Aliases for MMP16 Gene
- Matrix Metallopeptidase 16 (Membrane-Inserted) 2 3
- Membrane-Type Matrix Metalloproteinase 3 3 4
- Membrane-Type-3 Matrix Metalloproteinase 3 4
- MT-MMP 3 3 4
- MT3-MMP 3 4
- MMP-16 3 4
- MMP-X2 3 4
- MT3MMP 3 4
- MTMMP3 3 4
- Matrix Metalloproteinase 16 (Membrane-Inserted) 2
- Putative Transmembrane Protein C8orf57 3
External Ids for MMP16 Gene
Previous Symbols for MMP16 Gene
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The encoded protein activates MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16. [provided by RefSeq, Oct 2010]
GeneCards Summary for MMP16 Gene
MMP16 (Matrix Metallopeptidase 16 (Membrane-Inserted)) is a Protein Coding gene. Diseases associated with MMP16 include osteochondrosis and arthritis. Among its related pathways are MicroRNAs in cancer and Degradation of the extracellular matrix. GO annotations related to this gene include calcium ion binding and enzyme activator activity. An important paralog of this gene is MMP13.
UniProtKB/Swiss-Prot for MMP16 Gene
Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
Matrix metalloproteases (matrix metalloproteinase, MMPs), also called matrixins, are zinc-dependent endopeptidases that are the major proteases involved in ECM degradation. MMPs are capable of degrading a wide range of extracellular molecules and a number of bioactive molecules. 24 matrixin genes have been identified in humans, which can be organized into six groups based on domain organization and substrate preference: Collagenases (MMP-1, -8 and -13), Gelatinases (MMP-2 and MMP-9), Stromelysins (MMP-3, -10 and -11), Matrilysin (MMP-7 and MMP-26), Membrane-type (MT)-MMPs (MMP-14, -15, -16, -17, -24 and -25) and others (MMP-12, -19, -20, -21, -23, -27 and -28). MMP activity is regulated by two major endogenous inhibitors: alpha2-macroglobulin and tissue inhibitors of metalloproteases (TIMPs). MMPs play a central role in cell proliferation, migration, differentiation, angiogenesis, apoptosis and host defences. Dysregulatoin of MMPs has been implicated in many diseases including arthritis, chronic ulcers, encephalomyelitis and cancer. Tumour metastasis is a multistep process involving the dessemination of tumor cells from the primary tumor to secondarys at a distant organ or tissue. One of the first steps in metastasis is the degradation of the basement membrane, a process in which MMPs have been implicated. MMPs are secreted by tumor cells themselves or by surrounding stromal cells stimulated by the nearby tumor. Numerous studies have linked altered MMP expression in different human cancers with poor disease prognosis. MMP-1, -2, -3, -7, -9, -13 and -14 all have elevated expression in primary tumors and/or metastases. Synthetic or natural inhibitors of MMPs result in inhibition of metastasis, while up-regulation of MMPs led to enhanced cancer cell invasion.