## Abstract ## Objective The membrane‐anchored metalloproteinase disintegrin ADAM15 is up‐regulated in osteoarthritis and has been implicated in proteolysis and cell–matrix interactions. To address its role in cartilage metabolism, we performed an analysis of joint morphology in aging mice with a
The role of the disintegrin metalloproteinase ADAM15 in prostate cancer progression
✍ Scribed by Neali Lucas; Mark L. Day
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 152 KB
- Volume
- 106
- Category
- Article
- ISSN
- 0730-2312
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The metalloproteinase ADAM15 is a multi‐domain disintegrin protease that is upregulated in a variety of human cancers. ADAM15 mRNA and protein levels are increased in prostate cancer and its expression is significantly increased during metastatic progression. It is likely that ADAM15 supports disease progression differentially through the action of its various functional domains. ADAM15 may downregulate adhesion of tumor cells to the extracellular matrix, reduce cell–cell adhesion, and promote metastasis through the activity of its disintegrin and metalloproteinase domains. Additionally, ADAM15 can influence cell signaling by shedding membrane‐bound growth factors and other proteins that interact with receptor tyrosine kinases, leading to receptor activation. There is also evidence supporting a role for ADAM15 in angiogenesis and angioinvasion of tumor cells, which are critical for unrestrained tumor growth and metastatic spread. Given its diverse functions, ADAM15 may represent a pivotal regulatory component of tumor progression, an important target for therapeutic intervention, or emerge as a biomarker of disease progression. J. Cell. Biochem. 106: 967–974, 2009. © 2009 Wiley‐Liss, Inc.
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