MMP10

MMP10
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1Q3A, 3V96, 4ILW
Identifiers
Aliases	MMP10, SL-2, STMY2, matrix metallopeptidase 10
External IDs	OMIM: 185260 MGI: 97007 HomoloGene: 20546 GeneCards: MMP10
EC number	3.4.24.22
Gene location (Human)
Chr.	Chromosome 11 (human)
End	102,780,628 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	7,510,241 bp
RNA expression pattern
	Top expressed in
	palpebral conjunctiva; ; islet of Langerhans; ; stromal cell of endometrium; ; pancreatic epithelial cell; ; Achilles tendon; ; appendix; ; amniotic fluid; ; periodontal fiber; ; bronchial epithelial cell; ; trachea;
	Top expressed in
	duodenum; ; jejunum; ; Paneth cell; ; ileum; ; colon; ; ovary; ; muscle of leg; ; uterus; ; integument; ; integument;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	zinc ion binding; peptidase activity; metalloendopeptidase activity; hydrolase activity; metallopeptidase activity; metal ion binding; serine-type endopeptidase activity;
Cellular component	extracellular region; extracellular space; extracellular matrix;
Biological process	collagen catabolic process; extracellular matrix disassembly; regulation of cell migration; proteolysis; response to hypoxia; extracellular matrix organization;
	Sources:Amigo / QuickGO
Orthologs
	4319
	17384
	ENSG00000166670
	ENSMUSG00000047562
	P09238
	O55123
	NM_002425
	NM_019471
	NP_002416
	NP_062344
	Wikidata
View/Edit Human	View/Edit Mouse

Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene.^[5]^[6]

Function

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. The enzyme encoded by this gene degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.^[7]

Clinical significance

MMP10 has been linked to cancer stem cell vitality and metastasis.^[8]

MMP10 is a potential prognostic biomarker for oral cancer.^[9]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000166670 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047562 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988). "The collagenase gene family in humans consists of at least four members". The Biochemical Journal. 253 (1): 187–92. doi:10.1042/bj2530187. PMC 1149273. PMID 2844164.
↑ Jung JY, Warter S, Rumpler Y (1990). "Localization of stromelysin 2 gene to the q22.3-23 region of chromosome 11 by in situ hybridization". Annales de Génétique. 33 (1): 21–3. PMID 2369069.
↑ "Entrez Gene: MMP10 matrix metallopeptidase 10 (stromelysin 2)".
↑ Justilien V, Regala RP, Tseng IC, Walsh MP, Batra J, Radisky ES, Murray NR, Fields AP (2012). "Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential". PLOS ONE. 7 (4): e35040. Bibcode:2012PLoSO...735040J. doi:10.1371/journal.pone.0035040. PMC 3335833. PMID 22545096.
↑ Upadhyay P, Gardi N, Desai S, Chandrani P, Joshi A, Dharavath B, Arora P, Bal M, Nair S, Dutt A (2017). "Genomic characterization of tobacco/nut chewing HPV-negative early stage tongue tumors identify MMP10 asa candidate to predict metastases". Oral Oncology. 73: 56–64. doi:10.1016/j.oraloncology.2017.08.003. PMC 5628952. PMID 28939077.

Chandler S, Miller KM, Clements JM, Lury J, Corkill D, Anthony DC, Adams SE, Gearing AJ (February 1997). "Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview". Journal of Neuroimmunology. 72 (2): 155–61. doi:10.1016/S0165-5728(96)00179-8. PMID 9042108. S2CID 26495949.
Nagase H, Woessner JF (July 1999). "Matrix metalloproteinases". The Journal of Biological Chemistry. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
Fosang AJ, Neame PJ, Hardingham TE, Murphy G, Hamilton JA (August 1991). "Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins". The Journal of Biological Chemistry. 266 (24): 15579–82. doi:10.1016/S0021-9258(18)98442-5. PMID 1874716.
Sirum KL, Brinckerhoff CE (October 1989). "Cloning of the genes for human stromelysin and stromelysin 2: differential expression in rheumatoid synovial fibroblasts". Biochemistry. 28 (22): 8691–8. doi:10.1021/bi00448a004. PMID 2605216.
Lichtinghagen R, Helmbrecht T, Arndt B, Böker KH (February 1995). "Expression pattern of matrix metalloproteinases in human liver". European Journal of Clinical Chemistry and Clinical Biochemistry. 33 (2): 65–71. CiteSeerX 10.1.1.633.9185. doi:10.1515/cclm.1995.33.2.65. PMID 7632822. S2CID 34999090.
Nguyen Q, Murphy G, Hughes CE, Mort JS, Roughley PJ (October 1993). "Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein". The Biochemical Journal. 295 (Pt 2): 595–8. doi:10.1042/bj2950595. PMC 1134922. PMID 7694569.
Conca W, Willmroth F (June 1994). "Human T lymphocytes express a member of the Matrix Metalloproteinase gene family". Arthritis and Rheumatism. 37 (6): 951–6. doi:10.1002/art.1780370626. PMID 8003069.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Gack S, Vallon R, Schaper J, Rüther U, Angel P (April 1994). "Phenotypic alterations in fos-transgenic mice correlate with changes in Fos/Jun-dependent collagenase type I expression. Regulation of mouse metalloproteinases by carcinogens, tumor promoters, cAMP, and Fos oncoprotein". The Journal of Biological Chemistry. 269 (14): 10363–9. doi:10.1016/S0021-9258(17)34069-3. PMID 8144618.
Windsor LJ, Grenett H, Birkedal-Hansen B, Bodden MK, Engler JA, Birkedal-Hansen H (August 1993). "Cell type-specific regulation of SL-1 and SL-2 genes. Induction of the SL-2 gene but not the SL-1 gene by human keratinocytes in response to cytokines and phorbolesters". The Journal of Biological Chemistry. 268 (23): 17341–7. doi:10.1016/S0021-9258(19)85340-1. PMID 8349617.
Knäuper V, Murphy G, Tschesche H (January 1996). "Activation of human neutrophil procollagenase by stromelysin 2". European Journal of Biochemistry. 235 (1–2): 187–91. doi:10.1111/j.1432-1033.1996.00187.x. PMID 8631328.
Pendás AM, Santamaría I, Alvarez MV, Pritchard M, López-Otín C (October 1996). "Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3". Genomics. 37 (2): 266–8. doi:10.1006/geno.1996.0557. PMID 8921407.
Sorsa T, Salo T, Koivunen E, Tyynelä J, Konttinen YT, Bergmann U, Tuuttila A, Niemi E, Teronen O, Heikkilä P, Tschesche H, Leinonen J, Osman S, Stenman UH (August 1997). "Activation of type IV procollagenases by human tumor-associated trypsin-2". The Journal of Biological Chemistry. 272 (34): 21067–74. doi:10.1074/jbc.272.34.21067. PMID 9261109.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Madlener M, Werner S (November 1997). "cDNA cloning and expression of the gene encoding murine stromelysin-2 (MMP-10)". Gene. 202 (1–2): 75–81. doi:10.1016/S0378-1119(97)00456-3. PMID 9427548.
Nakamura H, Fujii Y, Ohuchi E, Yamamoto E, Okada Y (April 1998). "Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases". European Journal of Biochemistry. 253 (1): 67–75. doi:10.1046/j.1432-1327.1998.2530067.x. PMID 9578462.
Bord S, Horner A, Hembry RM, Compston JE (July 1998). "Stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) expression in developing human bone: potential roles in skeletal development". Bone. 23 (1): 7–12. doi:10.1016/S8756-3282(98)00064-7. PMID 9662124.

External links

The MEROPS online database for peptidases and their inhibitors: M10.006
Overview of all the structural information available in the PDB for UniProt: P09238 (Stromelysin-2) at the PDBe-KB.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000166670 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047562 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2844164-5] Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988). "The collagenase gene family in humans consists of at least four members". The Biochemical Journal. 253 (1): 187–92. doi:10.1042/bj2530187. PMC 1149273. PMID 2844164.

[pmid2369069-6] Jung JY, Warter S, Rumpler Y (1990). "Localization of stromelysin 2 gene to the q22.3-23 region of chromosome 11 by in situ hybridization". Annales de Génétique. 33 (1): 21–3. PMID 2369069.

[entrez-7] "Entrez Gene: MMP10 matrix metallopeptidase 10 (stromelysin 2)".

[pmid22545096-8] Justilien V, Regala RP, Tseng IC, Walsh MP, Batra J, Radisky ES, Murray NR, Fields AP (2012). "Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential". PLOS ONE. 7 (4): e35040. Bibcode:2012PLoSO...735040J. doi:10.1371/journal.pone.0035040. PMC 3335833. PMID 22545096.

[pmid28939077-9] Upadhyay P, Gardi N, Desai S, Chandrani P, Joshi A, Dharavath B, Arora P, Bal M, Nair S, Dutt A (2017). "Genomic characterization of tobacco/nut chewing HPV-negative early stage tongue tumors identify MMP10 asa candidate to predict metastases". Oral Oncology. 73: 56–64. doi:10.1016/j.oraloncology.2017.08.003. PMC 5628952. PMID 28939077.

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Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

Clinical significance

References

Further reading

External links