Regular ArticleADAM15 Overexpression in NIH3T3 Cells Enhances Cell–Cell Interactions
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Cited by (56)
ADAMTS and ADAM metalloproteinases in osteoarthritis – looking beyond the ‘usual suspects’
2017, Osteoarthritis and CartilageCitation Excerpt :Böhm et al. proposed that ADAM15 increases chondrocyte survival by reinforcing adhesion to collagen types II and VI74, promoting outside-in pro-survival signalling76,77 and up-regulating anti-apoptotic molecules such as X-linked inhibitor of apoptosis (XIAP)78. ADAM15 has been shown to affect cell–cell and cell–matrix adhesion in other cell types79–81, potentially also through its ability to interact with integrins. ADAM15 is the only ADAM that contains an integrin-binding Arginine-glycine-aspartic acid (RGD) motif in its disintegrin domain82, enabling RGD-dependent interaction with αvβ3 and α5β183, and ADAM15 is also able to bind to α9β3 in an RGD-independent manner84.
Overexpression of soluble ADAM33 promotes a hypercontractile phenotype of the airway smooth muscle cell in rat
2016, Experimental Cell ResearchCitation Excerpt :Although we demonstrated that sADAM33 could regulate tone and contractility of ASMCs, the exact mechanism through which ADAM33 variants regulate the functions of ASMCs in asthma is yet unknown. Here, inspired by the working of other subfamily members such as ADAM8, 12, 15, 19 [40,49–51], we propose the following hypothetical model to explain the possible cellular role of ADAM33 in ASMCs. As shown in Fig. 6, sADAM33 is supposed to be either secreted from cytoplasm or cleaved from mature tADAM33 on the cell surface [42].
Recombinant disintegrin domain of ADAM15 inhibits the proliferation and migration of Bel-7402 cells
2013, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Researchers showed that ADAM15 combines with integrins such as αvβ3 in an RGD-dependent or with α9β1 in an RGD-independent manner [12,13]. Over-expression of ADAM15 in NIH3T3 cells enhances cell–cell interaction [14] while shRNA-mediated ADAM15 down-expression in PC-3 cells decreases migration and adhesion to specific extracellular matrix proteins [15]. Furthermore, the recombinant disintegrin of ADAM15 inhibits the growth and metastasis of MDA-MB-231 tumor in vivo as a therapeutic protein [16].
ADAM15 Peptidase
2013, Handbook of Proteolytic EnzymesSemisynthetic analogues of the marine cembranoid sarcophine as prostate and breast cancer migration inhibitors
2011, Bioorganic and Medicinal ChemistryCitation Excerpt :The scratched monolayer heals in a characteristic manner; therefore, this assay is widely used to study cell migration rates, cell polarization, and matrix remodeling studies.15–17 WHA proved to be useful as a proxy for metastasis, angiogenesis and other pathophysiological and physiological processes.18–21 Therefore, WHA was used in this study to assess and rank the antimigratory potential of semisynthetic sarcophine derivatives.
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These authors contributed equally.
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To whom reprint requests should be addressed at the Department of Pathology, Box 359675, Harborview Medical Center, 325 Ninth Avenue, Seattle, WA 98104-2499. Fax: (206) 341-5416. E-mail: [email protected].