The protective effects of carvedilol on heart function observed in the acute phase of experimental autoimmune myocarditis seem to be associated with its ability to decrease MMP-2 activity and subsequently prevent degradation of myofilaments and release of troponin I while not related to suppression of inflammation.
Cell fractionationCells were washed twice in cold PBS and then resuspended in hypotonic buffer containing 10 mM
Localization of Enolase in the Subfractions of a Breast Cancer Cell LineEwa Seweryn*, Jadwiga Pietkiewicz, Iwona S. Bednarz-Misa, Ireneusz Ceremuga, Jolanta Saczko, Julita Kulbacka, and Andrzej Gamian Enolase detected on the cell surface may be a receptor for certain ligands, especially for plasminogen. It is important for the pathogen invasiveness and in the development of a tumour. Therefore, we sought to preliminarily determine the enolase location and catalytic activity in the subfractions of MCF-7 cells. The latter was done on intact cells and in subfractions of MCF-7 cells. We identifi ed enolase by immunoblotting. The binding of human plasminogen to enolase was performed by immunoblotting using monoclonal antibodies against plasminogen. The intact MCF-7 cells demonstrated activity of enolase. Enolase in postnuclear and perinuclear fractions is catalyticly active too. We identifi ed the enolase protein in immunoblots of these fractions, except for the nuclear subfraction. These results provide evidence that enolase is present on the intact surface of MCF-7 cells and in post-and perinuclear fractions. The surface protein maintained catalytic activity, which suggests that its location in the plasma membrane didn't change the active centre of the enzyme.
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Pseudomonas aeruginosa is one of the pathogenic bacteria which utilize binding of the host plasminogen (Plg) to promote their invasion throughout the host tissues. In the present study, we confirmed that P. aeruginosa exhibits binding affinity for human plasminogen. Furthermore, we showed that the protein detected on the cell wall of P. aeruginosa and binding human plasminogen is an enolase-like protein. The hypothesis that alpha-enolase, a cytoplasmatic glycolytic enzyme, resides also on the cell surface of the bacterium was supported by electron microscopy analysis. The plasminogen-binding activity of bacterial cell wall outer membrane enolase-like protein was examined by immunoblotting assay.
IntroductIon Exosomes are currently considered as the new biomarkers of colorectal cancer (CRC). Tetraspanins (CD9, CD63) belong to the well -known exosome markers, but can also be found on other subtypes of extracellular vesicles (EVs).objEctIvEs The aim of this study was to estimate the expression level of exosome markers and EVs in CRC.
PAtIEnts And mEthodsThe expression level of CD9 and CD63 antigens was evaluated by immunohistochemical staining in 109 patients diagnosed with CRC. Immunohistochemistry results were verified by nanoparticle tracking analysis (NTA), as well as the Western blot analysis and transmission electron microscopy. Exosomes isolation was performed on solid tissues. The immunohistochemical expression of both tetraspanins was compared with expression of cellular proliferation marker, Ki -67.rEsuLts A higher expression level of exosome markers was observed in CRC compared with the normal colonic mucosa. The NTA revealed higher concentrations of nanoparticles in CRC tissues than in controls. There was a strong positive correlation between exosome markers and the Ki -67 antigen. The expression levels of both tetraspanins were different for lymph node staging (N stage).concLusIons Exosome markers and EVs were more pronounced in the CRC samples compared with controls. Immunohistochemical evaluation of tetraspanins reflects the results obtained by the NTA. Exocytosis appears to play an important role in the pathogenesis of CRC. To the best of our knowledge, such analysis was carried out for the first time.
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