苦参素
化学
基质金属蛋白酶
劈理(地质)
分子生物学
免疫球蛋白D
抗体
生物化学
生物
免疫学
B细胞
古生物学
断裂(地质)
作者
A. J. H. Gearing,Susan J. Thorpe,Karen Miller,Matthew Mangan,Paul Varley,T.J. Dudgeon,George A. Ward,Christina Turner,Robin Thorpe
标识
DOI:10.1016/s0165-2478(01)00333-9
摘要
We have shown that two of the matrix metalloproteinases (MMPs), matrilysin and stromelysin-1, are capable of cleaving all of the human IgG subclasses. The cleavage occurs at a conserved site in the CH2 domain of the heavy chain of IgG, releasing a single chain Fc-like fragment. We have not been able to demonstrate cleavage of IgA, IgD, IgM or IgE classes, which lack the cleavage site, nor could we show cleavage of IgG by collagenase, gelatinase, macrophage metalloelastase or membrane-type (MT)-MMP. This cleavage of IgG, by separating the antigen-binding (Fab′)2 from the Fc portion, will remove much of the immunoglobulins' functionality, e.g. complement fixation, Fc receptor binding. In the context of a tumour producing matrilysin or stromelysin, this may represent a way in which the tumour protects itself from ADCC. In inflammed or damaged tissues where plasma protein leakage occurs, degradation by MMPs may be a mechanism for clearance of IgG.
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