An in vitro model of Giardia duodenalis and the Caco2 cell line enable the study of parameters that could play a part in trophozoite attachment. We explored the role of membranous lectins of G. duodenalis in attachment-inhibition studies using carbohydrates in solution. Attachment rates were reduced by 14% and 23% in the presence of 100 mmol/l mannose-6-phosphate and glucose, respectively, as compared with control values. No significant modification was observed after trophozoite trypsinization at room temperature or at 37 degrees C. The inhibitory effects of colchicine (35%) and nocodazole (70%) suggest a primordial role of the cytoskeleton; microtubules appear to be the principal effectors of trophozoite fixation. Scanning electron microscopy revealed circular imprints on the Caco2 brush border after trophozoite detachment. The mechanisms of attachment of G. duodenalis to intestinal enterocyte-like cells in culture are thus essentially of the mechanical or hydrodynamic type; surface lectins would appear to intervene in the specificity for duodenal cells.
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http://dx.doi.org/10.1007/BF00928679 | DOI Listing |
Biochimie
January 2025
Laboratory of Applied Toxinology, Center of Toxins, Immune-Response and Cell Signaling (CeTICS), Butantan Institute, São Paulo, Brazil. Electronic address:
PA-BJ is a serine protease present in Bothrops jararaca venom that triggers platelet aggregation and granule secretion by activating the protease-activated receptors PAR-1 and PAR-4, without clotting fibrinogen. These receptors also have a relevant role in endothelial cells, however, the interaction of PA-BJ with other membrane-bound or soluble targets is not known. Here we explored the activity of PA-BJ on endothelial cell receptor, cytoskeleton, and coagulation proteins in vitro, and show the degradation of fibrinogen and protein C, and the limited proteolysis of actin, EPCR, PAR-1, and thrombomodulin.
View Article and Find Full Text PDFRedox Biol
January 2025
Redox Biology Group, Danish Cancer Institute, 2100, Copenhagen, Denmark. Electronic address:
Focal adhesions (FAs), multi-protein complexes that link the extracellular matrix to the intracellular cytoskeleton, are key mediators of cell adhesion, migration, and proliferation. These dynamic structures act as mechanical sensors, transmitting stimuli from the extracellular to intracellular environment activating in this way signaling pathways and enabling cells to adapt to environmental changes. As such, FAs are critical for tissue organization and serve as hubs governing cell spatial arrangement within the organism.
View Article and Find Full Text PDFOpen Biol
January 2025
Laboratory of Integrative Biology, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czechia.
Epithelia are multicellular sheets that form barriers defining the internal and external environments. The constant stresses acting at this interface require that epithelial sheets are mechanically robust and provide a selective barrier to the hostile exterior. These properties are mediated by cellular junctions which are physically linked with heavily crosslinked cytoskeletal networks.
View Article and Find Full Text PDFPNAS Nexus
January 2025
Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
The microtubule cytoskeleton is a dynamic network essential for many cellular processes, influenced by physicochemical factor, such as temperature, pH, dimer concentration, and ionic environment. In this study, we used in vitro reconstitution assays to examine the effects of four monovalent ions (Na, K, Cl, and Ac) on microtubule dynamics, uncovering distinct effects for each ion. Na was found to increase microtubule dynamicity by raising catastrophe frequency, polymerization and depolymerization speeds, and ultimately reducing microtubule lifetime by 80%.
View Article and Find Full Text PDFJ Biol Phys
January 2025
Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Science, Beijing, 100190, China.
Conventional kinesin protein is a prototypical biological molecular motor that can step processively on microtubules towards the plus end by hydrolyzing ATP molecules, performing the biological function of intracellular transports. An important characteristic of the kinesin is the load dependence of its velocity, which is usually measured by using the single molecule optical trapping method with a large-sized bead attached to the motor stalk. Puzzlingly, even for the same kinesin, some experiments showed that the velocity is nearly independent of the forward load whereas others showed that the velocity decreases evidently with the increase in the magnitude of the forward load.
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