Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin.
Immunol Lett
; 81(1): 41-8, 2002 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-11841844
ABSTRACT
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 CH(2) 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 (Fabprime prime or minute)(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 inflamed or damaged tissues where plasma protein leakage occurs, degradation by MMPs may be a mechanism for clearance of IgG.
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Base de dados:
MEDLINE
Assunto principal:
Imunoglobulina G
/
Metaloproteinase 3 da Matriz
/
Metaloproteinase 7 da Matriz
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Immunol Lett
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
Reino Unido