Chaperoning osteogenesis: new protein-folding disease paradigms.
Chaperoning osteogenesis: new protein-folding disease paradigms.
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DOI：
10.1016/j.tcb.2010.11.007
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发表时间：
2011-03
影响因子：
19
通讯作者：
Leikin S
中科院分区：
文献类型：
--
作者：
Makareeva E;Aviles NA;Leikin S
最近发现几种内质网伴侣缺陷的患者存在严重骨疾病，这正在重塑 I 型胶原蛋白折叠和相关疾病的讨论。 I 型胶原蛋白是所有脊椎动物中最丰富的蛋白质，也是骨骼和其他结缔组织的重要结构分子。它的错误折叠会导致骨骼脆弱、骨骼畸形和其他组织衰竭。对新发现的骨疾病的研究表明，胶原蛋白折叠、参与折叠过程的伴侣、细胞对错误折叠的反应以及相关的骨病理学可能不遵循传统的蛋白质折叠范例。在这篇综述中，我们研究了区分胶原蛋白折叠与其他蛋白质的特征，并描述了开始揭示细胞如何管理胶原蛋白折叠和错误折叠的发现。我们讨论这些研究对一般蛋白质折叠范例、细胞中未折叠蛋白质反应和蛋白质折叠疾病的影响。
Recent discoveries of severe bone disorders in patients with deficiencies in several endoplasmic reticulum chaperones are reshaping the discussion of type I collagen folding and related diseases. Type I collagen is the most abundant protein in all vertebrates and a crucial structural molecule for bone and other connective tissues. Its misfolding causes bone fragility, skeletal deformities and other tissue failures. Studies of newly discovered bone disorders indicate that collagen folding, chaperones involved in the folding process, cellular responses to misfolding, and related bone pathologies may not follow conventional protein folding paradigms. In this review, we examine the features that distinguish collagen folding from that of other proteins and describe findings that are beginning to reveal how cells manage collagen folding and misfolding. We discuss implications of these studies on general protein folding paradigms, unfolded protein response in cells and protein folding diseases.