Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, MD, USA.
Endocr Rev. 2021 May 25;42(3):259-294. doi: 10.1210/endrev/bnaa033.
The kexin-like proprotein convertases perform the initial proteolytic cleavages that ultimately generate a variety of different mature peptide and proteins, ranging from brain neuropeptides to endocrine peptide hormones, to structural proteins, among others. In this review, we present a general introduction to proprotein convertase structure and biochemistry, followed by a comprehensive discussion of each member of the kexin-like subfamily of proprotein convertases. We summarize current knowledge of human proprotein convertase insufficiency syndromes, including genome-wide analyses of convertase polymorphisms, and compare these to convertase null and mutant mouse models. These mouse models have illuminated our understanding of the roles specific convertases play in human disease and have led to the identification of convertase-specific substrates; for example, the identification of procorin as a specific PACE4 substrate in the heart. We also discuss the limitations of mouse null models in interpreting human disease, such as differential precursor cleavage due to species-specific sequence differences, and the challenges presented by functional redundancy among convertases in attempting to assign specific cleavages and/or physiological roles. However, in most cases, knockout mouse models have added substantively both to our knowledge of diseases caused by human proprotein convertase insufficiency and to our appreciation of their normal physiological roles, as clearly seen in the case of the furin, proprotein convertase 1/3, and proprotein convertase 5/6 mouse models. The creation of more sophisticated mouse models with tissue- or temporally-restricted expression of specific convertases will improve our understanding of human proprotein convertase insufficiency and potentially provide support for the emerging concept of therapeutic inhibition of convertases.
该 kexin 样蛋白前体转化酶执行最初的蛋白水解切割,最终产生各种不同的成熟肽和蛋白质,从脑神经肽到内分泌肽激素,再到结构蛋白等。在这篇综述中,我们首先介绍蛋白前体转化酶的结构和生化特性,然后全面讨论 kexin 样蛋白前体转化酶亚家族的每个成员。我们总结了人类蛋白前体转化酶不足综合征的最新知识,包括对转化酶多态性的全基因组分析,并将这些与转化酶缺失和突变的小鼠模型进行了比较。这些小鼠模型阐明了我们对特定转化酶在人类疾病中的作用的理解,并导致了对转化酶特异性底物的鉴定;例如,在心脏中鉴定出 procorin 是 PACE4 的特异性底物。我们还讨论了小鼠缺失模型在解释人类疾病方面的局限性,例如由于物种特异性序列差异导致的前体切割差异,以及在试图分配特定切割和/或生理作用时转化酶之间功能冗余带来的挑战。然而,在大多数情况下,敲除小鼠模型大大增加了我们对人类蛋白前体转化酶不足引起的疾病的认识,并使我们更加了解它们的正常生理作用,这在 furin、蛋白前体转化酶 1/3 和蛋白前体转化酶 5/6 小鼠模型中得到了清晰体现。创建具有特定转化酶组织或时间特异性表达的更复杂的小鼠模型将有助于我们理解人类蛋白前体转化酶不足,并为新兴的转化酶治疗抑制概念提供支持。