Assessment of Bioprotect's Biodegradable Balloon System as a Rectal Spacer in Radiotherapy: An Animal Study on Tissue Response and Biocompatibility.

Prostate cancer is a significant health concern for men, emphasizing the need for effective treatment strategies. Dose-escalated external beam radiotherapy shows promise in improving outcomes but presents challenges due to radiation effects on nearby structures, such as the rectum. Innovative techniques, including rectal spacers, have emerged to mitigate these effects.

The fibrin(ogen)olytic properties of cathepsin D.

Fibrin(ogen) is important for hemostasis and is cleared from sites of vascular injury primarily by the plasminogen activator system. However, there is emerging evidence in plasminogen activator-deficient transgenic mice that non-plasmin pathways may also be important for endogenous fibrinolysis. We have recently described an alternative, plasmin-independent fibrinolytic pathway in activated human monocytes that utilizes the integrin Mac-1 (CD11b/CD18), which directly binds and internalizes fibrin, resulting in its lysosomal degradation.

Fibrin(ogen) is internalized and degraded by activated human monocytoid cells via Mac-1 (CD11b/CD18): a nonplasmin fibrinolytic pathway.

Fibrin(ogen) (FGN) is important for hemostasis and wound healing and is cleared from sites of injury primarily by the plasminogen activator system. However, there is emerging evidence in plasminogen activator-deficient transgenic mice that nonplasmin pathways may be important in fibrin(ogen)olysis, as well. Given the proximity of FGN and monocytes within the occlusive thrombus at sites of vascular injury, we considered the possibility that monocytes may play an ancillary role in the degradation and clearance of fibrin.

Lipoprotein(a) binds to human platelets and attenuates plasminogen binding and activation.

Lipoprotein(a) [Lp(a)] is a unique lipoprotein consisting of a low-density lipoprotein moiety (LDL) covalently linked to apoprotein(a). Previous work has demonstrated that Lp(a) can compete with plasminogen (PGN) for binding to endothelial and mononuclear cells and can inhibit PGN activation in cell-free systems. We have assessed the binding of Lp(a) to platelets and the influence of binding on the activation of PGN by tissue-type plasminogen activator (t-PA) in this system.