转甲状腺素蛋白聚集及毒性的机制。

Mechanisms of transthyretin aggregation and toxicity.

作者信息

Gasperini Robert J, Klaver David W, Hou Xu, Aguilar Marie-Isabel, Small David H

机构信息

Menzies Research Institute, University of Tasmania, Liverpool Street, 7001, Hobart, TAS, Australia,

出版信息

Subcell Biochem. 2012;65:211-24. doi: 10.1007/978-94-007-5416-4_9.

DOI:10.1007/978-94-007-5416-4_9

PMID:23225005

Abstract

Amyloidoses are characterised by the deposition of insoluble protein that occurs in the extracellular compartment of various tissues. One form of amyloidosis is caused by transthyretin (TTR) misfolding and deposition in target tissues. It is clear that many amyloidoses share common features of fibrillogenesis and toxicity. This chapter examines the mechanisms of TTR aggregation with a view to understanding the possible therapeutic interventions in amyloid disease.

摘要

淀粉样变性的特征是不溶性蛋白质沉积在各种组织的细胞外区室中。一种淀粉样变性形式是由转甲状腺素蛋白（TTR）错误折叠并沉积在靶组织中引起的。很明显，许多淀粉样变性具有共同的纤维形成和毒性特征。本章研究TTR聚集的机制，以期了解对淀粉样疾病可能的治疗干预措施。