MMP-3
MMP-3 (matrix metallopeptidase 3, also known as stromelysin-1, STMY1 or STMY) is a secreted zinc-dependent metalloproteinase of the M10 family. It degrades extracellular matrix components and activates growth factors, plasminogen and other matrix metalloproteinases. Browse Assay Genie's current range of MMP-3 research reagents below, or read on for the biology behind the target.
MMP-3 is a metalloproteinase with a rather broad substrate specificity. It can degrade fibronectin, laminin, gelatins of types I, III, IV and V, collagens III, IV, IX and X, and cartilage proteoglycans. It also activates other molecules, including growth factors, plasminogen and other matrix metalloproteinases such as MMP-9. Like most MMPs, it is released into the extracellular matrix as an inactive pro-enzyme, which is then activated through the plasmin cascade.
The enzyme also acts inside cells. In dopaminergic neurons, the serine protease HTRA2 activates MMP-3 under stress. There it contributes to neuronal degeneration by mediating microglial activation and cleavage of alpha-synuclein (SNCA). MMP-3 also plays a role in immune response and has antiviral activity against vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1. On viral infection it moves from the cytoplasm into the nucleus, where it influences NF-kappa-B activity.
The MMP3 gene belongs to the M10 matrix metallopeptidases gene group and encodes a member of the peptidase M10A family. It sits in a cluster of MMP genes on chromosome 11q. The MMP family is involved in extracellular matrix breakdown during embryonic development, reproduction and tissue remodelling, and in disease processes such as arthritis and metastasis. MMP-3 is thought to contribute to wound repair, progression of atherosclerosis and tumour initiation. Earlier names include matrix metalloproteinase 3 (stromelysin 1, progelatinase) and stromelysin 1.
MMP-3 degrades fibronectin, laminin, several collagens and cartilage proteoglycans, making it a key enzyme for studying matrix breakdown in development and tissue remodelling.
MMP family members are implicated in arthritis and metastasis, and MMP-3 is thought to be involved in tumour initiation.
MMP-3 is thought to be involved in wound repair and in the progression of atherosclerosis.
MMP-3 mediates microglial activation and alpha-synuclein cleavage in stressed dopaminergic neurons, and shows antiviral activity linked to NF-kappa-B.
MMP-3 is a broad-specificity metalloproteinase that degrades fibronectin, laminin, gelatins, several collagens and cartilage proteoglycans. It also activates growth factors, plasminogen and other MMPs such as MMP-9. It acts intracellularly too, in neuronal degeneration and in antiviral responses.
MMP-3 is also called stromelysin-1, with the gene aliases STMY1 and STMY. HGNC names it matrix metallopeptidase 3. Previous names include matrix metalloproteinase 3 (stromelysin 1, progelatinase) and stromelysin 1. It is secreted as an inactive pro-enzyme.
Yes. Mouse and rat both have an ortholog named Mmp3, so the protein can be studied in rodent models. MMP-3 has been linked to arthritis, atherosclerosis, tumour initiation and neuronal degeneration. Check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases, including stromelysins, collagenases and gelatinases, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P08254; product specifications from Assay Genie datasheets.