Henrik Gårdsvoll

TL;DR: The crystal structure of a soluble form of human urokinase‐type plasminogen activator receptor (uPAR/CD87), which is expressed at the invasive areas of the tumor‐stromal microenvironment in many human cancers, is reported.

TL;DR: Fibroblast-mediated collagen degradation proceeds preferentially as a sequential mechanism in which extracellular collagenolysis is followed by uPARAP/Endo180-mediated endocytosis of large collagen fragments, which is governed by the acquisition of a gelatin-like structure by the collagen, occurring upon collagenase-mediated cleavage under native conditions.

TL;DR: This study has identified the functional epitope on uPAR that is responsible for its interaction with the full-length, extended form of vitronectin by using a comprehensive alanine-scanning library of purified single-site uPAR mutants and raises the intriguing possibility that the canonical receptor and inhibitor for uPA (uPAR and PAI-1) may have reached a convergent solution for binding to the somatomedin B domain of vitRONectin.

TL;DR: The results support the hypothesis that enolase on the surface of Plasmodium ookinetes plays a dual role in midgut invasion: by acting as a ligand that interacts with the midGut epithelium and, further, by capturing plasminogen, whose conversion to active plAsmin promotes the invasion process.

TL;DR: A conceptual framework for understanding intravascular lipolysis and GPIHBP1 and LPL mutations causing familial chylomicronemia is provided and it is demonstrated that the acidic domain stabilizes LPL catalytic activity by mitigating the global unfolding of LPL's catalytic domain.