Potential role of kringle-integrin interaction in plasmin and uPA actions (a hypothesis).

ABSTRACT: We previously showed that the kringle domains of plasmin and angiostatin, the N-terminal four kringles (K1-4) of plasminogen, directly bind to integrins. Angiostatin blocks tumor-mediated angiogenesis and has great therapeutic potential. Angiostatin binding to integrins may be related to the antiinflammatory action of angiostatin. We reported that plasmin induces signals through protease-activated receptor (PAR-1), and plasmin-integrin interaction may be required for enhancing plasmin concentration on the cell surface, and enhances its signaling function. Angiostatin binding to integrin does not seem to induce proliferative signals. One possible mechanism of angiostatin's inhibitory action is that angiostatin suppresses plasmin-induced PAR-1 activation by competing with plasmin for binding

SUBMITTER: Takada Y 

PROVIDER: S-EPMC3480031 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature