Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11gene.
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. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.
↑Levy A, Zucman J, Delattre O, Mattei MG, Rio MC, Basset P (Aug 1992). "Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22". Genomics. 13 (3): 881–3. doi:10.1016/0888-7543(92)90175-R. PMID1639418.
↑Anglard P, Melot T, Guerin E, Thomas G, Basset P (Oct 1995). "Structure and promoter characterization of the human stromelysin-3 gene". J Biol Chem. 270 (35): 20337–44. doi:10.1074/jbc.270.35.20337. PMID7657606.
↑Luo D, Mari B, Stoll I, Anglard P (Jul 2002). "Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase". J Biol Chem. 277 (28): 25527–36. doi:10.1074/jbc.M202494200. PMID12006591.
Basset P, Bellocq JP, Wolf C, et al. (1991). "A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas". Nature. 348 (6303): 699–704. doi:10.1038/348699a0. PMID1701851.
Pei D, Majmudar G, Weiss SJ (1994). "Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3". J. Biol. Chem. 269 (41): 25849–55. PMID7523394.
Boulay A, Masson R, Chenard MP, et al. (2001). "High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase". Cancer Res. 61 (5): 2189–93. PMID11280785.
Nakopoulou L, Panayotopoulou EG, Giannopoulou I, et al. (2003). "Stromelysin-3 protein expression in invasive breast cancer: relation to proliferation, cell survival and patients' outcome". Mod. Pathol. 15 (11): 1154–61. doi:10.1097/01.MP.0000037317.84782.CD. PMID12429794.
Wasenius VM, Hemmer S, Kettunen E, et al. (2003). "Hepatocyte growth factor receptor, matrix metalloproteinase-11, tissue inhibitor of metalloproteinase-1, and fibronectin are up-regulated in papillary thyroid carcinoma: a cDNA and tissue microarray study". Clin. Cancer Res. 9 (1): 68–75. PMID12538453.
Fromigué O, Louis K, Wu E, et al. (2003). "Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase". Int. J. Cancer. 106 (3): 355–63. doi:10.1002/ijc.11232. PMID12845673.
Skoglund J, Emterling A, Arbman G, et al. (2004). "Clinicopathological significance of stromelysin-3 expression in colorectal cancer". Oncology. 67 (1): 67–72. doi:10.1159/000080288. PMID15459498.
Louis K, Guérineau N, Fromigué O, et al. (2005). "Tumor cell-mediated induction of the stromal factor stromelysin-3 requires heterotypic cell contact-dependent activation of specific protein kinase C isoforms". J. Biol. Chem. 280 (2): 1272–83. doi:10.1074/jbc.M405482200. PMID15509588.
Deng H, Guo RF, Li WM, et al. (2005). "Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells". Biochem. Biophys. Res. Commun. 326 (2): 274–81. doi:10.1016/j.bbrc.2004.11.027. PMID15582574.
Arora S, Kaur J, Sharma C, et al. (2005). "Stromelysin 3, Ets-1, and vascular endothelial growth factor expression in oral precancerous and cancerous lesions: correlation with microvessel density, progression, and prognosis". Clin. Cancer Res. 11 (6): 2272–84. doi:10.1158/1078-0432.CCR-04-0572. PMID15788677.