Matrixmetalloproteinase-2 (MMP-2), also called
gelatinase-A, is a 72 Kd protein present in chromosome 16 in human. It is a
zinc binding protein, responsible for the degradation of Extra Cellular Matrix
(ECM) in normal physiological as well as disease processes like arthritis and
cancer. It has a specific role in the cancer development and angiogenesis.
MMP-2 contributes to cell migration. MMPs are the key to normal development as
well as in the pathology of cancer and other inflammatory diseases. The
inhibitors of MMP-2 activity are very important in maintaining the normal
activity of MMP-2 and have an important role in the management of cancer.
Regulation of MMP-2 activity is done by inhibitors like, TIMPs. In this report,
we are discussing about a possible inhibitor(s) present in the PBS extract of
guava leaves, inhibiting the active MMP-2 present in the saliva of breast
cancer patients.
References
[1]
Cathcart, J., Pulkoski-Gross, A. and Cao, J. (2015) Targeting Matrix Metalloproteinases in Cancer: Bringing New Life to Old Ideas. Genes & Diseases, 2, 26-34.
https://doi.org/10.1016/j.gendis.2014.12.002
[2]
Quintero-Fabián, S., Arreola, R., Becerril-Villanueva, E., Torres-Romero, J.C., Arana-Argáez, V., Lara-Riegos, J., et al. (2019) Role of Matrix Metalloproteinases in Angiogenesis and Cancer. Frontiers in Oncology, 9, 1370.
https://doi.org/10.3389/fonc.2019.01370
[3]
Xu, X., Wang, Y., Chen, Z., Sternlicht, M.D., Hidalgo, M. and Steffensen, B. (2005) Matrix Metalloproteinase-2 Contributes to Cancer Cell Migration on Collagen. Cancer Research, 65, 130-136.
[4]
Celentano, A., Yap, T., Paolini, R., Yiannis, C., Mirams, M., Koo, K., et al. (2021) Inhibition of Matrix Metalloproteinase-2 Modulates Malignant Behaviour of Oral Squamous Cell Carcinoma Cells. Journal of Oral Pathology & Medicine, 50, 323-332.
https://doi.org/10.1111/jop.12992
[5]
Webb, A.H., Gao, B.T., Goldsmith, Z.K., Irvine, A.S., Saleh, N., Lee, R.P., et al. (2017) Inhibition of MMP-2 and MMP-9 Decreases Cellular Migration, and Angiogenesis in in Vitro Models of Retinoblastoma. BMC Cancer, 17, 1-11.
https://doi.org/10.1186/s12885-017-3418-y
[6]
Amar, S. and Fields, G.B. (2015) Potential Clinical Implications of Recent Matrix Metalloproteinase Inhibitor Design Strategies. Expert Review of Proteomics, 12, 445-447. https://doi.org/10.1586/14789450.2015.1069190
[7]
Hidalgo, M. and Rowinsky, E.K. (2000) The Rapamycin-Sensitive Signal Transduction Pathway as a Target for Cancer Therapy. Oncogene, 19, 6680-6686.
https://doi.org/10.1038/sj.onc.1204091
[8]
Bhattacharyya, N., Mondal, S., Ali, M.N., Mukherjee, R., Adhikari, A. and Chatterjee, A. (2017) Activated Salivary MMP-2-A Potential Breast Cancer Marker. The Open Conference Proceedings Journal, 8, 22-32.
https://doi.org/10.2174/2210289201708010022
[9]
Lok, B., Sandai, D., Baharetha, H.M., Nazari, V.M., Asif, M., Tan, C.S., et al. (2020) Anticancer Effect of Psidium guajava (Guava) Leaf Extracts against Colorectal Cancer through Inhibition of Angiogenesis. Asian Pacific Journal of Tropical Biomedicine, 10, 293. https://doi.org/10.4103/2221-1691.284944
[10]
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
[11]
Nishida, Y., Miyamori, H., Thompson, E.W., Takino, T., Endo, Y. and Sato, H. (2008) Activation of Matrix Metalloproteinase-2 (MMP-2) by Membrane Type 1 Matrix Metalloproteinase through an Artificial Receptor for proMMP-2 Generates Active MMP-2. Cancer Research, 68, 9096-9104.
https://doi.org/10.1158/0008-5472.CAN-08-2522
[12]
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.
[13]
Jiang, H. and Li, H. (2021) Prognostic Values of Tumoral MMP2 and MMP9 Overexpression in Breast Cancer: A Systematic Review and Meta-Analysis. BMC Cancer, 21, 1-13. https://doi.org/10.1186/s12885-021-07860-2
[14]
Itoh, Y. (2015) Membrane-Type Matrix Metalloproteinases: Their Functions and Regulations. Matrix Biology, 44, 207-223.
https://doi.org/10.1016/j.matbio.2015.03.004