Activator-dependent effects on cell-associated plasminogen activation
Cell-based study · Human THP-1 monocytic cells and primary mouse cortical neurons; purified human Glu- and Lys-plasminogen. [1]
Aminocaproic acid suppressed neuronal plasmin formation and cell-associated plasmin activity. In uPA-bearing THP-1 cultures it reduced cell-associated activity while soluble plasmin formation persisted or increased. The Glu/Lys-plasminogen comparison and antibody/CpB controls support a dependence on plasminogen state and cellular activator context.
| Endpoint | Reported result | Reference |
|---|---|---|
| Plasmin formation and cell-associated plasmin relative to no ε-ACA or antibody | Qualitative response Neuronal plasmin formation was inhibited; THP-1 plasmin formation persisted/increased while cell-associated activity fell. | [1] |
| Response of Glu- versus Lys-plasminogen activation to ε-ACA and CpB | Qualitative response ε-ACA stimulated Glu-plasminogen activation under the tested THP-1 conditions, while Lys-plasminogen activation was reduced; cell-associated plasmin decreased for both. | [1] |
Literature-Reported Treatment Conditions
- Treatment concentration
- 0–25 mM ε-ACA with 125 nM Glu-plasminogen (Figure 2); 5 or 25 mM with 500 nM Glu- or Lys-plasminogen (Figure 3).
- Exposure duration
- Kinetic assay; fixed total incubation duration not specified for Figures 2–3.
- Method
- Chromogenic plasmin assay at 37°C; 10^5 cells/well; 0.75 mM CBS0065; cell-associated activity assessed after PBS washing.
- Vehicle
- Cell medium; ε-ACA stock vehicle not specified.
- Co-treatment
- Exogenous plasminogen is the assay substrate. Separate mechanistic controls used anti-K1-LBS mAb 34D3 or CpB; these are not combination treatment claims.
- Reported limits
- No ε-ACA catalog number, lot/purity or stock solvent reported in the selected reagent description; no clinical exposure inference.
Methods and source locations
Compound reported in the paper: ε-Aminocaproic acid; Compound label in the paper: ε-ACA
Evidence concerns the named aminocaproic acid material in this model; it does not validate Adooq A10065 or establish equivalence of formulations.
Methods S3, S5, S8–S9, S13; Results S15–S17; Figures 1–3 and captions
Plasmin formation and cell-associated plasmin relative to no ε-ACA or antibody: CBS0065 hydrolysis; Figure 2 reports percentage mean ± SD, n = 3. Figure 1 identifies cellular activators; anti-K1-LBS antibody provides a complementary binding perturbation. — Results S16 P20; Figure 2A–C and caption
Response of Glu- versus Lys-plasminogen activation to ε-ACA and CpB: 500 nM Glu- or Lys-plasminogen; 5 or 25 mM ε-ACA; 50 μg/mL CpB control; Figure 3 mean ± SEM, n = 3. No exact heights or fold changes extracted from the curves/bars. — Results S17 P21–P22; Figure 3A–B and caption