TSE agents. In addition to the plasma membrane of several cells, PrP c was found in association with cytoplasmic organelles of central and nerve‐muscle synapses, and secretory granules of epithelial cells. Fibrils of amyloid plaques, synaptic structures, and lysosome‐like organelles constitute the subcellular sites harboring PrP sc . These findings have led to discussions on the physiological role of PrP c and the pathological mechanisms underlying prion spongiform encephalopathies. Microsc. Res. Tech. 50:76–88, 2000. © 2000 Wiley‐Liss, Inc.