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Abstract
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.