29Įnamelysin (MMP-20), which digests amelogenin, is primarily located within newly formed tooth enamel. MMP-19 was identified by cDNA cloning from liver 28 and as a T-cell–derived autoantigen from patients with rheumatoid arthritis (RASI). 27 Besides elastin, it digests a number of other proteins. Metalloelastase (MMP-12) is mainly expressed in macrophages 26 and is essential for macrophage migration. Seven MMPs are not classified in the above categories.

Pro–cat domain 1SLM cat domain D8M, 1CIZ, 1CAQ, 1B8Y, 2SRT, 1HFS, 1SLN, 2USN, 1USN, 1D5J, 1BQO, 1D7X, 1D8F, 1BIW, 1UMS, 3USN, 1UMT, 1BM6, 1B3D, 1CQR, 1G4K, 1G49, 1HY7, 1G05 complex with N-TIMP-1 1UEAĬat domain in complex with TIMP-2 1BQQ, 1BUV Pro–cat domain 1L6J cat domain 1GKC, 1GKD Hpx domain 1ITV ProMMP-2 1CK7 proMMP-2–TIMP-2 complex 1GXD cat domain 1QIB, 1HOV, 1EAK Hpx domain 1GEN, 1RTG Fn 1CXW, 1KS0 These files with their references can be downloaded from the protein databank (An extended version of this table including the substrates cleaved by the individual MMPs is available in online Table 1 (see online data supplement available at ). The names of the PDB files of structures determined by x-ray crystallography and NMR are listed. Groups of MMPs are listed with their trivial names and chromosomal location. An extended version of Table 1, including MMP substrates, is available in the online data supplement (available at ). On the basis of substrate specificity, sequence similarity, and domain organization, vertebrate MMPs can be divided into six groups (see Figure 1 and Table 1), as described below. They are either secreted from the cell or anchored to the plasma membrane. MMPs generally consist of a prodomain, a catalytic domain, a hinge region, and a hemopexin domain (see Figure 1). The exception is MMP-23, which lacks the cysteine switch motif, but its amino acid sequence of the catalytic domain is related to MMP-1.

11 The sequence homology with collagenase 1 (MMP-1), the cysteine switch motif PRCGXPD in the propeptide that maintains MMPs in their zymogen form (proMMP), and the zinc-binding motif HEXGHXXGXXH in the catalytic domain are the signatures used to assign proteinases to this family. Matrixins are also found in Hydra, 9 sea urchin, 10 and Arabidopsis. To date, 24 different vertebrate MMPs have been identified, of which 23 are found in humans. The first MMP activity discovered was a collagenase in the tail of a tadpole undergoing metamorphosis.

6–8 In the present review, we give an overview of structure, function, and biochemistry of MMPs and TIMPs. 4,5 The pathological effects of MMPs and TIMPs in cardiovascular disease processes that involve vascular remodeling, atherosclerotic plaque instability, and left ventricular remodeling after myocardial infarction are of considerable interest and are covered by other reviews in this series. 3 Tissue inhibitors of metalloproteinases (TIMPs) are specific inhibitors of matrixins that participate in controlling the local activities of MMPs in tissues. 1,2 A loss of activity control may result in diseases such as arthritis, cancer, atherosclerosis, aneurysms, nephritis, tissue ulcers, and fibrosis. 1,2 Under normal physiological conditions, the activities of MMPs are precisely regulated at the level of transcription, activation of the precursor zymogens, interaction with specific ECM components, and inhibition by endogenous inhibitors. Matrix metalloproteinases (MMPs), collectively called matrixins, are proteinases that participate in ECM degradation.

Customer Service and Ordering InformationĮxtracellular matrix (ECM) macromolecules are important for creating the cellular environments required during development and morphogenesis.

Stroke: Vascular and Interventional Neurology.

Journal of the American Heart Association (JAHA).

Circ: Cardiovascular Quality & Outcomes.

Arteriosclerosis, Thrombosis, and Vascular Biology (ATVB).

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