Acknowledged Signatures of Matrix Metalloproteinases in Takayasu’s Arteritis

Figure 1

Structure of matrix metalloproteinases (MMPs). MMPs contain four domains, that is, prodomain, catalytic domain, hinge region, and hemopexin domain; however, each MMP has a slight difference in its subunit organization. Catalytic domain has Zn²⁺ binding site. Matrilysins lack hinge region and hemopexin domain. Gelatinases (MMP-2 and MMP-9) contain three repeats of a fibronectin-like motif that bind gelatin. MMPs contain a specific recognition motif for intracellular furin-like serine proteinases (Fu) that allows intracellular activation by these proteinases. Membrane-type MMPs contain a transmembrane domain or a glycosylphosphatidylinositol anchor. MMP-23 has a unique cysteine-rich region and an immunoglobulin-like domain in the place of hemopexin domain.