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{{ | '''Matrix metalloproteinase-25''' is an [[enzyme]] that in humans is encoded by the ''MMP25'' [[gene]].<ref name="pmid10628838">{{cite journal | author = Pei D | title = Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage | journal = Cell Res | volume = 9 | issue = 4 | pages = 291–303 |date=Feb 2000 | pmid = 10628838 | pmc = | doi = 10.1038/sj.cr.7290028 }}</ref><ref name="pmid10706098">{{cite journal |vauthors=Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C | title = Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors | journal = Cancer Res | volume = 60 | issue = 4 | pages = 877–82 |date=Mar 2000 | pmid = 10706098 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MMP25 matrix metallopeptidase 25| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64386| accessdate = }}</ref> | ||
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| summary_text = 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, attached to the plasma membrane via a glycosylphosphatidyl inositol anchor. In response to bacterial infection or inflammation, the encoded protein is thought to inactivate alpha-1 proteinase inhibitor, a major tissue protectant against proteolytic enzymes released by activated neutrophils, facilitating the transendothelial migration of neutrophils to inflammatory sites. The encoded protein may also play a role in tumor invasion and metastasis through activation of MMP2. The gene has previously been referred to as MMP20 but has been renamed MMP25.<ref name="entrez">{{cite web | title = Entrez Gene: MMP25 matrix metallopeptidase 25| url = | | summary_text = 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, attached to the plasma membrane via a glycosylphosphatidyl inositol anchor. In response to bacterial infection or inflammation, the encoded protein is thought to inactivate alpha-1 proteinase inhibitor, a major tissue protectant against proteolytic enzymes released by activated neutrophils, facilitating the transendothelial migration of neutrophils to inflammatory sites. The encoded protein may also play a role in tumor invasion and metastasis through activation of MMP2. The gene has previously been referred to as MMP20 but has been renamed MMP25.<ref name="entrez">{{cite web | title = Entrez Gene: MMP25 matrix metallopeptidase 25| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64386| accessdate = }}</ref> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal |vauthors=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=10.1074/jbc.274.31.21491 }} | ||
*{{cite journal | *{{cite journal |vauthors=Will H, Atkinson SJ, Butler GS, etal |title=The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17119–23 |year= 1996 |pmid= 8663332 |doi=10.1074/jbc.271.29.17119 }} | ||
*{{cite journal | *{{cite journal |vauthors=Bernot A, Heilig R, Clepet C, etal |title=A transcriptional Map of the FMF region. |journal=Genomics |volume=50 |issue= 2 |pages= 147–60 |year= 1998 |pmid= 9653642 |doi=10.1006/geno.1998.5313 }} | ||
*{{cite journal |vauthors=Kojima S, Itoh Y, Matsumoto S, etal |title=Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP. |journal=FEBS Lett. |volume=480 |issue= 2-3 |pages= 142–6 |year= 2000 |pmid= 11034316 |doi=10.1016/S0014-5793(00)01919-0 }} | |||
*{{cite journal |vauthors=English WR, Velasco G, Stracke JO, etal |title=Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25). |journal=FEBS Lett. |volume=491 |issue= 1-2 |pages= 137–42 |year= 2001 |pmid= 11226436 |doi=10.1016/S0014-5793(01)02150-0 }} | |||
*{{cite journal | *{{cite journal |vauthors=Kang T, Yi J, Guo A, etal |title=Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils. |journal=J. Biol. Chem. |volume=276 |issue= 24 |pages= 21960–8 |year= 2001 |pmid= 11282999 |doi= 10.1074/jbc.M007997200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} | ||
*{{cite journal | *{{cite journal |vauthors=Shin BK, Wang H, Yim AM, etal |title=Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7607–16 |year= 2003 |pmid= 12493773 |doi= 10.1074/jbc.M210455200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Matsuda A, Itoh Y, Koshikawa N, etal |title=Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils. |journal=J. Biol. Chem. |volume=278 |issue= 38 |pages= 36350–7 |year= 2003 |pmid= 12860995 |doi= 10.1074/jbc.M301509200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Nie J, Pei D |title=Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond. |journal=Cancer Res. |volume=63 |issue= 20 |pages= 6758–62 |year= 2003 |pmid= 14583471 |doi= }} | ||
*{{cite journal | *{{cite journal |vauthors=Blanton SH, Bertin T, Serna ME, etal |title=Association of chromosomal regions 3p21.2, 10p13, and 16p13.3 with nonsyndromic cleft lip and palate. |journal=Am. J. Med. Genet. A |volume=125 |issue= 1 |pages= 23–7 |year= 2004 |pmid= 14755462 |doi= 10.1002/ajmg.a.20426 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Nie J, Pei D |title=Rapid inactivation of alpha-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6. |journal=Exp. Cell Res. |volume=296 |issue= 2 |pages= 145–50 |year= 2004 |pmid= 15149845 |doi= 10.1016/j.yexcr.2004.02.008 }} | ||
*{{cite journal | *{{cite journal |vauthors=Sun Q, Weber CR, Sohail A, etal |title=MMP25 (MT6-MMP) is highly expressed in human colon cancer, promotes tumor growth, and exhibits unique biochemical properties. |journal=J. Biol. Chem. |volume=282 |issue= 30 |pages= 21998–2010 |year= 2007 |pmid= 17513868 |doi= 10.1074/jbc.M701737200 | pmc=1978545 }} | ||
*{{cite journal | | |||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{ | ==External links== | ||
{{ | * The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.024 M10.024] | ||
{{Metalloendopeptidases}} | |||
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[[Category:Matrix metalloproteinases]] | |||
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Matrix metalloproteinase-25 is an enzyme that in humans is encoded by the MMP25 gene.[1][2][3]
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, attached to the plasma membrane via a glycosylphosphatidyl inositol anchor. In response to bacterial infection or inflammation, the encoded protein is thought to inactivate alpha-1 proteinase inhibitor, a major tissue protectant against proteolytic enzymes released by activated neutrophils, facilitating the transendothelial migration of neutrophils to inflammatory sites. The encoded protein may also play a role in tumor invasion and metastasis through activation of MMP2. The gene has previously been referred to as MMP20 but has been renamed MMP25.[3]
References
- ↑ Pei D (Feb 2000). "Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage". Cell Res. 9 (4): 291–303. doi:10.1038/sj.cr.7290028. PMID 10628838.
- ↑ Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C (Mar 2000). "Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors". Cancer Res. 60 (4): 877–82. PMID 10706098.
- ↑ 3.0 3.1 "Entrez Gene: MMP25 matrix metallopeptidase 25".
Further reading
- Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
- Will H, Atkinson SJ, Butler GS, et al. (1996). "The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3". J. Biol. Chem. 271 (29): 17119–23. doi:10.1074/jbc.271.29.17119. PMID 8663332.
- Bernot A, Heilig R, Clepet C, et al. (1998). "A transcriptional Map of the FMF region". Genomics. 50 (2): 147–60. doi:10.1006/geno.1998.5313. PMID 9653642.
- Kojima S, Itoh Y, Matsumoto S, et al. (2000). "Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP". FEBS Lett. 480 (2–3): 142–6. doi:10.1016/S0014-5793(00)01919-0. PMID 11034316.
- English WR, Velasco G, Stracke JO, et al. (2001). "Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25)". FEBS Lett. 491 (1–2): 137–42. doi:10.1016/S0014-5793(01)02150-0. PMID 11226436.
- Kang T, Yi J, Guo A, et al. (2001). "Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils". J. Biol. Chem. 276 (24): 21960–8. doi:10.1074/jbc.M007997200. PMID 11282999.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function". J. Biol. Chem. 278 (9): 7607–16. doi:10.1074/jbc.M210455200. PMID 12493773.
- Matsuda A, Itoh Y, Koshikawa N, et al. (2003). "Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils". J. Biol. Chem. 278 (38): 36350–7. doi:10.1074/jbc.M301509200. PMID 12860995.
- Nie J, Pei D (2003). "Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond". Cancer Res. 63 (20): 6758–62. PMID 14583471.
- Blanton SH, Bertin T, Serna ME, et al. (2004). "Association of chromosomal regions 3p21.2, 10p13, and 16p13.3 with nonsyndromic cleft lip and palate". Am. J. Med. Genet. A. 125 (1): 23–7. doi:10.1002/ajmg.a.20426. PMID 14755462.
- Nie J, Pei D (2004). "Rapid inactivation of alpha-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6". Exp. Cell Res. 296 (2): 145–50. doi:10.1016/j.yexcr.2004.02.008. PMID 15149845.
- Sun Q, Weber CR, Sohail A, et al. (2007). "MMP25 (MT6-MMP) is highly expressed in human colon cancer, promotes tumor growth, and exhibits unique biochemical properties". J. Biol. Chem. 282 (30): 21998–2010. doi:10.1074/jbc.M701737200. PMC 1978545. PMID 17513868.
External links
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