calcimycin has been researched along with monodansylcadaverine* in 2 studies
2 other study(ies) available for calcimycin and monodansylcadaverine
| Article | Year |
|---|---|
Transglutaminase 1 stabilizes beta-actin in endothelial cells correlating with a stabilization of intercellular junctions.
Microvascular endothelial monolayers from mouse myocardium become resistant to various barrier-compromising stimuli correlating with the expression of transglutaminase 1 (TGase1) and its translocation towards cellular junctions. In contrast, endothelial monolayers from mouse lung microvessels do not express TGase1 and remain sensitive to barrier-compromising stimuli corresponding to the known in vivo sensitivity of the lung microvasculature. Using the TGase-substrate 5-(biotinamido)-pentylamine, specific TGase inhibitors and RNAi, one target protein of TGase1 in endothelial cells was found to be beta-actin, suggesting that tissue-specific stabilization of the cortical actin filament network by intracellular TGase1 activity may play a role in controlling barrier properties of endothelial monolayers. Topics: Actins; Amines; Animals; Biotin; Cadaverine; Calcimycin; Calcium; Capillary Permeability; Cell Line; Coronary Vessels; Endothelial Cells; Enzyme Inhibitors; Intercellular Junctions; Ionophores; Lung; Mice; Microcirculation; Protein Transport; RNA Interference; RNA, Small Interfering; Transglutaminases | 2007 |
Calcium pretreatment induces the decrease in epidermal growth factor binding through the activation of transglutaminase in isolated liver membrane.
Pretreatment of hepatocytes with Ca2+ and A23187 resulted in the decrease in epidermal growth factor (EGF) binding to the receptor. This decrease could be induced by only the pretreatment of the isolated liver membrane with Ca2+. By the pretreatment with 1 mM Ca2+ for 30 min, EGF binding was decreased to 40% of control. Scatchard plot analyses indicated that high affinity binding sites of EGF receptor disappeared after Ca2+ pretreatment. No effect of Ca2+ pretreatment on the degradation of receptor occurred. The Ca2+ effect was prevented by monodansylcadaverine or iodoacetamide, transglutaminase (TGase) inhibitors. After membrane-bound TGase was inactivated, the Ca2+ effect did not occur, except in the presence of purified TGase. Labeled putrescine was incorporated into some proteins of membrane with Ca2+ treatment. These results suggest that Ca(2+)-activated TGase induces the decrease in EGF binding to the receptor via modification of some membrane protein. Topics: Animals; Cadaverine; Calcimycin; Calcium; Cations, Divalent; Cell Membrane; Enzyme Activation; Epidermal Growth Factor; ErbB Receptors; Iodoacetamide; Liver; Male; Membrane Proteins; Putrescine; Rats; Rats, Wistar; Transglutaminases | 1993 |