Klein-Szanto Andres J, Bassi Daniel E
Fox Chase Cancer Center, 333 Cotman Ave, Philadelphia 19111, USA.
Fox Chase Cancer Center, 333 Cotman Ave, Philadelphia 19111, USA.
Biochem Pharmacol. 2017 Sep 15;140:8-15. doi: 10.1016/j.bcp.2017.04.027. Epub 2017 Apr 27.
Proprotein convertases are serine proteases responsible for the cleavage and subsequent activation of protein substrates, many of them relevant for the development of an ample variety of diseases. Seven of the PCs, including furin and PACE4, recognize and hydrolyze the C-terminal end of the general sequence RXRR/KXR, whereas PCSK-9 recognizes a series of non-basic amino acids. In some systems, PC-mediated substrate activation results in the development of pathological processes, such as cancer, endocrinopathies, and cardiovascular and infectious diseases. After establishing PCs as relevant contributors to disease processes, research efforts were directed towards the development of inhibition strategies, including small and large molecules, anti-sense therapies, and antibody-based therapies. Most of these inhibitors mimic the consensus sequence of PCs, blocking the active site in a competitive manner. The most promising inhibitors were designed as bioengineered proteins; however, some non-protein and peptidomimetic agents have also proved to be effective. These efforts led to the design of pre-clinical studies and clinical trials utilizing inhibitors to PCs. Although the initial studies were performed using non-selective PCs inhibitors, such as CMK, the search for more specific, and compartmentalized selective inhibitors resulted in specific activities ascribed to some, but not all of the PCs. For instance, PACE4 inhibitors were effective in decreasing prostate cancer cell proliferation, and neovascularization. Decreased metastatic ovarian cancer utilizing furin inhibitors represents one of the major endeavors, currently in a phase II trial stage. Antibodies targeting PCSK-9 decreased significantly the levels of HDL-cholesterol, in a phase III trial. The study of Proprotein convertases has reached a stage of maturity. New strategies based on the alteration of their activity at the cellular and clinical level represent a promising experimental pharmacology field. The development of allosteric inhibitors, or specific agents directed against individual PCs is one of the challenges to be unraveled in the future.
前体蛋白转化酶是丝氨酸蛋白酶,负责切割并随后激活蛋白质底物,其中许多底物与多种疾病的发生发展相关。包括弗林蛋白酶和PACE4在内的7种前体蛋白转化酶识别并水解通用序列RXRR/KXR的C末端,而PCSK-9识别一系列非碱性氨基酸。在某些系统中,前体蛋白转化酶介导的底物激活会导致病理过程的发生,如癌症、内分泌疾病以及心血管和传染病。在确定前体蛋白转化酶是疾病过程的相关促成因素之后,研究工作转向了抑制策略的开发,包括小分子和大分子、反义疗法以及基于抗体的疗法。这些抑制剂大多模拟前体蛋白转化酶的共有序列,以竞争性方式阻断活性位点。最有前景的抑制剂被设计为生物工程蛋白;然而,一些非蛋白和拟肽药物也已被证明是有效的。这些努力促成了利用前体蛋白转化酶抑制剂进行临床前研究和临床试验的设计。尽管最初的研究使用的是非选择性前体蛋白转化酶抑制剂,如CMK,但对更特异性、更具区室化选择性的抑制剂的探索导致了某些(但不是全部)前体蛋白转化酶具有特定活性。例如,PACE4抑制剂可有效降低前列腺癌细胞的增殖和新血管形成。使用弗林蛋白酶抑制剂减少转移性卵巢癌是目前处于II期试验阶段的主要研究之一。在一项III期试验中,靶向PCSK-9的抗体显著降低了高密度脂蛋白胆固醇水平。前体蛋白转化酶的研究已进入成熟阶段。基于在细胞和临床水平改变其活性的新策略代表了一个有前景的实验药理学领域。开发变构抑制剂或针对单个前体蛋白转化酶的特异性药物是未来有待解决的挑战之一。