マトリックスメタロプロテアーゼ2

関: matrix metalloproteinase 2

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the 13th letter of the Roman alphabet (同)m

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Mach number / mark[s] / Monsieur

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/30 13:35:13」(JST)

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72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene.^[1]

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. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.^[2]

Activation[edit]

Activation of MMP-2 requires proteolytic processing. A complex of membrane type 1 MMP (MT1-MMP/MMP14) and tissue inhibitor of metalloproteinase 2 recruits pro-MMP 2 from the extracellular milieu to the cell surface. Activation then requires an active molecule of MT1-MMP and auto catalytic cleavage. Clustering of integrin chains promotes activation of MMP-2. Another factor that will support the activation of MMP-2 is cell-cell clustering. A wild-type activated leukocyte cell adhesion molecule (ALCAM) is also required to activate MMP-2.

Clinical significance[edit]

Mutations in the MMP2 gene are associated with Torg-Winchester syndrome, multicentric osteolysis, arthritis syndrome,^[3] and possibly keloids.

Interactions[edit]

MMP2 has been shown to interact with THBS2,^[4] TIMP2,^[5]^[6]^[7]^[8] Thrombospondin 1,^[4] CCL7^[9] and TIMP4.^[7]^[8]

References[edit]

^ Devarajan P, Johnston JJ, Ginsberg SS, Van Wart HE, Berliner N (December 1992). "Structure and expression of neutrophil gelatinase cDNA. Identity with type IV collagenase from HT1080 cells". J. Biol. Chem. 267 (35): 25228–32. PMID 1460022.
^ "Entrez Gene: MMP2 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)".
^ Martignetti JA, Aqeel AA, Sewairi WA, Boumah CE, Kambouris M, Mayouf SA, Sheth KV, Eid WA, Dowling O, Harris J, Glucksman MJ, Bahabri S, Meyer BF, Desnick RJ (July 2001). "Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome". Nat. Genet. 28 (3): 261–5. doi:10.1038/90100. PMID 11431697.
^ ^a ^b Bein K, Simons M (October 2000). "Thrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activity". J. Biol. Chem. 275 (41): 32167–73. doi:10.1074/jbc.M003834200. PMID 10900205.
^ Morgunova E, Tuuttila A, Bergmann U, Tryggvason K (May 2002). "Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7414–9. doi:10.1073/pnas.102185399. PMC 124245. PMID 12032297.
^ Overall CM, Tam E, McQuibban GA, Morrison C, Wallon UM, Bigg HF, King AE, Roberts CR (December 2000). "Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation". J. Biol. Chem. 275 (50): 39497–506. doi:10.1074/jbc.M005932200. PMID 10991943.
^ ^a ^b Bigg HF, Shi YE, Liu YE, Steffensen B, Overall CM (June 1997). "Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2". J. Biol. Chem. 272 (24): 15496–500. doi:10.1074/jbc.272.24.15496. PMID 9182583.
^ ^a ^b Kai HS, Butler GS, Morrison CJ, King AE, Pelman GR, Overall CM (December 2002). "Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain". J. Biol. Chem. 277 (50): 48696–707. doi:10.1074/jbc.M209177200. PMID 12374789.
^ McQuibban GA, Gong JH, Tam EM, McCulloch CA, Clark-Lewis I, Overall CM (August 2000). "Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3". Science 289 (5482): 1202–6. doi:10.1126/science.289.5482.1202. PMID 10947989.

External links[edit]

The MEROPS online database for peptidases and their inhibitors: M10.003

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English Journal

Ginkgolic Acid Inhibits Invasion and Migration and TGF-β-Induced EMT of Lung Cancer Cells Through PI3K/Akt/mTOR Inactivation.

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Journal of cellular physiology.J Cell Physiol.2017 Feb;232(2):346-354. doi: 10.1002/jcp.25426. Epub 2016 Jun 2.
Epithelial-to-mesenchymal transition (EMT) is a critical cellular phenomenon regulating tumor metastases. In the present study, we investigated whether ginkgolic acid can affect EMT in lung cancer cells and the related underlying mechanism(s) of its actions. We found that ginkgolic acid C15:1 (GA C1
PMID 27177359

Expression and localization of matrix metalloproteinases (MMP-2, -7, -9) and their tissue inhibitors (TIMP-2, -3) in the chicken oviduct during pause in laying induced by tamoxifen.

Leśniak-Walentyn A1, Hrabia A2.
Theriogenology.Theriogenology.2017 Jan 15;88:50-60. doi: 10.1016/j.theriogenology.2016.09.051. Epub 2016 Oct 6.
Induced pause in egg laying simulates natural molting events in which the hen's reproductive organs regress and rejuvenate. Such processes require extracellular matrix remodeling that is maintained, at least in part, by the action of proteolytic enzymes known as matrix metalloproteinases (MMPs). Nev
PMID 27865412

Silk-based biomaterials functionalized with fibronectin type II promotes cell adhesion.

Pereira AM1, Machado R2, da Costa A3, Ribeiro A3, Collins T3, Gomes AC3, Leonor IB4, Kaplan DL5, Reis RL4, Casal M6.
Acta biomaterialia.Acta Biomater.2017 Jan 1;47:50-59. doi: 10.1016/j.actbio.2016.10.002. Epub 2016 Oct 3.
The objective of this work was to exploit the fibronectin type II (FNII) module from human matrix metalloproteinase-2 as a functional domain for the development of silk-based biopolymer blends that display enhanced cell adhesion properties. The DNA sequence of spider dragline silk protein (6mer) was
PMID 27713086

Japanese Journal

Berberine Attenuates Vascular Remodeling and Inflammation in a Rat Model of Metabolic Syndrome

, , , , , , ,
Biological and Pharmaceutical Bulletin 38(6), 862-868, 2015
… In addition, the levels of p38 mitogen-activated protein kinase (p38 MAPK), activating transcription factor 2 (ATF-2) and matrix metalloproteinase 2 (MMP-2) were significantly decreased in the MS+B group compared to the MS group. …
NAID 130005072665

Different Responses in MMP/TIMP Expression of U937 and HepG2 Cells to Dengue Virus Infection

, , , ,
Japanese Journal of Infectious Diseases 68(3), 221-229, 2015
… A previous study reported that supernatants of DV-infected dendritic cells (DCs), which contained high levels of MMP-2 and MMP-9, induced vascular leakage in a mouse model. … In the present study, we investigated whether hepatocytes (HepG2) and monocytes (U937) could be additional sources of MMPs during DV infection. … HepG2 and U937 cells were exposed to DV serotype 2 strain 16681. …
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, , , , , , , , , ,
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… EPA administration and DHA administration significantly decreased the expression of tumor necrosis factor-α, monocyte chemoattractant protein-1, transforming growth factor-β, matrix metalloproteinases (MMP)-2, MMP-9, and vascular cell adhesion molecule-1 in the aortas. …
NAID 130005068466

「matrix metalloproteinase 2」

Matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)
	; PDB rendering based on 1ck7.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1CK7, 1CXW, 1EAK, 1GEN, 1GXD, 1HOV, 1J7M, 1KS0, 1QIB, 1RTG, 3AYU
Identifiers
Symbols	MMP2; CLG4; CLG4A; MMP-II; MONA; TBE-1
External IDs	OMIM: 120360 MGI: 97009 HomoloGene: 3329 ChEMBL: 333 GeneCards: MMP2 Gene
EC number	3.4.24.24
Gene Ontology
Molecular function	• metalloendopeptidase activity; • serine-type endopeptidase activity; • protein binding; • zinc ion binding;
Cellular component	• extracellular region; • proteinaceous extracellular matrix; • extracellular space; • nucleus; • mitochondrion; • plasma membrane; • sarcomere;
Biological process	• angiogenesis; • response to hypoxia; • blood vessel maturation; • intramembranous ossification; • proteolysis; • embryo implantation; • extracellular matrix disassembly; • extracellular matrix organization; • collagen catabolic process; • cellular protein metabolic process; • face morphogenesis; • bone trabecula formation; • cellular response to amino acid stimulus;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

マトリックスメタロプロテアーゼ2、マトリックスメタロプロテイナーゼ2

関: gelatinase A、MMP-2

「マトリックスメタロプロテアーゼ2」

　　[★]

英: matrix metalloproteinase 2、MMP-2
関: マトリックスメタロプロテイナーゼ2

「MMP-20」

　　[★]

マトリックスメタロプロテアーゼ20

関: matrix metalloproteinase 20

「MM」

　　[★]

「MMP」

　　[★] マトリックスメタロプロテアーゼ matrix metalloproteinase

「MMPs」

　　[★] マトリックスメタロプロテアーゼ

「M」

　　[★] メチオニン methionine 　　

[pmid1460022-1] Devarajan P, Johnston JJ, Ginsberg SS, Van Wart HE, Berliner N (December 1992). "Structure and expression of neutrophil gelatinase cDNA. Identity with type IV collagenase from HT1080 cells". J. Biol. Chem. 267 (35): 25228–32. PMID 1460022.

[2] "Entrez Gene: MMP2 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)".

[pmid11431697-3] Martignetti JA, Aqeel AA, Sewairi WA, Boumah CE, Kambouris M, Mayouf SA, Sheth KV, Eid WA, Dowling O, Harris J, Glucksman MJ, Bahabri S, Meyer BF, Desnick RJ (July 2001). "Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome". Nat. Genet. 28 (3): 261–5. doi:10.1038/90100. PMID 11431697.

[pmid10900205-4] Bein K, Simons M (October 2000). "Thrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activity". J. Biol. Chem. 275 (41): 32167–73. doi:10.1074/jbc.M003834200. PMID 10900205.

[pmid12032297-5] Morgunova E, Tuuttila A, Bergmann U, Tryggvason K (May 2002). "Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7414–9. doi:10.1073/pnas.102185399. PMC 124245. PMID 12032297.

[pmid10991943-6] Overall CM, Tam E, McQuibban GA, Morrison C, Wallon UM, Bigg HF, King AE, Roberts CR (December 2000). "Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation". J. Biol. Chem. 275 (50): 39497–506. doi:10.1074/jbc.M005932200. PMID 10991943.

[pmid9182583-7] Bigg HF, Shi YE, Liu YE, Steffensen B, Overall CM (June 1997). "Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2". J. Biol. Chem. 272 (24): 15496–500. doi:10.1074/jbc.272.24.15496. PMID 9182583.

[pmid12374789-8] Kai HS, Butler GS, Morrison CJ, King AE, Pelman GR, Overall CM (December 2002). "Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain". J. Biol. Chem. 277 (50): 48696–707. doi:10.1074/jbc.M209177200. PMID 12374789.

[pmid10947989-9] McQuibban GA, Gong JH, Tam EM, McCulloch CA, Clark-Lewis I, Overall CM (August 2000). "Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3". Science 289 (5482): 1202–6. doi:10.1126/science.289.5482.1202. PMID 10947989.

リンク元	「matrix metalloproteinase 2」「マトリックスメタロプロテアーゼ2」
拡張検索	「MMP-20」
関連記事	「MM」「MMP」「MMPs」「M」

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案内

MMP-2