@entity1 @entity35632 has been implicated in antitumorigenic and antiangiogenic activities, independent of its ribonuclease capacities. We constructed a truncated version of @entity1 @entity35632 , starting at E50 ( @entity42596 -50) and devoid of ribonuclease activity. @entity42596 -50 maintained its ability to bind actin and to inhibit angiogenesis and tumorigenesis. @entity42596 -50 binds to cell surface actin and formed a complex with actin in vitro. The antiangiogenic effect of this protein was demonstrated in @entity1 umbilical vein endothelial cells (HUVECs) by its ability to arrest tube formation on Matrigel, induced by angiogenic factors. Immunofluorescence staining of HUVECs showed nuclear and cytosolic @entity35632 protein that was no longer detectable inside the cell following @entity42596 -50 treatment. This effect was associated with disruption of the intracellular actin network. @entity42596 -50 co-localized with angiogenin, suggesting that both molecules bind (or compete) for similar cellular epitopes. Moreover, @entity42596 -50 led to a significant @entity5 development. Histological analysis demonstrated abundant necrotic tissue and a substantial loss of endothelial structure in @entity42596 -50-treated @entity5 . Collectively, the present results indicate that @entity42596 -50, a molecule engineered to be deficient of its catalytic activity, still maintained its actin binding and anticancer-related biological activities. We therefore suggest that @entity42596 -50 may serve as a potential @entity5 therapeutic agent.

XXXX recombinant truncated @entity35632 , devoid of RNase activity; A potential @entity5 therapeutic agent.

@entity1 :: ('9606', 'Species') :: ['human', 'Human'] @entity42596 :: ('7237', 'Gene') :: ['trT2'] @entity5 :: ('MESH:D009369', 'Disease') :: ['cancer', 'inhibition of tumor', 'tumors'] @entity35632 :: ('8635', 'Gene') :: ['RNASET2']
@entity1 :: (9606,Species) :: ['Human']
