MMP10

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Matrix metallopeptidase 10 (stromelysin 2)
Protein MMP10 PDB 1q3a.png
PDB rendering based on 1q3a.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols MMP10 ; SL-2; STMY2
External IDs OMIM185260 MGI97007 HomoloGene20546 ChEMBL: 4270 GeneCards: MMP10 Gene
EC number 3.4.24.22
RNA expression pattern
PBB GE MMP10 205680 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4319 17384
Ensembl ENSG00000166670 ENSMUSG00000047562
UniProt P09238 O55123
RefSeq (mRNA) NM_002425 NM_019471
RefSeq (protein) NP_002416 NP_062344
Location (UCSC) Chr 11:
102.64 – 102.65 Mb
Chr 9:
7.5 – 7.51 Mb
PubMed search [1] [2]

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.[1][2]

Function[edit]

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. 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.[3]

MMP10 has been linked to cancer stem cell vitality and metastasis [4]

References[edit]

  1. ^ 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". Biochem. J. 253 (1): 187–92. PMC 1149273. PMID 2844164. 
  2. ^ 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". Ann. Genet. 33 (1): 21–3. PMID 2369069. 
  3. ^ "Entrez Gene: MMP10 matrix metallopeptidase 10 (stromelysin 2)". 
  4. ^ http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0035040?utm_source=feedburner&utm_medium=feed&utm_campaign=Feed%3A+plosone%2FBiochemistry+%28PLoS+ONE+Alerts%3A+Biochemistry%29

Further reading[edit]

  • Chandler S, Miller KM, Clements JM, et al. (1997). "Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview". J. Neuroimmunol. 72 (2): 155–61. doi:10.1016/S0165-5728(96)00179-8. PMID 9042108. 
  • Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
  • Fosang AJ, Neame PJ, Hardingham TE, et al. (1991). "Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins". J. Biol. Chem. 266 (24): 15579–82. PMID 1874716. 
  • Sirum KL, Brinckerhoff CE (1990). "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 (1995). "Expression pattern of matrix metalloproteinases in human liver". European Journal of Clinical Chemistry and Clinical Biochemistry 33 (2): 65–71. doi:10.1515/cclm.1995.33.2.65. PMID 7632822. 
  • Nguyen Q, Murphy G, Hughes CE, et al. (1993). "Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein". Biochem. J. 295 ( Pt 2) (Pt 2): 595–8. PMC 1134922. PMID 7694569. 
  • Conca W, Willmroth F (1994). "Human T lymphocytes express a member of the Matrix Metalloproteinase gene family". Arthritis Rheum. 37 (6): 951–6. doi:10.1002/art.1780370626. PMID 8003069. 
  • Maruyama K, Sugano S (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, et al. (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". J. Biol. Chem. 269 (14): 10363–9. PMID 8144618. 
  • Windsor LJ, Grenett H, Birkedal-Hansen B, et al. (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". J. Biol. Chem. 268 (23): 17341–7. PMID 8349617. 
  • Knäuper V, Murphy G, Tschesche H (1996). "Activation of human neutrophil procollagenase by stromelysin 2". Eur. J. Biochem. 235 (1–2): 187–91. doi:10.1111/j.1432-1033.1996.00187.x. PMID 8631328. 
  • Pendás AM, Santamaría I, Alvarez MV, et al. (1997). "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, et al. (1997). "Activation of type IV procollagenases by human tumor-associated trypsin-2". J. Biol. Chem. 272 (34): 21067–74. doi:10.1074/jbc.272.34.21067. PMID 9261109. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (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 (1998). "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, et al. (1998). "Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases". Eur. J. Biochem. 253 (1): 67–75. doi:10.1046/j.1432-1327.1998.2530067.x. PMID 9578462. 
  • Bord S, Horner A, Hembry RM, Compston JE (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[edit]

  • The MEROPS online database for peptidases and their inhibitors: M10.006