de Groot Natalia S, Sabate Raimon, Ventura Salvador
Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain.
Trends Biochem Sci. 2009 Aug;34(8):408-16. doi: 10.1016/j.tibs.2009.03.009. Epub 2009 Aug 3.
Protein misfolding and aggregation into amyloid structures are associated with dozens of human diseases. Recent studies have provided compelling evidence for the existence of highly ordered, amyloid-like conformations in the insoluble inclusion bodies produced during heterologous protein expression in bacteria. Thus, amyloid aggregation seems to be an omnipresent process in both eukaryotic and prokaryotic organisms. Amyloid formation inside cell factories raises important safety concerns with regard to the toxicity and infectivity of recombinant proteins. Yet such findings also suggest that prokaryotic cells could be useful systems for studying how and why proteins aggregate in vivo, and they could also provide a biologically relevant background for screening therapeutic approaches to pathologic protein deposition.
蛋白质错误折叠并聚集成淀粉样结构与数十种人类疾病相关。最近的研究提供了有力证据，证明在细菌中异源蛋白质表达过程中产生的不溶性包涵体中存在高度有序的淀粉样构象。因此，淀粉样聚集似乎是真核生物和原核生物中普遍存在的过程。细胞工厂内淀粉样蛋白的形成引发了关于重组蛋白毒性和感染性的重要安全问题。然而，这些发现也表明原核细胞可能是研究蛋白质在体内如何以及为何聚集的有用系统，并且它们还可以为筛选病理性蛋白质沉积的治疗方法提供生物学相关背景。
