有限的蛋白酶剪切是一种有效的机制，用于确保血栓素在细胞外基质中的活动动态调节。血栓素是多功能基质细胞蛋白，由多个区域组成，每个区域与细胞受体、基质成分和可溶性因子（生长因子、细胞因子和蛋白酶）具有特定的相互作用模式，因此对细胞行为和对微环境变化的响应产生不同影响。因此，血栓素的蛋白酶降解具有多种功能后果，反映了活性片段和孤立域的局部释放、暴露或破坏活性序列、变化的蛋白质位置，以及TSP基质周围相互作用网络的组成和功能的变化。本文评述了当前文献和数据库中关于不同蛋白酶对哺乳动物血栓素的剪切的数据，讨论了在特定病理情境下产生的片段的作用，特别关注癌症和肿瘤微环境。版权所有 © 2023 Elsevier B.V. 发表。

Limited proteolysis of thrombospondins is a powerful mechanism to ensure dynamic tuning of their activities in the extracellular space. Thrombospondins are multifunctional matricellular proteins composed of multiple domains, each with a specific pattern of interactions with cell receptors, matrix components and soluble factors (growth factors, cytokines and proteases), thus with different effects on cell behavior and responses to changes in the microenvironment. Therefore, the proteolytic degradation of thrombospondins has multiple functional consequences, reflecting the local release of active fragments and isolated domains, exposure or disruption of active sequences, altered protein location, and changes in the composition and function of TSP-based pericellular interaction networks. In this review current data from the literature and databases is employed to provide an overview of cleavage of mammalian thrombospondins by different proteases. The roles of the fragments generated in specific pathological settings, with particular focus on cancer and the tumor microenvironment, are discussed.Copyright © 2023. Published by Elsevier B.V.