Distribution and submicroscopic immunogold localization of cellular prion protein (PrPc) in extracerebral tissues.
In transmissible spongiform encephalopathies (TSE), such as scrapie in animals and Creutzfeldt-Jakob disease in humans, the central event is the conversion of a host-encoded amyloidogenic protein (PrPc) into an abnormal isoform (PrPsc) that accumulates as amyloid in TSE brain. PrPc is a membrane sialoglycoprotein synthesized in the central nervous system and elsewhere. We have examined the ultrastructural localization of PrPc in numerous hamster and some human extracerebral tissues, by means of a post-embedding electron-microscopic method combined with immunogold labeling. In stomach, intestine, lung, and kidney from hamsters, and in stomach, kidney, and spleen from humans, immunogold labeling specific for PrPc is observed on various cellular substructures related to secretory pathways: Golgi apparatus, secretory globules, and plasma membrane. In mucous epithelial cells of stomach and intestine, PrPc appears to be concentrated in secretory globules, suggesting a role for PrPc in the secretory function of the digestive tract. The secretory aspect of PrPc may be a key to understanding the physiopathological mechanisms underlying TSE.
Fournier
J G
JG
U 153 INSERM, Institut de Myologie, Hôpital Pitié-Salpêtrière, 47 Bd de l'Hôpital, F-75651 Paris cedex 13, France.
Escaig-Haye
F
F
Billette de Villemeur
T
T
Robain
O
O
Lasmézas
C I
CI
Deslys
J P
JP
Dormont
D
D
Brown
P
P
D000818:Animals; D001923:Brain Chemistry; D006224:Cricetinae; D006801:Humans; D008647:Mesocricetus; D016253:Microscopy, Immunoelectron / Q000379:methods; D009928:Organ Specificity; D018621:PrPC Proteins / Q000378:metabolism*; D013347:Subcellular Fractions / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D016610:Tissue Embedding
D018621:PrPC Proteins