MMP14
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Official Full Name
matrix metallopeptidase 14 (membrane-inserted)
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Overview
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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion. [provided by RefSeq, Jul 2008] -
Synonyms
MMP14; matrix metallopeptidase 14 (membrane-inserted); MMP-14; MMP-X1; MT-MMP; MT1MMP; MTMMP1; WNCHRS; MT1-MMP; MT-MMP 1; matrix metalloproteinase-14; membrane type 1 metalloprotease; membrane-type-1 matrix metalloproteinase; 1;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Assay Kits
- Homo sapiens (Human)
- Human
- Mouse
- Mus musculus (Mouse)
- Rat
- Rhesus Macaque
- Rhesus monkey
- E.coli
- E.coli expression system
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mammalian Cell
- Mammalian cells
- Wheat Germ
- Flag
- GST
- His
- His (Fc)
- Avi
- SUMO
- Myc
- DDK
- Myc|DDK
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
- MMP14 Related Articles
- MMP14 Related Gene Family
- MMP14 Related Research Area
MMP14 involved in several pathways and played different roles in them. We selected most pathways MMP14 participated on our site, such as TNF signaling pathway, GnRH signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with MMP14 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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TNF signaling pathway | SOCS3;RPS6KA5;CXCL3;CASP10;VCAM1;PIK3R5;CXCL10;TRAF2;TRAF1 |
GnRH signaling pathway | CACNA1DA;GRB2A;EGFRA;FSHB;MAPK9;MMP2;PRKACBB;ADCY1A;HRAS |
MMP14 has several biochemical functions, for example, calcium ion binding, integrin binding, metalloendopeptidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by MMP14 itself. We selected most functions MMP14 had, and list some proteins which have the same functions with MMP14. You can find most of the proteins on our site.
Function | Related Protein |
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calcium ion binding | ATP2C1;DSG3;GUCA1B;KCNIP1;S100A12;PCDHAC2;SYT11A;GUCA1E;CELSR3 |
integrin binding | L1CAM;ADAM9;GFAP;VWF;NF2;TSPAN4;LAMB1;S1PR3;NISCH |
metalloendopeptidase activity | ADAMTS13;Adamts19;ADAM9;HE1A;ADAM12;MMP2;MEP1B;ADAM5;OSGEPL1 |
peptidase activator activity | PCOLCE2;PCOLCE;MMP14;PSME4B;FN1;FBLN1;PINK1;APP;PSME4 |
protein binding | RASSF1;HUS1;C5orf20;NRG4;PDPK1;GAD1;IFT88;DHX58;PKIA |
zinc ion binding | RNF150;RBM20;ZCWPW1;AFG3L2;RBM4.2;ABLIM2;RERE;VPS41;LHX2 |
MMP14 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MMP14 here. Most of them are supplied by our site. Hope this information will be useful for your research of MMP14.
ADI1; Gorasp2; LUM
- Q&As
- Reviews
Q&As (7)
Ask a questionMMP14, also known as matrix metalloproteinase 14, is primarily expressed by cells of mesenchymal origin, such as fibroblasts and endothelial cells. Its expression is tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms. Transcriptional regulation involves the binding of various transcription factors, such as AP-1 and SP-1, to the MMP14 promoter region. Additionally, microRNAs and RNA-binding proteins can modulate its mRNA stability and translation.
MMP14 plays a crucial role in cancer progression and metastasis. It facilitates tumor invasion by degrading components of the extracellular matrix, promoting cancer cell migration, and aiding in angiogenesis. MMP14 also influences tumor cell behavior by interacting with other proteins involved in cell signaling pathways and epithelial-mesenchymal transition. Its overexpression is associated with poor prognosis in various types of cancer.
Overexpression of MMP14 has been strongly associated with tumor progression and poor prognosis in various types of cancer. Increased levels of MMP14 lead to enhanced degradation of the ECM, promoting tumor cell invasion and metastasis. Additionally, MMP14 can activate other matrix metalloproteinases (MMPs), further amplifying the proteolytic activity and facilitating tumor growth and angiogenesis. Moreover, MMP14 has been implicated in tumor-associated angiogenesis and immunosuppression, contributing to tumor progression and metastasis.
Targeting MMP14 holds potential for therapeutic interventions in cancer and other diseases. Strategies such as selective inhibition of MMP14 activity, antibody-based therapies, and gene silencing techniques are being explored. However, the development of MMP14-targeted therapies faces challenges, including the need for specificity, avoiding off-target effects, and optimizing delivery methods to reach the tumor microenvironment.
Yes, there are endogenous inhibitors of MMP14, known as tissue inhibitors of metalloproteinases (TIMPs). TIMPs bind to the active site of MMP14 and prevent its activity. TIMP-2 is a specific inhibitor of MMP14 and forms a complex with MMP14, regulating its enzymatic activity. The balance between MMP14 and TIMPs is crucial for maintaining tissue homeostasis and preventing excessive extracellular matrix degradation. Dysregulation of this balance can contribute to pathological conditions, including cancer progression.
MMP14 plays a crucial role in tissue remodeling processes, such as embryogenesis, wound healing, and tissue repair. It is essential for the degradation and turnover of extracellular matrix components during tissue restructuring. MMP14 also influences cell behavior and migration during tissue development and regeneration. Additionally, it participates in the modulation of immune responses and angiogenesis, which are crucial for proper tissue remodeling.
MMP14 possesses a catalytic domain responsible for substrate cleavage. It predominantly cleaves components of the extracellular matrix, such as collagen type I and type II. The interaction between MMP14 and its substrates occurs through specific binding sites within the substrate proteins. This interaction is facilitated by the hemopexin-like domain of MMP14, which acts as a docking site for substrate recognition and binding.
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