2021
DOI: 10.1016/j.taap.2021.115593
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Molecular and clinical insights of matrix metalloproteinases into cancer spread and potential therapeutic interventions

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Cited by 34 publications
(23 citation statements)
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“…Upregulation of interstitial marker proteins N-cadherin and vimentin causes the cells to acquire interstitial phenotypes and move easily [ 46 ]. MMPs degrade the extracellular matrix, which is beneficial to invasion and metastasis of malignant tumor cells [ 47 ].…”
Section: Curcumin In Treatment Of Malignant Tumorsmentioning
confidence: 99%
“…Upregulation of interstitial marker proteins N-cadherin and vimentin causes the cells to acquire interstitial phenotypes and move easily [ 46 ]. MMPs degrade the extracellular matrix, which is beneficial to invasion and metastasis of malignant tumor cells [ 47 ].…”
Section: Curcumin In Treatment Of Malignant Tumorsmentioning
confidence: 99%
“…Moreover, the angiogenic switch and the tumor neovascularization may be due to hypoxic conditions or the consequence of therapies promoting tumor progression [ 12 ]. Various studies have demonstrated the key participation of MMPs along with EMT to promote angiogenesis, infiltration by cancer cells, and metastasis [ 79 ]. MMPs participate in the degradation of ECM components, including the basement membrane and the tumor surface, resulting in tumor cell migration into the near tissue.…”
Section: Roles Of Mir-29b In Breast Cancermentioning
confidence: 99%
“…Metalloproteinases (MMPs, ADAMs and ADAMTSs) collectively cleave a large array of ECM substrates including proteoglycans, collagens and membrane-associated protein substrates such as cytokines (Black et al, 1997;Khatwa et al, 2010). Functionally, MMPs are responsible for regulating and degrading a variety of ECM components including collagen, elastin, and gelatin and contribute to regulation of cytokine expression (Ra and Parks, 2007;Siddhartha and Garg, 2021). Similarly, ADAMs cleave and release soluble factors like chemokines (Reiss and Saftig, 2009), mediate shedding of membrane-associated proteins into their active forms (i.e.…”
Section: Function Structure and Regulation Of Zinc-dependent Metalloproteinases Functionmentioning
confidence: 99%