The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family.
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family.
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DOI：
10.1186/s13059-015-0676-3
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发表时间：
2015-05-30
期刊：
影响因子：
12.3
通讯作者：
Edwards DR
中科院分区：
文献类型：
--
作者：
Kelwick R;Desanlis I;Wheeler GN;Edwards DR
ADAMTS(带有血栓反应蛋白基序的去整合素和金属蛋白酶)酶是一种分泌的、多结构域基质相关的锌金属内肽酶，在组织形态发生和病理生理重塑、炎症和血管生物学中具有不同的作用。人类家族有19个成员，可以根据它们的已知底物进行细分，即聚糖酶或蛋白聚糖酶(ADAMTS1、4、5、8、9、15和20)、前胶原N-肽酶(ADAMTS2、3和14)、软骨低聚基质蛋白裂解酶(ADAMTS7和12)、von-Willebrand因子蛋白水解酶(ADAMTS13)和一组孤儿酶(ADAMTS6、10、16、17、18和19)。细胞外基质(ECM)的结构和功能的控制是ADAMTS生物学的中心主题，例如胶原纤维组装中的前胶原N-前肽酶和ECM蛋白多糖的裂解或修饰中的聚集聚糖酶的作用。某些家庭成员的缺陷会导致遗传性遗传疾病，而其他家庭成员的异常表达或功能与关节炎、癌症和心血管疾病有关。特别是，ADAMTS4和5已成为关节炎的治疗靶点。来自不同亚组的多种ADAMTS在肿瘤的发生和转移中发挥积极或消极的作用，既有金属蛋白酶依赖的作用，也有非金属蛋白酶依赖的作用。ADAMTS的基本结构包括一个金属蛋白酶催化结构域和一个羧基末端的辅助结构域，后者决定了底物的专一性和蛋白酶及其相互作用伙伴的定位；辅助结构域可能也具有独立的生物学功能。这篇综述主要集中在聚集聚糖酶和蛋白聚糖酶上，对ADAMTS家族的进化、它们与发育和疾病机制的联系以及未来的关键问题提供了一个视角。
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) enzymes are secreted, multi-domain matrix-associated zinc metalloendopeptidases that have diverse roles in tissue morphogenesis and patho-physiological remodeling, in inflammation and in vascular biology. The human family includes 19 members that can be sub-grouped on the basis of their known substrates, namely the aggrecanases or proteoglycanases (ADAMTS1, 4, 5, 8, 9, 15 and 20), the procollagen N-propeptidases (ADAMTS2, 3 and 14), the cartilage oligomeric matrix protein-cleaving enzymes (ADAMTS7 and 12), the von-Willebrand Factor proteinase (ADAMTS13) and a group of orphan enzymes (ADAMTS6, 10, 16, 17, 18 and 19). Control of the structure and function of the extracellular matrix (ECM) is a central theme of the biology of the ADAMTS, as exemplified by the actions of the procollagen-N-propeptidases in collagen fibril assembly and of the aggrecanases in the cleavage or modification of ECM proteoglycans. Defects in certain family members give rise to inherited genetic disorders, while the aberrant expression or function of others is associated with arthritis, cancer and cardiovascular disease. In particular, ADAMTS4 and 5 have emerged as therapeutic targets in arthritis. Multiple ADAMTSs from different sub-groupings exert either positive or negative effects on tumorigenesis and metastasis, with both metalloproteinase-dependent and -independent actions known to occur. The basic ADAMTS structure comprises a metalloproteinase catalytic domain and a carboxy-terminal ancillary domain, the latter determining substrate specificity and the localization of the protease and its interaction partners; ancillary domains probably also have independent biological functions. Focusing primarily on the aggrecanases and proteoglycanases, this review provides a perspective on the evolution of the ADAMTS family, their links with developmental and disease mechanisms, and key questions for the future.
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影响因子：
2.7
作者：
Dupuis LE;McCulloch DR;McGarity JD;Bahan A;Wessels A;Weber D;Diminich AM;Nelson CM;Apte SS;Kern CB
通讯作者：
Kern CB
影响因子：
3
作者：
Cudic, Mare;Burstein, Gayle D.;Lauer-Fields, Janelle
通讯作者：
Lauer-Fields, Janelle
影响因子：
1.5
作者：
Dubail, Johanne;Aramaki-Hattori, Noriko;Bader, Hannah L.;Nelson, Courtney M.;Katebi, Negin;Matuska, Brittany;Olsen, Bjorn R.;Apte, Suneel S.
通讯作者：
Apte, Suneel S.
影响因子：
3.4
作者：
Brunet FG;Fraser FW;Binder MJ;Smith AD;Kintakas C;Dancevic CM;Ward AC;McCulloch DR
通讯作者：
McCulloch DR
影响因子：
4.8
作者：
Abbaszade, I;Liu, RQ;Burn, TC
通讯作者：
Burn, TC