PA-IIL

PA-IIL (50 μg/mL; 6-12 h) disrupts epithelial polarity and tight junction integrity in MDCK cells when applied basolaterally, whereas apical application has no such effects^[1].
PA-IIL (50 μg/mL; 1-6 h + 5-20 h washout recovery) causes rapid internalization of β1-integrins in MDCK cells when applied basolaterally, and this effect is reversible upon LecB washout, with integrin surface localization and TEER recovering over time^[1].
PA-IIL specifically binds to glycosylated β1-integrins at the basolateral surface of MDCK cells, with strong binding affinity capable of extracting 75% of total β1-integrin^[1].
PA-IIL (50 μg/mL; 10 min-6 h) causes internalization and lysosomal degradation of α3β1-integrin-laminin complexes in MDCK cells when applied basolaterally, regardless of β1-integrin activation status^[1].
PA-IIL induces membrane invaginations by binding fucose-bearing glycosphingolipids, and cross-links these invaginated membrane regions with β1-integrins in MDCK cells, providing a mechanism for integrin internalization^[1].
PA-IIL (5-100 μg/mL; 3-22 h) inhibits epithelial wound healing in MDCK cells in vitro in a dose-dependent manner, with concentrations greater than 50 μg/mL completely blocking migration, by inducing β1-integrin internalization in wound edge cells and preventing lamellipodium formation^[1].
PA-IIL (5 μM; 3 days) inhibits emigration of dermal CD14⁺ DCs, dermal CD14^- DCs, and epidermal Langerhans cells from human skin explants, and reduces CD18/ITGb2-CD11c/ITGb2 heterodimer expression on dermal DCs^[3].
PA-IIL (1 μg/mL; 2 h) binds to ex vivo isolated human blood and lymphatic endothelial cells^[3].
PA-IIL (5 μg/mL; 17 h) impairs transmigration of human PBMCs, lymphocytes, and monocytes across a human CMEC/D3 endothelial monolayer, increases leukocyte adherence to the monolayer, and disrupts VE-cadherin localization at endothelial cell membranes^[3].
PA-IIL (5 μg/mL; 1-5 h) induces time-dependent endocytosis and degradation of VE-cadherin, reorganization of the F-actin cytoskeleton, displacement of FAK, reduced myosin regulatory light chain phosphorylation, and arrested motility in human HUVECs, without causing cytotoxicity^[3].
PA-IIL (0.015-3 μM) induces intracellular reactive oxygen species production in LPS-primed and TNFα-primed human neutrophils (but not unprimed or 37°C-primed neutrophils) in a concentration-dependent manner, with significant activity at 1.5 μM and above^[4].
PA-IIL (0.015-3 μM; 30 min on ice) binds equally to the surface of unprimed, 37°C-primed, LPS-primed, and TNFα-primed human neutrophils, with binding increasing in a concentration-dependent manner, and binding is completely inhibited by methyl fucoside^[4].
PA-IIL (1.5 μM) inhibits phagocytosis-induced intracellular reactive oxygen species production in unprimed human neutrophils exposed to serum-opsonized Pseudomonas aeruginosa or Staphylococcus aureus^[4].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.