TY - JOUR
AU - Niland, Stephan
AU - Komljenovic, Dorde
AU - Macas, Jadranka
AU - Bracht, Thilo
AU - Bäuerle, Tobias
AU - Liebner, Stefan
AU - Eble, Johannes A
TI - Rhodocetin-αβ selectively breaks the endothelial barrier of the tumor vasculature in HT1080 fibrosarcoma and A431 epidermoid carcinoma tumor models.
JO - OncoTarget
VL - 9
IS - 32
SN - 1949-2553
CY - [S.l.]
PB - Impact Journals LLC
M1 - DKFZ-2018-02327
SP - 22406- 22422
PY - 2018
AB - The tumor vasculature differs from normal blood vessels in morphology, composition and stability. Here, we describe a novel tumor vessel-disrupting mechanism. In an HT1080/mouse xenograft tumor model rhodocetin-αβ was highly effective in disrupting the tumor endothelial barrier. Mechanistically, rhodocetin-αβ triggered MET signaling via neuropilin-1. As both neuropilin-1 and MET were only lumen-exposed in a subset of abnormal tumor vessels, but not in normal vessels, the prime target of rhodocetin-αβ were these abnormal tumor vessels. Consequently, cells lining such tumor vessels became increasingly motile which compromised the vessel wall tightness. After this initial leakage, rhodocetin-αβ could leave the bloodstream and reach the as yet inaccessible neuropilin-1 on the basolateral side of endothelial cells and thus disrupt nearby vessels. Due to the specific neuropilin-1/MET co-distribution on cells lining such abnormal tumor vessels in contrast to normal endothelial cells, rhodocetin-αβ formed the necessary trimeric signaling complex of rhodocetin-αβ-MET-neuropilin-1 only in these abnormal tumor vessels. This selective attack of tumor vessels, sparing endothelial cell-lined vessels of normal tissues, suggests that the neuropilin-1-MET signaling axis may be a promising drugable target for anti-tumor therapy, and that rhodocetin-αβ may serve as a lead structure to develop novel anti-tumor drugs that target such vessels.
LB - PUB:(DE-HGF)16
C6 - pmid:29854288
C2 - pmc:PMC5976474
DO - DOI:10.18632/oncotarget.25032
UR - https://inrepo02.dkfz.de/record/142097
ER -