The cathepsin family and their role in colorectal cancer
The cathepsin family and their role in colorectal cancer
复制标题
DOI：
10.1016/j.prp.2008.04.010
复制
发表时间：
2008-01-01
影响因子：
2.8
通讯作者：
Krueger, Sabine
中科院分区：
文献类型：
--
作者：
Kuester, Doerthe;Lippert, Hans;Krueger, Sabine
组织蛋白是一类球状蛋白水解酶，最初被描述为细胞内的多肽水解酶，尽管一些组织蛋白也具有细胞外功能。组织蛋白酶B、C、F、H、L、K、O、S、V、W和X是木瓜蛋白酶家族中最大和最知名的一类半胱氨酸蛋白酶。组织蛋白酶G是一种丝氨酸羧肽酶，组织蛋白酶D和组织蛋白酶E是天冬氨酸蛋白酶。组织蛋白被合成为失活的酶原，并被加工成成熟的和活性的酶。内源性蛋白抑制物，如半胱氨酸氨基转移酶和某些蛇毒蛋白，会抑制活性酶。作为主要的溶酶体蛋白水解酶，组织蛋白在生理过程中发挥着重要的作用，在一些疾病中也发挥着重要的作用。基于其降解细胞外基质蛋白的能力，组织蛋白被认为在结直肠癌的侵袭和转移中发挥作用。本文就组织蛋白酶在结直肠癌发病过程中的作用及其与临床病理特征的关系进行综述。此外，我们还综述了组织蛋白酶在动物模型和结直肠疾病体外实验中的最新进展，并提供了组织蛋白酶抑制剂作为可能的治疗药物的信息。(C)2008年爱思唯尔股份有限公司。版权所有。
Cathepsins are a class of globular proteases, initially described as intracellular peptide hydrolases, although several cathepsins also have extracellular functions. Cathepsins B, C, F, H, L, K, O, S, V, W, and X are cysteine proteases of the papain family, and represent the largest and best-known class of the cathepsins. Cathepsin G is a serine carboxypeptidases, and cathepsins D and E are aspartic proteases. Cathepsins are synthesized as inactive proenzymes and processed to become mature and active enzymes. Endogenous protein inhibitors, such as cystatins and some serpins, inhibit active enzymes. As primarily lysosomal proteases, cathepsins play important roles in proteolysis during physiological processes, as well as in several diseases. On the basis of their ability to degrade extracellular matrix proteins, cathepsins have been implicated to play a role in invasion and metastasis of colorectal cancer. In the present review, the role of cathepsins in the disease process of colorectal cancers and the correlation of cathepsin expression and activity with clinicopathological features is discussed. Furthermore, we give an overview of the recent developments of cathepsins in animal models and in in vitro experiments of colorectal disease, and provide information on inhibitors of cathepsins as possible therapeutics. (C) 2008 Elsevier GmbH. All rights reserved.