What are MMP substrates?
The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, Fibronectin, Laminin and proteoglycan. In stock MMP Substrates are available for immediate shipping. …
What does MMP 7 do?
MMP-7 plays a role in remodeling of tissues involved in development and reproduction such as the uterus, and could play a role in remodeling following tissue injury. MMP-7 degrades ECM components and cleaves cell-surface molecules such as Fas–ligand, pro-TNF-α, syndecan-1, and E-cadherin to generate soluble forms.
What is MMP made of?
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade various proteins in the extracellular matrix (ECM). Typically, MMPs have a propeptide sequence, a catalytic metalloproteinase domain with catalytic zinc, a hinge region or linker peptide, and a hemopexin domain.
Are MMPs cytokines?
Matrix metalloproteinases (MMPs) are involved in tissue remodeling and disease processes such as arthritis and cancer. In addition to modifying extracellular matrix proteins, MMPs are intimately involved in the regulation of the activities of cytokines and cytokine receptors.
What do metalloproteinases do?
A member of a group of enzymes that can break down proteins, such as collagen, that are normally found in the spaces between cells in tissues (i.e., extracellular matrix proteins). Because these enzymes need zinc or calcium atoms to work properly, they are called metalloproteinases.
What do MMPs cleave?
MMPs may be described as multifunctional enzymes capable of cleaving the extracellular matrix components (collagens, laminin, fibronectin, vitronectin, aggrecan, enactin, versican, perlecan, tenascin, elastin and many others), growth factors, cytokines and cell surface-associated adhesion and signaling receptors.
What is the structure of MMP7?
MMP genes are clustered in q region of human Chromosome 11 including matrilysin, collagenase-1, stromelysin1, stromelysin-2, and metalloelastase genes. It consists of 267 amino acids. The cDNA of MMP7 is 49% homologous to stromelysin-1. Comparing to other members of MMP family, MMP7 does not have a C-terminal protein domain.
What is the optimal pH of MMP7?
MMP7 was initially characterized by Woessner et al. It digests components of the extracellular matrix, cleaves the α 2 (I) chain of gelatin more rapidly, and digests the B chain of insulin at Ala 14 -Leu and Tyr 16 -Leu, and has no action on collagen types I, II, IV, V. The optimal pH of MMP7 is at 7 and the pI is at 5.9.
What are MMP inhibitors and how do they work?
MMP7 cleaves collagen III/IV/V/IX/X/XI and proteoglycan indicating that MMP inhibitors can potentially be used in therapies that are involved in inhibition of tissue degradation, remodeling, anti-angiogenesis and inhibition of tumor invasion. MMP7 is found to potentially be involved in tumor metastasis and inflammatory processes.
What is the cysteine switch in MMP7?
The prodoamin of MMP7 contains an approximately 9 kD highly conserved “cysteine switch” PRCGXPD sequence near the C-terminal containing cysteine residues. Cysteine residues bind to the catalytic zinc keeping the protein latent.