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ADAMTS Proteases: Their Multifaceted Role in the Regulation of Cancer Metastasis

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Journal Dis Res
Date 2024 Jul 1
PMID 38948119
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Abstract

Cancer leads to nearly 10 million deaths worldwide per year. The tumour microenvironment (TME) is fundamental for tumour growth and progression. A key component of the TME, the extracellular matrix (ECM) has recently become a focus of interest in cancer research. Dysregulation of ECM synthesis and proteolysis leads to uncontrolled tumour growth and metastasis. Matrix remodelling enzymes, secreted by cancer cells and stromal cells, modify the overall structure and organisation of ECM proteins, therefore influencing biochemical interactions, tissue integrity and tissue turnover. While A Disintegrin and Metalloproteinases (ADAMs)' and matrix metalloproteinases' role in cancer has been deeply investigated, other proteolytic enzymes, like ADAMs with thrombospondin(-like) motifs (ADAMTSs) have been gaining interest due to their roles in modulating cancer cell-ECM interactions and oncogenic signalling pathways. In this review, we will discuss the dysregulation of ADAMTSs in cancer and their roles in regulating cancer development and progression, via ECM remodelling and cell signalling modulation.

References
1.
Haraguchi N, Ohara N, Koseki J, Takahashi H, Nishimura J, Hata T . High expression of ADAMTS5 is a potent marker for lymphatic invasion and lymph node metastasis in colorectal cancer. Mol Clin Oncol. 2017; 6(1):130-134. PMC: 5244970. DOI: 10.3892/mco.2016.1088. View

2.
Stanton H, Melrose J, Little C, Fosang A . Proteoglycan degradation by the ADAMTS family of proteinases. Biochim Biophys Acta. 2011; 1812(12):1616-29. DOI: 10.1016/j.bbadis.2011.08.009. View

3.
Yip H, Papa A . Signaling Pathways in Cancer: Therapeutic Targets, Combinatorial Treatments, and New Developments. Cells. 2021; 10(3). PMC: 8002322. DOI: 10.3390/cells10030659. View

4.
Shindo T, Kurihara H, Kuno K, Yokoyama H, Wada T, Kurihara Y . ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function. J Clin Invest. 2000; 105(10):1345-52. PMC: 315464. DOI: 10.1172/JCI8635. View

5.
Cross N, Chandrasekharan S, Jokonya N, Fowles A, Hamdy F, Buttle D . The expression and regulation of ADAMTS-1, -4, -5, -9, and -15, and TIMP-3 by TGFbeta1 in prostate cells: relevance to the accumulation of versican. Prostate. 2004; 63(3):269-75. DOI: 10.1002/pros.20182. View