{"title":"Prion diseases: contribution of high-resolution immunomorphology.","authors":"J G Fournier, B Grigoriev","doi":"10.1111/j.1582-4934.2001.tb00171.x","DOIUrl":null,"url":null,"abstract":"<p><p>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 (PrPsc) produced by a post-translational event involving conformational change of its normal cellular counterpart (PrPc). 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 (PrPc) 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.</p>","PeriodicalId":94327,"journal":{"name":"Journal of cellular and molecular medicine","volume":null,"pages":null},"PeriodicalIF":4.3000,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6740125/pdf/JCMM-5-367.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of cellular and molecular medicine","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1111/j.1582-4934.2001.tb00171.x","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
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 (PrPsc) produced by a post-translational event involving conformational change of its normal cellular counterpart (PrPc). 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 (PrPc) 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.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
