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Journal of Environmental Pathology, Toxicology and Oncology

Erscheint 4 Ausgaben pro Jahr

ISSN Druckformat: 0731-8898

ISSN Online: 2162-6537

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 2.4 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.8 The Immediacy Index is the average number of times an article is cited in the year it is published. The journal Immediacy Index indicates how quickly articles in a journal are cited. Immediacy Index: 0.5 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00049 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.59 SJR: 0.429 SNIP: 0.507 CiteScore™:: 3.9 H-Index: 49

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Cell Membrane-Associated MT1-MMP-Dependent Activation of Pro-MMP-2 in A375 Melanoma Cells

Volumen 24, Ausgabe 1, 2005, pp. 3-18
DOI: 10.1615/JEnvPathToxOncol.v24.i1.20
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ABSTRAKT

Matrix metalloproteinases (MMPs), a family of zinc-dependent endopeptidases, can degrade extracellular matrix components under physiological conditions and during cancer invasion and metastasis. Among the MMPs, the 72 kDa type IV collagenase MMP-2 (gelatinase A) is activated in a membrane-associated manner by an activation complex composed of membrane type 1 matrix metalloproteinase (MT1-MMP), tissue inhibitor of matrixmetalloproteinase-2 (TIMP-2), and pro-MMP-2 in the presence of αvβ3 integrin receptor. The activation of pro-MMP-2 correlates with increased occurrence of metastases. Increased MMP-2 activity has been demonstrated in many human tumors. In the present communication, we studied cell surface-associated activation of MMP-2 (72 kDa collagenase type IV) in the moderately metastatic human melanoma cell line A375. Results: Activation of purified 72 kDa collagenase type IV, pro-MMP-2 from cervical cancer tissue homogenate and from serum-free culture medium of HT1080 cells grown in presence of concanavalin A, by A375 cells, was shown by gelatin zymography. A375 cells activated only pro-MMP-2 from purified MMP-9/MMP-2 mixture indicating that the activation is specific for MMP-2. Activation of MMP-2 and purified collagenase type IV by A375 membrane fraction and membrane extract was also demonstrated by gelatin zymography. When A375 cells were first incubated with anti-MT1-MMP polyclonal antibody, activation of collagenase type IV was significantly decreased, indicating that membrane-associated MMP-2 activation is MT1-MMP-mediated. Immunocytochemistry showed MT1-MMP localization at focal adhesion sites. The presence of the components of activation complex—MT1-MMP and integrin αvβ3—were confirmed by Western blot, cell adhesion assay, and integrin subunit assay. Conclusion: Our experimental findings furnish another example of the unique membrane-associated MMP-2 activation mechanism in A375 melanoma cells and clearly indicate the role of MT1-MMP in MMP-2 activation. The information could help in developing new therapies designed to interfere with MMP activation and management of cancer and metastases.

REFERENZIERT VON
  1. Zhong Jun, Cornelsen Gencay Mikael M., Bubendorf Lukas, Burgess Janette K., Parson Holly, Robinson Bruce W.S., Tamm Michael, Black Judith L., Roth Michael, ERK1/2 and p38 MAP kinase control MMP-2, MT1-MMP, and TIMP action and affect cell migration: A comparison between mesothelioma and mesothelial cells, Journal of Cellular Physiology, 207, 2, 2006. Crossref

  2. Chan Carmen C. M., Wong Angel K., Liu Jie, Steeves John D., Tetzlaff Wolfram, ROCK inhibition with Y27632 activates astrocytes and increases their expression of neurite growth-inhibitory chondroitin sulfate proteoglycans, Glia, 55, 4, 2007. Crossref

  3. Liu Bin, Pang Bo, Hou Xianzeng, Fan Haitao, Liang Nan, Zheng Shuai, Feng Bin, Liu Wei, Guo Hua, Xu Shangchen, Pang Qi, Expression of high-mobility group AT-hook protein 2 and its prognostic significance in malignant gliomas, Human Pathology, 45, 8, 2014. Crossref

  4. Watts Stephanie W., Rondelli Catherine, Thakali Keshari, Li Xiaopeng, Uhal Bruce, Pervaiz Mohammad H., Watson Ralph E., Fink Gregory D., Morphological and biochemical characterization of remodeling in aorta and vena cava of DOCA-salt hypertensive rats, American Journal of Physiology-Heart and Circulatory Physiology, 292, 5, 2007. Crossref

  5. Bhattacharyya Nabanita, Mondal Subhajit, Moulik Shuvojit, Paul Sathi, Bhattacharrya Shreoshi, Hazra Alok Kumar, Ali Md. Nasim, Adhikari Anjan, Chatterjee Amitava, Effect of Black Tea Polyphenol on Cell-ECM Interaction and MMP, American Journal of Plant Sciences, 08, 04, 2017. Crossref

  6. Majumder Aheli, Ray Sajal, Banerji Aniruddha, Epidermal growth factor receptor-mediated regulation of matrix metalloproteinase-2 and matrix metalloproteinase-9 in MCF-7 breast cancer cells, Molecular and Cellular Biochemistry, 452, 1-2, 2019. Crossref

  7. Tan Mei Lin, Choong Peter FM, Dass Crispin R, Direct anti-metastatic efficacy by the DNA enzyme Dz13 and downregulated MMP-2, MMP-9 and MT1-MMP in tumours, Cancer Cell International, 10, 1, 2010. Crossref

  8. Moon Ji Wook, Choi Jong-Ho, Lee Soo Kyung, Lee Yong Woo, Lee Jung Ok, Kim Nami, Lee Hye Jeong, Seo Jung Seon, Kim Jin, Kim Hyeon Soo, Kim Gi Jin, Park Sun-Hwa, Promoter hypermethylation of membrane type 3 matrix metalloproteinase is associated with cell migration in colorectal adenocarcinoma, Cancer Genetics, 208, 5, 2015. Crossref

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