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OALib Journal期刊
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Plant Matrix Metalloproteinase Like Molecules (MMPs)

DOI: 10.4236/oalib.1111315, PP. 1-9

Subject Areas: Plant Science

Keywords: Plants, Flowers, Leaves, MMPs

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Abstract

Matrix metalloproteinases (MMPs) are Zn2+ dependent endopeptidase be-longing to metzincin family. Matrix metalloproteinases (MMPs) have been classified in detail in mammals and have been shown to play key roles in many physiological and pathological processes.

Cite this paper

Bera, A. , Mondal, S. , Chatterjee, S. and Chatterjee, A. (2024). Plant Matrix Metalloproteinase Like Molecules (MMPs). Open Access Library Journal, 11, e1315. doi: http://dx.doi.org/10.4236/oalib.1111315.

References

[1]  Liotta, L.A. (1989) Principles of Molecular Cell Biology of Cancer; Cancer Metastases. In: DeVita Jr., V.T., Lawrence, T.S. and Rosenberg, S.A., Eds., Cancer Principles and Practice of Oncology, Lippincott Williams & Wilkins, Philadelphia, 98-115.
[2]  Paget, S. (1889) The Distribution of Secondary Growths in Cancer of the Breast. The Lancet, 133, 571-573. https://doi.org/10.1016/S0140-6736(00)49915-0
[3]  Wang, Y., Klijn, J., Zhang, Y., Sieuwerts, A., Look, M., Yang, F., Talantov, D., Timmermans, M., Meijer-van Gelder, M., Yu, J., Jatkoe, T., Berns, E., Atkins, D. and Foekens, J. (2005) Gene-Expression Profiles to Predict Distant Metastasis of Lymph-Node-Negative Primary Breast Cancer. The Lancet, 365, 671-679. https://doi.org/10.1016/S0140-6736(05)17947-1
[4]  Bernards, R. and Weinberg, R.A. (2002) Metastasis Genes: A Pro-gression Puzzle. Nature, 418, 823-823. https://doi.org/10.1038/418823a
[5]  Kaplan, R., Riba, R., Zacharoulis, S., Bramley, A., Vincent, L., Costa, C., MacDonald, D., Jin, D., Shido, K., Kerns, S., Zhu, Z., Hicklin, D., Wu, Y., Port, J., Altorki, N., Port, E., Ruggero, D., Shmelkov, S., Jensen, K., Rafii, S. and Lyden, D. (2005) VEGFR1-Positive Haematopoietic Bone Marrow Progenitors Initiate the Pre-Metastatic Niche. Nature, 438, 820-827. https://doi.org/10.1038/nature04186
[6]  Mondal, A., Mukherjee, R., Mondal, S. and Chatterjee, A. (2021) MMP-2 Inhibitory Activity of PBS Extract of Guava Leaves. American Journal of Plant Sciences, 12, 1761-1767. https://doi.org/10.4236/ajps.2021.1212122
[7]  Mukherjee, R., Ray, S., Mondal, S. and Chatterjee, A. (2022) Salivary Active MMP-2 of Breast Cancer Patients Is Inhibited by Guava Leaves PBS Extract. American Journal of Plant Sciences, 13, 650-658. https://doi.org/10.4236/ajps.2022.135043
[8]  Mondal, S., Bardhan, K., Dutta, A. and Chatterjee, A. (2018) Identification of Vertebrate MMP-2 and MMP-9 Like Molecules in the Aqueous Extract of Nasturtium (Tropaeolum Majus) Flowers, Bambusa Balcooa Leaves and Nayantara (Catharanthus Roseus) Flowers. Journal of Tumor, 6, 540-544.
[9]  Chambers, A.F. and Matrisian, L.M. (1997) Changing Views of the Role of Matrix Metalloproteinases in Metas-tasis. Journal of the National Cancer Institute, 89, 1260-1270. https://doi.org/10.1093/jnci/89.17.1260
[10]  Liotta, L.A. and Stetler-Stevenson, W.G. (1990) Metalloproteinases and Cancer Invasion. Seminars in Cancer Biology, 1, 99-106.
[11]  Liotta, L.A., Wewer, U., Rao, N.C., Schiffmann, E., Stracke, M., Guirguis, R., Thorgeirsson, U., Muschel, R. and Sobel, M. (1988) Biochemical Mechanisms of Tumor Invasion and Metastases. Progress in Clinical and Biological Research, 256, 3-16.
[12]  Curran, S. and Graeme, I.M. (1999) Matrix Metalloproteinases in Tumour Invasion and Metastasis. The Journal of Pathology, 189, 300-308. https://doi.org/10.1002/(SICI)1096-9896(199911)189:3<300::AID-PATH456>3.0.CO;2-C
[13]  Levy, A.T., Cioce, V., Sobel, M.E., Garbisa, S., Grigioni, W.F., Liotta, L.A. and Stetler-Stevenson, W.G. (1991) Increased Expression of the Mr 72,000 Type IV Collagenase in Human Colonic Adenocarcinoma. Cancer Research, 51, 439-444.
[14]  Giannelli, G., Bergamini, C., Marinosci, F., Fransvea, E., Quaranta, M., Lupo, L., Schiraldi, O. and Antonaci, S. (2002) Clinical Role of MMP-2/TIMP-2 Im-balance in Hepatocellular Carcinoma. International Journal of Cancer, 97, 425-431. https://doi.org/10.1002/ijc.1635
[15]  Sakata, K., Shigemasa, K., Nagai, N. and Ohama, K. (2000) Expression of Matrix Metalloproteinases (MMP-2, MMP-9, MT1-MMP) and Their Inhibitors (TIMP-1, TIMP-2) in Common Epithelial Tumors of the Ovary. International Journal of Oncology, 17, 673-754. https://doi.org/10.3892/ijo.17.4.673
[16]  Verma, R.P. and Corwin, H. (2007) Matrix Metalloproteinases (MMPs): Chemical-Biological Functions and (Q) SARs. Bioorganic & Medicinal Chemistry, 15, 2223-2268. https://doi.org/10.1016/j.bmc.2007.01.011
[17]  Van Wart, H.E.and Birkedal-Hansen, H. (1990) The Cysteine Switch: A Principle of Regulation of Metalloproteinase Activity with Potential Applicability to the Entire Matrix Metalloproteinase Gene Family. Proceedings of the National Academy of Sciences, 87, 5578-5582. https://doi.org/10.1073/pnas.87.14.5578
[18]  Snoek-van, B., Patricia, A.M. and Von den Hoff, J.W. (2005) Zymographic Techniques for the Analysis of Matrix Metalloproteinases and Their Inhibitors. Biotechniques, 38, 73-83. https://doi.org/10.2144/05381RV01
[19]  Van Lint, P., and Claude, L. (2007) Chemokine and Cytokine Processing by Matrix Metalloproteinases and Its Effect on Leukocyte Migration and Inflammation. Journal of Leucocyte Biology, 82, 1375-1381. https://doi.org/10.1189/jlb.0607338
[20]  Lohi, J., Wilson, C.L., Roby, J.D. and Parks, W.C. (2001) Epilysin, a Novel Human Matrix Metalloproteinase (MMP-28) Expressed in Testis and Keratinocytes and in Response to Injury. Journal of Biological Chemistry, 276, 10134-10144. https://doi.org/10.1074/jbc.M001599200
[21]  Manzetti, S., McCulloch, D.R., Herington, A.C. and van der Spoel, D. (2003) Modeling of Enzyme-Substrate Complexes for the Metalloproteases MMP-3, ADAM-9 and ADAM-10. Journal of Computer-Aided Molecular Design, 17, 551-565. https://doi.org/10.1023/B:JCAM.0000005765.13637.38
[22]  Kester, W.R. and Matthews, B.W. (1977) Crystallographic Study of the Binding of Dipeptide Inhibitors to Thermolysin: Implications for the Mechanism of Catalysis. Biochemistry, 16, 2506-2516. https://doi.org/10.1021/bi00630a030
[23]  Gross, J. and Lapiere, C.M. (1962) Collagenolytic Activity in Amphibian Tissues: A Tissue Culture Assay. Proceedings of the National Academy of Sciences, 48, 1014-1022. https://doi.org/10.1073/pnas.48.6.1014
[24]  Eisen, A.Z., John, J.J. and Gross, J. (1968) Human Skin Collagenase, Isolation and Mechanism of Attack on the Collagen Molecule. Biochimica et Biophysica Acta (BBA)-Enzymology, 151, 637-645. https://doi.org/10.1016/0005-2744(68)90010-7
[25]  Trexler, M., Briknarová, K., Gehrmann, M., Llinás, M. and Patthy, L. (2003) Peptide ligands for the Fibronectin Type II Modules of Matrix Metalloproteinase 2 (MMP-2). Journal of Biological Chemistry, 278, 12241-12246. https://doi.org/10.1074/jbc.M210116200
[26]  Tareq Hassan Khan, M., Dedachi, K., Matsui, T., Kurita, N., Borgatti, M., Gambari, R. and Sylte, I. (2012) Dipeptide Inhibitors of Thermolysin and Angiotensin I-Converting Enzyme. Current Topics in Medicinal Chemistry, 12, 1748-1762. https://doi.org/10.2174/1568026611209061748
[27]  Dollery, C.M., Jean, R.M. and Adriano, M.H. (1995) Matrix Metalloproteinases and Cardiovascular Disease. Circulation Research, 77, 863-868. https://doi.org/10.1161/01.RES.77.5.863
[28]  Pei, D., Kang, T. and Qi, H. (2000) Cysteine Array Matrix Metalloproteinase (CA-MMP)/MMP-23 Is a Type II Transmembrane Matrix Metalloproteinase Regulated by a Single Cleavage for Both Secretion and Activation. Journal of Biological Chemistry, 275, 33988-33997. https://doi.org/10.1074/jbc.M006493200

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