Opdenakker G, Van den Steen P E, Van Damme J
Rega Institute for Medical Research, Laboratory of Molecular Immunology, University of Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium.
Trends Immunol. 2001 Oct;22(10):571-9. doi: 10.1016/s1471-4906(01)02023-3.
Gelatinase B (matrix metalloproteinase-9) is a secreted multidomain enzyme that is important for the remodeling of the extracellular matrix and the migration of normal and tumor cells. It cleaves denatured collagens (gelatins) and type IV collagen, which is present in basement membranes. In the immune system, this cleavage helps lymphocytes and other leukocytes to enter and leave the blood and lymph circulations. Gelatinase B also cleaves myelin basic protein and type II gelatins, and this clipping leads to remnant epitopes that generate autoimmunity, the so-called REGA model of autoimmunity. Recently, gelatinase B has been found to process cytokines and chemokines, resulting in skewed immune functions. Therefore, gelatinase B, often considered as a pure effector molecule, acts as a switch and catalyst in both innate and specific immunity, and constitutes a prototypic example of the regulation of immune functions by proteolysis.
明胶酶B（基质金属蛋白酶-9）是一种分泌型多结构域酶，对细胞外基质重塑以及正常细胞和肿瘤细胞的迁移至关重要。它能切割变性胶原蛋白（明胶）和存在于基底膜中的IV型胶原蛋白。在免疫系统中，这种切割有助于淋巴细胞和其他白细胞进出血液循环和淋巴循环。明胶酶B还能切割髓鞘碱性蛋白和II型明胶，这种切割会产生导致自身免疫的残余表位，即所谓的自身免疫REGA模型。最近，人们发现明胶酶B可加工细胞因子和趋化因子，从而导致免疫功能失衡。因此，明胶酶B通常被视为一种单纯的效应分子，在固有免疫和特异性免疫中都起着开关和催化剂的作用，构成了通过蛋白水解调节免疫功能的一个典型例子。
