[Effect of extracorporeal shockwave administration on biological behavior of bone cells in vitro].

Aim: Osteo-destructive effects as well as stimulation of bone growth are often described after extracorporeal shock-wave application (ESWA). A correlation between the applicated energy and outcome is assumed. The purpose of this study was to analyze, whether ESWA has an influence on growth and proliferation of bone cells in vitro.

Cell surface-bound urokinase-type plasminogen activator facilitates infiltration of freshly isolated granulocytes into fibrin matrix.

Human cell lines of myelo/monocytic origin express the cellular receptor for urokinase-type plasminogen activator (uPA-R). The receptor localizes urokinase-type plasminogen activator (uPA) to the surface of the cell, where it can convert plasminogen to the active serine proteinase plasmin. Plasmin may subsequently account for proteolysis of pericellular proteins.

Urokinase-type plasminogen activator enhances invasion of human T cells (Jurkat) into a fibrin matrix.

The receptor for urokinase-type plasminogen activator (uPA-R) localizes uPA to the cell surface. The receptor-bound uPA converts plasminogen to the trypsin-like endopeptidase plasmin. Thus uPA is involved in the initiation of pericellular proteolysis.

Charge-dependent binding of granzyme A (MTSP-1) to basement membranes.

The murine T cell-associated serine proteinase granzyme A [also termed Murine T cell-associated serine proteinase-1 (MTSP-1), or SE-1] expresses optimal enzymatic activity under extracellular milieu conditions. It degrades a variety of proteins that are constituents of basement membranes. Granzyme A is harbored within intracellular storage granules from which its release can be induced by appropriate ligand binding to extracellular matrix receptors of T cells.

A T-cell-related proteinase expressed by T-lymphoma cells activates their endogenous pro-urokinase.

In this report, we investigated the expression and activation of proteolytic enzymes by mouse T-lymphoma cell lines of differing metastatic potential. In contrast to the low metastatic Eb line, the metastatic variants ESb and ESb-MP secreted urokinase-type plasminogen activator (u-PA), which was present in the culture supernatant predominantly in the active form (ESb, 96%; ESb-MP, 80%). All three T-lymphoma variants expressed a mainly cell surface-associated proteinase, which proved to be immunologically and enzymatically related to the murine T-cell-associated serine proteinase-1 (MTSP-1).

Coordinate secretion and functional synergism of T cell-associated serine proteinase-1 (MTSP-1) and endoglycosidase(s) of activated T cells.

Cell lysates and exocytosed soluble mediator(s) (ESM) released from CD8+ T cell lines (TCL) by receptor-triggered secretory exocytosis were tested for degradation of proteoglycans associated with in vitro produced subendothelial extracellular matrix (ECM). ESM was found to release low-molecular weight (kav 0.5-0.