Clin Chem Lab Med. 2016 Aug 1;54(8):1281-90. doi: 10.1515/cclm-2015-0668.
Matrix metallo-proteinases (MMPs) are a family of zinc-dependent endopeptidases, capable of degrading all the molecular components of extracellular matrix. A class of MMPs is gelatinases which includes gelatinase A or MMP-2 (72 kDa) and gelatinase B or MMP-9 (92 kDa), which have been shown to play critical roles in pathophysiology of many human disease and, in particular, cancer progression. For these reasons they obtained a great interest as potential non-invasive biomarker in providing useful clinical information in cancer diagnosis and therapy. A sensitive and unexpensive method for analysis of gelatinases is the gelatine zymography, which allows to measure the relative amounts of active and inactive enzymes in body fluids and tissue extracts. The procedure involves the electrophoretic separation of proteins under denaturing but non reducing conditions through a polyacrylamide gel containing a synthetic substrate (gelatin). The aim of this mini-review has been to describe the general principles of gelatine zymography technique, underling the main advantages and disadvantages. Even though an improvement of this method is necessary for a better applicability in laboratory medicine, gelatine zymography represents the most convenient method to detect the activity of the different gelatinases from a wide range of biological samples.
基质金属蛋白酶（MMPs）是一类锌依赖性内肽酶，能够降解细胞外基质的所有分子成分。MMPs 中的一类是明胶酶，包括明胶酶 A 或 MMP-2（72 kDa）和明胶酶 B 或 MMP-9（92 kDa），它们已被证明在许多人类疾病的病理生理学中发挥关键作用，特别是在癌症进展中。出于这些原因，它们作为潜在的非侵入性生物标志物引起了极大的兴趣，为癌症诊断和治疗提供了有用的临床信息。分析明胶酶的一种敏感且廉价的方法是胶凝电泳，它允许测量体液和组织提取物中活性和无活性酶的相对量。该程序涉及在变性但非还原条件下通过含有合成底物（明胶）的聚丙烯酰胺凝胶电泳分离蛋白质。本综述的目的是描述胶凝电泳技术的一般原理，强调其主要优点和缺点。尽管需要改进这种方法才能使其更适用于实验室医学，但胶凝电泳仍然是从广泛的生物样本中检测不同明胶酶活性的最方便方法。
