Jörn Krätzschmar

TL;DR: The mouse and human homologue of a widely expressed cellular disintegrin is cloned and sequenced, and it is proposed that MDC9 might function as a membrane-anchored integrin ligand or metalloprotease, or that it may combine both activities in one protein.

TL;DR: CDNA cloning and initial biochemical characterization of the first cellular disintegrin protein with an RGD sequence in its disintegrin domain are reported, which are consistent with a model in which metargidin is an integrin ligand which, as a transmembrane protein, might function in cell-cell adhesion and/or signaling.

TL;DR: The cloning and initial biochemical characterization of the mouse metalloprotease/disintegrin/cysteine-rich (MDC) protein meltrin β and the analysis of the mRNA expression of four MDC genes in bone cells suggest that meltrin α and meltrinβ may play a role in osteoblast differentiation and/or function but are not likely to be involved in osteoclast fusion.

TL;DR: Proteins containing a membrane-anchored metalloprotease domain, a disintegrin domain, and a cysteine-rich region (MDC proteins) are thought to play an important role in mammalian fertilization as well as in somatic cell-cell interactions.

TL;DR: The cloning of cDNAs encoding three full-length and one partial metalloprotease-disintegrin from the amphibian Xenopus laevis are reported, and the analysis of their expression during early X. Laevis development and in adult tissues finds a highly localized and specific expression pattern of xmdc11a at the tailbud stage in the cranial neural crest and in a subset of neural tube cells in the trunk region.