General information on MMP Protein
MMP protein stands for matrix metallopeptidases, matrix metalloproteinases or matrixins which are calcium-dependent zinc-containing endopeptidases. MMPs proteins are capable of degrading different protein components of the Extracellular Matrix. Data has shown (Wilson et al. 1997) that MMP protein knockout indicate that these proteinases act on a variety of extracellular proteins such as cytokines, chemokines, antimicrobial peptides. They are also involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand). MMPs proteins are believed to play a major role in cell behaviors such as cell differentiation, proliferation, migration, apoptosis, angiogenesis and host defense. MMPs carry out effector roles in a variety of biological and disease processes including inflammation and immunity. MMPs proteins are secreted and anchored to the surface of the cell.
MMP1 protein, which is also known as interstitial collagenase and fibroblast collagenase, is an enzyme involved in collagen degradation. More precisely, MMP-1 breaks down the interstitial collagens, types I, II and III, VII and X. MPP1 protein has also been shown to interact with CD49b. MMP1 protein has an archetypal structure consisting of a pre-domain, a pro-domain, a catalytic domain, a hemopexin-like domain and a linker region. The Catalytic Domain of MMP-1 is composed of five β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing three Ca2+ metal ions and two Zn2+ metal ions.
In case of an increase of the mechanical force, the expression of MMP1 in human periodontal ligament may also be increases. In case of HIV infection, interacts and cleaves the viral Tat protein. This step leads to a decrease in neuronal Tat’s mediated neurotoxicity. High MPP1 protein expression levels have been associated with enhanced breast cancer growth and metastasis. MMP1 overexpression has been linked to significantly reduced drug sensitivity and may also predict poor prognosis.
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