CLG, CLGN, Matrix metalloproteinase-1, MMP-1.
CLG, CLGN, Matrix metalloproteinase-1, MMP-1.
Matrix Metalloproteinase-1 (MMP-1), also known as interstitial collagenase or collagenase-1, is a member of the matrix metalloproteinase (MMP) family. These enzymes are crucial for the degradation of extracellular matrix (ECM) components, playing significant roles in both physiological and pathological processes. MMP-1 is particularly known for its ability to degrade fibrillar collagens, which are major structural components of the ECM .
MMP-1, like other MMPs, is synthesized as an inactive zymogen. It contains a pro-peptide domain that must be cleaved to activate the enzyme. The pro-peptide domain includes a conserved cysteine residue that interacts with the zinc ion in the active site, keeping the enzyme inactive. Upon activation, the pro-peptide is removed, allowing the enzyme to cleave its substrates .
The active form of MMP-1 consists of three main domains:
MMP-1 plays a pivotal role in the remodeling of the extracellular matrix. It is capable of degrading type I, II, and III collagens, which are the most abundant collagens in the human body. This degradation is essential for various physiological processes, including tissue repair, embryonic development, and angiogenesis .
In addition to its physiological roles, MMP-1 is also involved in pathological conditions. Overexpression of MMP-1 has been linked to various diseases, such as arthritis, cancer, and cardiovascular diseases. In these conditions, excessive degradation of the ECM can lead to tissue damage and disease progression .
Recombinant MMP-1 is produced using genetic engineering techniques, where the human MMP-1 gene is inserted into a suitable expression system, such as bacteria or mammalian cells. This allows for the production of large quantities of the enzyme for research and therapeutic purposes. Recombinant MMP-1 is often used in studies to understand its structure, function, and role in various diseases .