MMP-2
MMP-2 (matrix metallopeptidase 2, also known as gelatinase A, 72 kDa type IV collagenase, TBE-1, CLG4 and CLG4A) is a zinc-dependent endopeptidase of the matrix metalloproteinase family. It cleaves extracellular matrix components and molecules involved in signal transduction. Browse Assay Genie's current range of MMP-2 research reagents below, or read on for the biology behind the target.
MMP-2 is a member of the matrix metalloproteinase (MMP) family of zinc-dependent enzymes, which cleave components of the extracellular matrix and molecules involved in signal transduction. It is a gelatinase A and type IV collagenase. Its catalytic region contains three fibronectin type II repeats that allow binding of denatured type IV and V collagen and elastin. UniProt also annotates a role in mediating proteolysis of CHUK/IKKA, initiating a primary innate immune response by inducing mitochondrial-nuclear stress signalling and activating the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
Unlike most MMP family members, MMP-2 can be activated at the cell membrane. The enzyme can be activated extracellularly by proteases, or intracellularly by S-glutathiolation, which does not require proteolytic removal of the pro-domain. UniProt lists localisation in the extracellular matrix, membrane, nucleus, cytoplasm and mitochondrion. The protein belongs to the peptidase M10A family, and HGNC places the MMP2 gene in the M10 matrix metallopeptidases group. Alternative splicing produces multiple transcript variants encoding different isoforms.
The MMP-2 protein is thought to act in several pathways, including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularisation and metastasis. Mutations in the gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Earlier nomenclature described the gene as matrix metalloproteinase 2 (gelatinase A, 72 kDa gelatinase, 72 kDa type IV collagenase). Mouse and rat both carry an orthologous gene, Mmp2.
MMP-2 cleaves matrix components and binds denatured type IV and V collagen and elastin, making it a central enzyme in matrix turnover studies.
The protein is thought to contribute to metastasis, so MMP-2 is widely examined in studies of tumour invasion and matrix degradation.
MMP-2 is implicated in the regulation of vascularisation, which makes it relevant to work on vessel formation and remodelling.
MMP-2 proteolyses CHUK/IKKA and induces NF-kappaB, NFAT and IRF pathways, linking it to mitochondrial-nuclear stress and inflammation research.
MMP-2 is a zinc-dependent gelatinase that cleaves extracellular matrix components, including denatured type IV and V collagen and elastin, and molecules involved in signal transduction. It also proteolyses CHUK/IKKA, triggering NF-kappaB, NFAT and IRF signalling in an innate immune response.
MMP-2 is also called matrix metallopeptidase 2, gelatinase A, 72 kDa type IV collagenase, TBE-1, CLG4 and CLG4A. The official gene symbol is MMP2. Alternative splicing gives multiple transcript variants that encode different isoforms.
Mutations in the MMP2 gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. The protein is also thought to act in metastasis. Mouse and rat each have an Mmp2 ortholog; check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases, including gelatinases, collagenases and membrane-type MMPs, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P08253; product specifications from Assay Genie datasheets.