- 期刊
人類與動物之普粒子疾病
Human and Animal Prion Diseases
摘要
普粒子疾病屬於長期潛伏的哺乳類傳染性海綿狀腦病變，一旦出現臨床病兆，病程就會無情的惡化，並且藥石罔效。四種與其相關的人類疾病包括克（庫）魯氏症、典型（傳統型）庫賈氏症、新型庫賈氏症、致死性家族性失眠症。牛、羊、貂與麋鹿等被認為可能與新型庫賈氏症有關聯。人類普粒子疾病的神經病理特徵包括神經喪失、神經膠質細胞增生、不具發炎反應、神經毯出現空泡。目前理論認為動物體內普粒子正常型摺疊蛋白遭遇致病型蛋白之後，會以致病型為模板，以指數倍數使得正常轉變成致病型。大量致病型（β-form）糾結成穩定類澱粉堆積於腦部造成腦組織死亡。目前為止對於此症的治療仍然一籌莫展。
並列摘要
With long incubation periods, prion diseases responsible for the transmissible spongiform encephalopathies in a variety of mammals, progress inexorably once clinical symptoms appear and are currently untreatable and universally fatal. Four human prion diseases are currently recognized: Kuru disease, Creutzfeldt-Jakob disease (CJD), variant Creutzfeldt-Jakob disease (vCJD also known as new variant CJD), and fatal familial insomnia (FFI). Animal Spongiform encephalopathy (BSE) inclusive of cattle, sheep, mink and elk related to a number of prion infections affecting animals, was responsible for bringing these agents to more widespread public attention with its possible link to vCJD. These human prion diseases share certain common neuropathologic features including neuronal loss, proliferation of glial cells, absence of an inflammatory response, and the presence of small vacuoles within the neuropil, which produces a spongiform appearance. The current theory is that folded proteins (PrPc) convert into the disease-associated, prion form (PrPSc); the prion acts as a template to guide the misfolding of more protein into prion form by the exponential growth rate. Prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This stable aggregates are extremely stable and accumulates in brain, causing tissue damage and cell death. No effective treatment has been identified for prion diseases, which are universally fatal.