PMC:4502371 / 32169-32999 JSONTXT

{"project":"2_test","denotations":[{"id":"25917920-16452136-43299649","span":{"begin":56,"end":60},"obj":"16452136"},{"id":"25917920-17015622-43299650","span":{"begin":267,"end":271},"obj":"17015622"},{"id":"25917920-17641224-43299651","span":{"begin":615,"end":619},"obj":"17641224"},{"id":"25917920-18388324-43299652","span":{"begin":621,"end":625},"obj":"18388324"},{"id":"25917920-17015622-43299653","span":{"begin":824,"end":828},"obj":"17015622"}],"text":"DPY-17 is known to interact with DPY-31 (Novelli et al. 2006). DPY-31 is a homolog of bone morphogenic protein-1 metalloprotease. The human bone morphogenic protein-1 is a tolloid-like gene whose proteolytic activity is required for TGFβ activation (Ge and Greenspan 2006). In humans, increased activity of other metalloproteases such as MMP2 (metalloprotease 2) and MMP9 has clear implications in Marfan pathology; in Marfan syndrome, these endopeptidases cleave ECM components, including microfibrils, elastic fibers, and collagen, resulting in loss of ECM integrity and aggravation of the syndrome (Chung et al. 2007, 2008). Our study suggests that DPY-31 in C. elegans and BMP-1 in humans may be involved in TGFβ dysregulation, a process that has been implicated in Marfan syndrome disease progression (Ge and Greenspan 2006)."}