Biology:MMP10
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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
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.[3]
Clinical significance
MMP10 has been linked to cancer stem cell vitality and metastasis.[4]
MMP10 is a potential prognostic biomarker for oral cancer.[5][unreliable medical source]
References
- ↑ "The collagenase gene family in humans consists of at least four members". The Biochemical Journal 253 (1): 187–92. July 1988. doi:10.1042/bj2530187. PMID 2844164.
- ↑ "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. 1990. PMID 2369069.
- ↑ "Entrez Gene: MMP10 matrix metallopeptidase 10 (stromelysin 2)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4319.
- ↑ "Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential". PLOS ONE 7 (4): e35040. 2012. doi:10.1371/journal.pone.0035040. PMID 22545096. Bibcode: 2012PLoSO...735040J.
- ↑ "Genomic characterization of tobacco/nut chewing HPV-negative early stage tongue tumors identify MMP10 asa candidate to predict metastases". Oral Oncology 73: 56–64. 2017. doi:10.1016/j.oraloncology.2017.08.003. PMID 28939077.
Further reading
- "Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview". Journal of Neuroimmunology 72 (2): 155–61. February 1997. doi:10.1016/S0165-5728(96)00179-8. PMID 9042108.
- "Matrix metalloproteinases". The Journal of Biological Chemistry 274 (31): 21491–4. July 1999. doi:10.1074/jbc.274.31.21491. PMID 10419448.
- "Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins". The Journal of Biological Chemistry 266 (24): 15579–82. August 1991. doi:10.1016/S0021-9258(18)98442-5. PMID 1874716.
- "Cloning of the genes for human stromelysin and stromelysin 2: differential expression in rheumatoid synovial fibroblasts". Biochemistry 28 (22): 8691–8. October 1989. doi:10.1021/bi00448a004. PMID 2605216.
- "Expression pattern of matrix metalloproteinases in human liver". European Journal of Clinical Chemistry and Clinical Biochemistry 33 (2): 65–71. February 1995. doi:10.1515/cclm.1995.33.2.65. PMID 7632822.
- "Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein". The Biochemical Journal 295 (Pt 2): 595–8. October 1993. doi:10.1042/bj2950595. PMID 7694569.
- "Human T lymphocytes express a member of the Matrix Metalloproteinase gene family". Arthritis and Rheumatism 37 (6): 951–6. June 1994. doi:10.1002/art.1780370626. PMID 8003069.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "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. April 1994. doi:10.1016/S0021-9258(17)34069-3. PMID 8144618.
- "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. August 1993. doi:10.1016/S0021-9258(19)85340-1. PMID 8349617.
- "Activation of human neutrophil procollagenase by stromelysin 2". European Journal of Biochemistry 235 (1–2): 187–91. January 1996. doi:10.1111/j.1432-1033.1996.00187.x. PMID 8631328.
- "Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3". Genomics 37 (2): 266–8. October 1996. doi:10.1006/geno.1996.0557. PMID 8921407.
- "Activation of type IV procollagenases by human tumor-associated trypsin-2". The Journal of Biological Chemistry 272 (34): 21067–74. August 1997. doi:10.1074/jbc.272.34.21067. PMID 9261109.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "cDNA cloning and expression of the gene encoding murine stromelysin-2 (MMP-10)". Gene 202 (1–2): 75–81. November 1997. doi:10.1016/S0378-1119(97)00456-3. PMID 9427548.
- "Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases". European Journal of Biochemistry 253 (1): 67–75. April 1998. doi:10.1046/j.1432-1327.1998.2530067.x. PMID 9578462.
- "Stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) expression in developing human bone: potential roles in skeletal development". Bone 23 (1): 7–12. July 1998. 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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