Department of Chemistry, The University of Western Ontario, 1151 Richmond St., London, ON N6A5B7, Canada.
Int J Mol Sci. 2020 Aug 9;21(16):5697. doi: 10.3390/ijms21165697.
Carbonic anhydrases (CAs) and metallothioneins (MTs) are both families of zinc metalloproteins central to life, however, they coordinate and interact with their Zn ion cofactors in completely different ways. CAs and MTs are highly sensitive to the cellular environment and play key roles in maintaining cellular homeostasis. In addition, CAs and MTs have multiple isoforms with differentiated regulation. This review discusses current literature regarding these two families of metalloproteins in carcinogenesis, with a dialogue on the association of these two ubiquitous proteins in vitro in the context of metalation. Metalation of CA by Zn-MT and Cd-MT is described. Evidence for protein-protein interactions is introduced from changes in metalation profiles of MT from electrospray ionization mass spectrometry and the metalation rate from stopped-flow kinetics. The implications on cellular control of pH and metal donation is also discussed in the context of diseased states.
碳酸酐酶 (CA) 和金属硫蛋白 (MT) 都是锌金属蛋白酶家族，对生命至关重要，但它们与锌离子辅因子的配位和相互作用方式完全不同。CA 和 MT 对细胞环境高度敏感，在维持细胞内环境稳定方面发挥着关键作用。此外，CA 和 MT 具有多种具有差异化调节的同工型。本综述讨论了目前关于这两种金属蛋白酶家族在致癌作用中的文献，并就这两种普遍存在的蛋白质在体外金属化背景下的关联进行了对话。描述了 CA 通过 Zn-MT 和 Cd-MT 的金属化。从电喷雾电离质谱中 MT 的金属化谱的变化和停流动力学的金属化速率引入了蛋白质-蛋白质相互作用的证据。还讨论了在疾病状态下细胞对 pH 和金属供体控制的影响。
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