LaurenJansen/Sandbox1
From Proteopedia
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One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
| + | Molecular Playground banner: '''"MMP-14 allows for 3D ''in vitro'' cell migration"''' | ||
| - | Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) is 1 of ~ | + | ==Structure== |
| + | Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) is 1 of ~24 members of the MMP family of endopeptidases. MMPs are zinc dependent proteinases that are capable of degrading virtually any extracellular matrix component [1]. Inherently, this enables MMPs to be a key player in regulation of cell behavior. There are 8 structure classes for MMPs, of which 5 are secreted molecules and 3 are membrane-type [2]. MT1-MMP or also known as MMP-14 is covalently linked to the cell membrane. | ||
| - | There are 8 structure classes for MMPs, of which 5 are secreted molecules and 3 are membrane-type. MT1-MMP or also known as MMP-14 is covalently bound to the cell membrane and | ||
| + | <Structure load='3C7X' size='400' frame='true' align='right' caption='PBD file obtained from http://pdb.org/pdb/explore/explore.do?structureId=3C7X ' scene='Insert optional scene name here' /> | ||
| - | <Structure load='3C7X' size='400' frame='true' align='right' caption='PBD file obtained from http://pdb.org/pdb/explore/explore.do?structureId=1bqq ' scene='Insert optional scene name here' /> | ||
| - | |||
| - | ==Structure== | ||
==Inhibition== | ==Inhibition== | ||
| - | < | + | |
| + | Tissue inhibitors of metalloproteinases (TIMPs) are small molecules that can regulate the activity of MMPs. A unique relationship exists between TIMP-2 and MMP-14 where TIMP-2 <scene name='56/566496/Timp1_bind_mmp1/1'>binds</scene> the MMP-14 and allows MMP-2 to be activated [3]. | ||
| + | |||
==Extracellular Matrix Components== | ==Extracellular Matrix Components== | ||
| - | + | MMP-14 degrades the following substrates in the extracellular matrix [2]: | |
| - | In the [http://www.peytonlab.org/ Peyton Lab] I work to combine materials science with stem cell and cancer biology to design in vitro model biomaterial systems to understand cell motility. My project aims to design 3D biomaterial tissue mimics using poly(ethylene glycol) and I incorporate degradable MMP crosslinkers into these materials to allow cells the opportunity to remodel their surrounding matrix. | + | :Aggrecan |
| + | :Collagen I | ||
| + | :Collagen II | ||
| + | :Collagen III | ||
| + | :Entactin/Nidogen | ||
| + | :Fibrillin | ||
| + | :Fibronectin | ||
| + | :Gelatin I | ||
| + | :Laminin | ||
| + | :Vitronectin | ||
| + | :α2-M | ||
| + | :α1-PI | ||
| + | :Factor XII | ||
| + | :Fibrin | ||
| + | :Fibrinogen | ||
| + | :ProMMP2 | ||
| + | :ProTNFα | ||
| + | |||
| + | ==My Research Interest== | ||
| + | |||
| + | In the [http://www.peytonlab.org/ Peyton Lab] I work to combine materials science with stem cell and cancer biology to design ''in vitro'' model biomaterial systems to understand cell motility. My project aims to design 3D biomaterial tissue mimics using poly(ethylene glycol) and I incorporate degradable MMP crosslinkers into these materials to allow cells the opportunity to remodel their surrounding matrix. | ||
| + | |||
| + | ==References== | ||
| - | + | [1] L. Coussens, et al., Matrix Metalloproteinase Inhibitors and Cancer: Trials and Tribulations, Science, 2002. 295: p. 2387-92 | |
| - | + | ||
| - | + | [2] M. Sternlicht, et al., How Matrix Metalloproteinases Regulate Cell Behavior, Annu Rev Cell Dev Biol, 2001. 17: p. 463–516. | |
| - | + | [3] Egeblad, et. al., New Functions for the Matrix Metalloproteinases in Cancer Progression, Nat. Rev. Can., 2002, 2: 162-74 | |
Current revision
Contents |
Membrane Type 1 Matrix Metalloproteinase
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground. Molecular Playground banner: "MMP-14 allows for 3D in vitro cell migration"
Structure
Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) is 1 of ~24 members of the MMP family of endopeptidases. MMPs are zinc dependent proteinases that are capable of degrading virtually any extracellular matrix component [1]. Inherently, this enables MMPs to be a key player in regulation of cell behavior. There are 8 structure classes for MMPs, of which 5 are secreted molecules and 3 are membrane-type [2]. MT1-MMP or also known as MMP-14 is covalently linked to the cell membrane.
|
Inhibition
Tissue inhibitors of metalloproteinases (TIMPs) are small molecules that can regulate the activity of MMPs. A unique relationship exists between TIMP-2 and MMP-14 where TIMP-2 the MMP-14 and allows MMP-2 to be activated [3].
Extracellular Matrix Components
MMP-14 degrades the following substrates in the extracellular matrix [2]:
- Aggrecan
- Collagen I
- Collagen II
- Collagen III
- Entactin/Nidogen
- Fibrillin
- Fibronectin
- Gelatin I
- Laminin
- Vitronectin
- α2-M
- α1-PI
- Factor XII
- Fibrin
- Fibrinogen
- ProMMP2
- ProTNFα
My Research Interest
In the Peyton Lab I work to combine materials science with stem cell and cancer biology to design in vitro model biomaterial systems to understand cell motility. My project aims to design 3D biomaterial tissue mimics using poly(ethylene glycol) and I incorporate degradable MMP crosslinkers into these materials to allow cells the opportunity to remodel their surrounding matrix.
References
[1] L. Coussens, et al., Matrix Metalloproteinase Inhibitors and Cancer: Trials and Tribulations, Science, 2002. 295: p. 2387-92
[2] M. Sternlicht, et al., How Matrix Metalloproteinases Regulate Cell Behavior, Annu Rev Cell Dev Biol, 2001. 17: p. 463–516.
[3] Egeblad, et. al., New Functions for the Matrix Metalloproteinases in Cancer Progression, Nat. Rev. Can., 2002, 2: 162-74
