To investigate the role of cathepsin X in the migration of T lymphocytes, Jurkat T cells were stably transfected with a pcDNA3 expression vector containing cathepsin X cDNA. The cathepsin-X-overexpressing T lymphocytes exhibited polarised migration-associated morphology, enhanced migration on 2D and 3D models and increased homotypic aggregation. We propose that cathepsin X causes cytoskeletal rearrangements and stimulates migration of T lymphocytes by modulating the activity of the beta2 integrin receptor LFA-1.
COBISS.SI-ID: 2370417
Two-step serial carbohydrate affinity chromatography was used to isolate a lectin from the edible mushroom clouded agaric (Clitocybe nebularis). It was characterized biochemically, its gene and cDNA cloned and the deduced amino acid sequence analyzed. Its activity was tested by hemagglutination assay and carbohydrate-binding specificity determined by glycan microarray analysis. The lectin exerts antiproliferative activity specific to human leukemic T cells.
COBISS.SI-ID: 1939791
The maturation status of dendritic cells (DCs) is crucial for effective antigen presentation and activation of T cell dependent immune response. Maturation stimuli include also various lectins. The maturation process consists of activation of integrin receptors, adhesion of immature dendritic cells to the extracellular matrix, reorganisation of cytoskeleton and the formation of cell extensions, podosomes. Important role in these processes has cysteine protease cathepsin X. Inhibition of cathepsin X results in altered phenotype and function of mature DCs.
COBISS.SI-ID: 2369393
Membrane nanotubes were recently described as a new principle of cell-cell communication enabling the exchange of vesicles, cell surface components, or calcium fluxes. For the first time the formation of nanotubes has been shown in T cells as a consequence of overexpressed cathepsin X. This results in enhanced activation of integrin receptor LFA-1 with subsequent cytoskeletal reorganisation forming a physically conected network of T lymphocytes through nanotubes.
COBISS.SI-ID: 2513009
Many of the recognition and adhesion functions of DCs are attributed to DC-SIGN (DCspecific ICAM-3 grabbing non-integrin), a C-type lectin expressed by DCs. We reported a new DC-SIGN mediated dendritic cell adhesion assay for identifying functional DC-SIGN inhibitors using either immature or mature dendritic cells. The repeatibility and reproducibility of the assay enables robust screening of compound library.
COBISS.SI-ID: 2513009