Meprin β and BMP-1 are differentially regulated by CaCl2. (July 2017)

• Record Type: Journal Article
• Authors: Schneppenheim, Janna; Scharfenberg, Franka; Lucius, Ralph; Becker-Pauly, Christoph; Arnold, Philipp
• Is Part Of: Cell calcium. Volume 65(2017)
• Page Start: 8
• Page End: 13
• Publication Date: 2017-07
• Subjects: Meprin β -- BMP-1 -- Calcium -- Molecular dynamics simulation; Calcium -- Metabolism -- Periodicals; Vertebrates -- Physiology -- Periodicals; Calcium -- Physiological effect -- Periodicals; Cell physiology -- Periodicals; Calcium in the body -- Periodicals; 572.516
• DOI: 10.1016/j.ceca.2017.03.005
• Languages: English
• ISSNs: 0143-4160

Abstract

Graphical abstract: Highlights: Calcium regulates meprin β and BMP-1 differently. Calcium ions could bind to BMP-1 close to the active site. Calcium ions might destabelize the N-terminus of meprin β. Abstract: The two metalloproteases meprin β and bone morphogenetic protein 1 (BMP-1) are both members of the astacin protease family. They share specificity for negatively charged residues around the scissile bond and they are expressed in overlapping compartments of the human body. One important proteolytic substrate they share is pro-collagen I. Ablation of one of the two proteases however leads to different collagen I associated phenotypes in vivo . Over the last years calcium emerged as a regulator for the proteolytic activity of both enzymes. For meprin β a reduction and for BMP-1 an increase in activity was reported under increasing calcium concentrations. Here we revisit different compartments that rely on pro-collagen I maturation and explore the crystal structure of both proteases to highlight possible calcium binding sites. With this we aim to emphasize a to date underestimated regulator that influences both proteases.