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PubMed1979

Differential effects of trypsin on the epidermis of Rana catesbeiana. Observations on differentiating junctions and cytoskeletons.

The filamentous cytoskeletons of epidermal cells of the bullfrog (Rana catesbeiana) were investigated by electron microscopy. Following treatment with trypsin, sheets of epithelium were removed from swatches of abdominal skin. Trypsinization produces differential effects on the ultrastructure of the various cell layers. The desmosomes of all layers, except those of the stratum corneum, are split by trypsinization and the resulting desmosomal plaques fastened to tonofilaments are retracted into cells to form deep "inpouchings" of the plasma membranes, while tonofilament bundles become diffuse. Epidermal sheets were gently homogenized to form a suspension of cell remnants with damaged plasma membranes as indicated by vital dye exclusion tests and electron microscopy. Cytoskeletons retain their shapes, yet the lateral distances between individual tonofilaments within bundles appear to increase, thus forming diffuse lacelike structures. These observations support the suggestion that tonofilament bundles, when fastened to desmosomes, have elastic properties. The possible role of the cytoskeletons in the maintenance of cell size and shape in an ion-transporting epithelium is discussed.

Animals↗
PubMed1991

Axonal cytoskeleton at the nodes of Ranvier.

The relationship between the degree of nodal narrowing and the changes in the structure of the axonal cytoskeleton was studied in 53 fibres of mouse sciatic nerve. Nodal narrowing increased with increasing fibre calibre to reach about 20% of the internodal area in the thicker fibres. The narrowing corresponded quantitatively to a decreased number of nodal neurofilaments. Nodal microtubule numbers varied greatly, and a majority of fibres had considerably (approximately 55%) more microtubules in their nodal profile than in the internode. Nodal profiles of different calibre showed an increase in the number of filaments and of microtubules with nodal calibre, although at rates different from those in the internode. The degree of observed axon non-circularities had no discernible effect on the restructuring of the axonal cytoskeleton at the node. A transnodal transport of the axonal cytoskeleton can occur with: (1) accelerated transnodal transport of filaments, (2) stationary internodal fraction of filaments, (3) depolymerization of filaments proximal to the node and repolymerization distally, or (4) different nodal and internodal polymerization equilibria.

Animals↗
PubMed1991

Three-dimensional studies of the cytoskeleton of cultured hepatocytes: a quick-freezing and deep-etching study.

The ultrastructure of the cytoskeleton of cultured mouse hepatocytes was studied by a quick-freezing and deep-etching method. Isolated mouse hepatocytes were cultured on collagen gels for 48 h, fixed in paraformaldehyde and centrifuged to prepare cell pellets. The hepatocytes were split open to remove cytoplasmic soluble proteins for replica preparations. Some specimens were decorated with anti-actin antibody or S1 myosin fragments to identify actin filaments. They were quickly frozen in isopentane-propane mixture, fractured in liquid nitrogen, deeply etched in a freeze-fracture machine and rotary shadowed by platinum and carbon. The basal cell membranes of hepatocytes were in contact with the collagen gels and the apical surface faced the culture medium. Networks of actin filaments were attached to the apical cell membranes, but intermediate filaments were localized along the basal layer. Some intermediate filaments were associated with cell organelles, such as the endoplasmic reticulum. The Golgi apparatus was less associated with the cytoskeleton and showed synthesized materials in the cisternae. Cytoskeletal organization in cultured hepatocytes was revealed three-dimensionally, indicating that the interaction of cell membranes with collagen gels is important for the organization of the cytoskeleton.

Animals↗
PubMed1984

Intercellular communication and the control of growth: XI. Alteration of junctional permeability by the src gene in a revertant cell with normal cytoskeleton.

To learn whether the reduction of cell-to-cell communication in transformation is a possible primary effect of pp60src phosphorylation or secondary to a cytoskeletal alteration, we examined the junctional permeability in transformed cells with normal cytoskeleton. The permeability to fluorescent-labelled mono- and diglutamate was compared in clones of Faras' vole cells--clones transformed by Rous sarcoma virus and reverted from that transformation. One revertant clone (partial revertant), had the high level of pp60src kinase activity and tumorigenicity of the fully transformed parent clone, but had lost the cytoskeletal alterations of that clone. Another revertant clone (full revertant) had lost the tumorigenicity and most of the pp60src kinase activity, in addition (J.F. Nawrocki et al., 1984, Mol. Cell Biol. 4:212). The junctional permeability of the partial revertant with normal cytoskeleton was similar to that of the fully transformed parent clone with abnormal cytoskeleton. The permeabilities of both were lower than those of the full revertant and the normal uninfected cell, demonstrating that the junctional change by the src gene is independent of the cytoskeletal one.

Animals↗
PubMed1996

The structure of the neurofilament cytoskeleton in the squid giant axon and synapse.

Stereo views of thick sections (< 0.5 micron), or freeze etch replicas taken from selected regions of the squid giant axon and giant synapse, using an electron energy loss spectroscopic ultrastructural method, revealed a meshwork of anastomosing neurofilaments intersecting at a wide range of angles. This type of architectural organisation differs significantly from the ladder-like construction of the mammalian neurofilament cytoskeleton, in which longitudinally oriented core filaments are interconnected by lateral crossbridges. The deviant organization of squid neurofilaments is consistent with recent evidence that squid neurofilament proteins more closely resemble nuclear lamin rather than mammalian neurofilament proteins. A proximo-distal gradient of increasing width of the neurofilament meshes along the giant axon correlated well with the previously described gradient of increasing neurofilament phosphorylation. In these thick sections the presynaptic terminal of the giant synapse exhibited a mature neurofilament cytoskeleton that extended to the active zones without detectable signs of degradation. The observations are discussed in the context of current hypotheses concerned with the function of phosphorylation of neurofilaments, and with the steady state maintenance of the cytoskeleton in the squid axon and presynaptic terminal.

Animals↗
PubMed1994

Ca2+ channel Ca(2+)-dependent inactivation in a mammalian central neuron involves the cytoskeleton.

Ca2+ channel inactivation was investigated in acutely isolated hippocampal pyramidal neurons from adult rats and found to have a component dependent on intracellular Ca2+. Ca(2+)-dependent inactivation was indentified as the additional inactivation of channel current observed when Ca2+ replaced Ba2+ as the current carrying ion, and was found to be an independent process from that of Ba2+ current inactivation based on three lines of evidence: (1) no correlation between Ca(2+)-dependent inactivation and Ba2+ current inactivation was found, (2) only Ca(2+)-dependent inactivation was reduced by intracellular application of Ca2+ chelators, and (3) only Ca(2+)-dependent inactivation was sensitive to compounds which alter the cytoskeleton. Drugs which stabilize (taxol and phalloidin) and destabilize (colchicine and cytochalasin B) the cytoskeleton altered the development and recovery from Ca(2+)-dependent inactivation, indicating that the neuronal cytoskeleton may mediate Ca2+ channel sensitivity to intracellular Ca2+. Ca(2+)-dependent inactivation was not associated with a particular subset of Ca2+ channels, suggesting that all Ca2+ channels in these neurons are inactivated by intracellular Ca2+.

Animals↗
PubMed1998

Interaction of vaccinia virus with the actin cytoskeleton.

Vaccinia virus infection results in large rearrangements of the host actin cytoskeleton including the formation of actin tails that are strikingly similar to those seen in Listeria, Shigella and Rickettsia infections. Using actin polymerization as the driving force the intracellular enveloped form of the vaccinia virus (IEV) is propelled on the tip of actin tails at a speed of 2.8 microns/min, both intra- and intercellularly. The similarities between the actin-based motility of the vaccinia virus, Listeria, Shigella and Rickettsia suggest that intracellular pathogens have developed a common strategy to exploit the actin cytoskeleton of the host to facilitate their intercellular spread. This review focuses on our current understanding of the interactions between the vaccinia virus and the actin cytoskeleton.

Actins↗
PubMedDate not supplied

Relationships between smooth muscle and cytoskeleton antibodies in human serum samples.

In order to characterize the relationship between smooth muscle antibodies (SMA) and antibodies directed to the cytoskeleton components (microfilaments, intermediate filaments and microtubules), 338 serum samples from patients with various diseases and from healthy control subjects were tested for SMA and anti-cytoskeleton antibodies using a conventional immunofluorescence method employing traditional substrates and vinblastine-treated fibroblasts. The correspondence between SMA and these antibodies turned out to be incomplete and more evident for anti-microfilaments and anti-microtubules than for anti-intermediate filaments antibodies. Our data confirm that SMA are a quite heterogeneous family of antibodies, whose specificities are not entirely related to the cytoskeleton components. Studies with purified antigens will probably characterize these specificities.

Antibodies↗
PubMed2000

Cytoskeleton involvement on intestinal absorption processes.

It has been recently demonstrated in the laboratory that the cytoskeletal inhibitor cytochalasin E has an indirect inhibitory effect on the function of the intestinal Na+-sugar cotransporter (SGLT1). The present work confirms that cytochalasin E inhibits SGLT1 activity through cytoskeleton disruption, showing that in anaerobic conditions (N2 bubbling), which implies low cytosolic ATP levels, the inhibition is not observed. As it occurs in sugar transport, the Na+-dependent intestinal transport of phenylalanine decreases if cytochalasin E is present in the incubation medium. However, the activity of the brush border enzymes sucrase, amino peptidase N and gamma-glutamyl transferase is not affected by the inhibitor. These enzymes only have one transmembrane domain and the active center is projected to the intestinal lumen. Therefore, cytoskeleton changes that could modify the transmembrane enzyme segment do not alter the activity of these enzymes. Examination of the intestine morphology after 30 min incubation with cytochalasin E shows only light modifications which do not seem to explain the inhibitory effects of the toxin on Na+-sugar or Na+-phenylalanine cotransporters function. On the whole, these results indicate that the inhibition of cytochalasin E on galactose and phenylalanine intestinal transport is secondary to its action on cytoskeleton through protein structure modifications.

Animals↗
PubMed1998

Role of the cytoskeleton in stimulation of Na+ channels in A6 cells by changes in osmolality.

Permeable supports with A6 cell monolayers were mounted in an Ussing chamber and bilaterally bathed with Ringer solution at room temperature. Short-circuit current (Isc) was recorded continuously, and noise analysis revealed microscopic channel current characteristics. Our investigation focuses on the stimulation of apical Na+ entry caused by exposing the serosal surface of the A6 cell monolayers to hyposmotic Ringer solution. To evaluate the possible role of the cytoskeleton in the regulation of Na+ channels in response to a change in osmolality we used four different experimental approaches. In the control group, which were not exposed to any cytoskeleton-influencing drugs, there was a 1.5-fold increase in Isc and in the number of open Na+ channels after osmotic stimulation. For the second group cytochalasin D (0.1 microg/ml) was present on the serosal side during the experiments. Neither Isc nor the number of open Na+ channels increased after osmotic stimulation. In the third group colchicine (0.2 mM) or nocodazole (20 microM) was present on the serosal side, which resulted in 1.8-fold and 1.5-fold increases in Isc as well as 3-fold and 2-fold increases in the number of Na+ channels, respectively. In the fourth experimental group erythro-9-(2-hydroxy-3-nonyl) adenine hydrochloride (EHNA, 0.5 mM), a dynein inhibitor, was present on the serosal side. In this group Isc decreased to about 0.4 microA/cm2, and subsequent application of amiloride abolished Isc completely. Under hyposmolar conditions EHNA abolished entirely the sensitivity of Isc to the osmotic challenge. Because of the EHNA-induced down-regulation of Isc, the density of apical Na+ channels in this experimental group could not be determined. These results show that the cytoskeleton is dominantly involved in osmotic channel regulation at the apical membrane, and that actin filaments, microtubules and molecular motors are involved in the recruitment of additional Na+ channels.

Actins↗
PubMed2000

Developing prolamine protein bodies are associated with the cortical cytoskeleton in rice endosperm cells.

The mRNAs that encode the prolamine storage proteins in rice (Oryza sativa L.) endosperm cells are enriched on the surface of the prolamine protein bodies (PBs), a subcellular structure consisting of a prolamine intracisternal granule surrounded by rough endoplasmic reticulum membrane. Previous biochemical studies (D.G. Muench et al., 1998, Plant Physiol. 116: 559-569) have shown that prolamine mRNAs may be anchored to the PB surface via the cytoskeleton. To better understand the mechanism and role of mRNA localization in rice endosperm cells, we studied the subcellular development of prolamine PBs and their relationship with the cytoskeleton in rice endosperm cells. Confocal microscopy of endosperm cells showed that, unlike the glutelin PBs, the developing prolamine PBs are not randomly distributed within the cell, but instead are often enriched in the cortical region of the cell only a few micrometers beneath the plasma membrane. In addition, the peripheral prolamine PBs are closely associated with the cortical microtubule and actin filament networks. The cortical enrichment of rice prolamine protein bodies represents a unique example of endoplasmic reticulum subdomain localization in plant cells. The interaction of this endoplasmic reticulum subdomain with the cytoskeleton provides new insights on the possible mechanism and role of mRNA localization in plants.

Cytoskeleton↗
PubMed2001

Improved methods for examination of Toxoplasma gondii cytoskeleton at ultrastructural level.

To evaluate an improved method for identifying the presence of the structural elements of the cytoskeleton of Toxoplasma gondii and their influence on invasion of the parasite in host cells, copper grids coated with plastic film were used for adhesion of whole parasites. Tachyzoites were incubated with 0.5% Triton X-100 in PHEM buffer containing protease inhibitors, post-fixed in 1% glutaraldehyde, stained with uranyl acetate and submitted to critical point drying. In order to analyze the presence of the structural elements of the cytoskeleton, immunolocalization was carried out using colloidal gold. Invasion of the parasite was examined on cell culture after treatment of tachyzoites with cytochalasin B (CB). In order to observe this effect, an immunocytochemical assay using alkaline phosphatase was carried out. A very well conserved extraction of the cytoskeleton elements of T. gondii, such as conoid and microtubules, as well as the rhoptries, was observed. By immunolocalization with colloidal gold, it was possible to detect the actin in its globular form. In the assay of invasion of the parasite on the host cell, after treatment of the T. gondii tachyzoites with CB, the invasion process was totally inhibited.

Actins↗
PubMed1998

A possible role of the plasmalemmal cytoskeleton, nitric oxide synthase, and innervation in infantile hypertrophic pyloric stenosis. A confocal laser scanning microscopic study.

In reference to a possible neuropathy in the pathogenesis of infantile hypertrophic pyloric stenosis (IHPS), previous studies have described alterations in peptidergic transmission while others have recently attributed an important role to nitrinergic activity. Little attention has been given to the organization of the extracellular matrix (ECM) and the constituent cytoskeleton and subsarcolemma of the pyloric smooth-muscle cell. To study a possible relationship between neuronal and muscular elements in IHPS, 9 biopsies from patients with IHPS and 5 biopsies of normal pylorus were examined using immunohistochemical techniques with regard to the distribution of nerve cells and fibers (bNOS and PGP 9.5) and the ECM (laminin) and cytoskeleton (talin, vinculin, dystrophin, alpha-smooth iso-actin, desmin) components of the pyloric muscle. Our results showed anti-protein gene product 9.5 and b-nitric oxide synthase immunoreaction respectively reduced or absent in nerve fibers with a positive reaction inside the ganglion cells. An uneven distribution of the ECM component laminin was evident, together with a negative immunoreaction to talin and dystrophin. The imunolocalization of vinculin, alpha-smooth iso-actin, and desmin was similar to the controls. Our findings suggest that there is a close relationship between the nerve and muscle elements in the pathophysiology of IHPS and that non-alteration of some elements of cytoskeleton organization can play an important role in regaining pyloric function after pyloromyotomy.

Cytoskeletal Proteins↗
PubMed2001

Uptake of Malassezia furfur by human dermal fibroblasts: effect of ketoconazole and cytoskeleton inhibitors.

We showed the ability of human dermal fibroblasts to take up Malassezia furfur and the effect of ketoconazole and cytoskeleton inhibitors, including cytochalasin D and colchicine, on invasivity. Engulfment was evaluated by May Grunwald Giemsa stain and confirmed by acridine orange staining and electron microscopy. Both revealed the different steps of engulfment, including a fusion event between lysosomes and phagosomes containing M. furfur. Subinhibitory concentrations of ketoconazole (5 microg/ml) reduced the invasive capacity compared to controls (52.0+/-6.3 vs 10.0+/-1.2). M. furfur induced changes in the cytoskeleton of human dermal fibroblasts, with signs of disaggregation of actin fibres. We also studied the effect of the cytoskeleton inhibitors, cytochalasin D (1 microg/ml) and colchicine (1 microg/ml), on engulfment. Cytochalasin D, an inhibitor of actin polymers, inhibited the uptake of M. furfur by human dermal fibroblasts. Colchicine, a microtubule inhibitor, reduced the uptake of M. furfur less markedly. This suggests that the process of engulfment is F-actin-dependent, but the integrity of microtubules is also important in "non-professional" phagocytic cells such as dermal fibroblasts.

Antifungal Agents↗
PubMed2006

Actin cytoskeleton derangement induces apoptosis in renal ischemia/reperfusion.

UNLABELLED: This study evaluated whether cytoskeletal alterations during the ischemic conditions associated with kidney preservation could determine apoptosis. Cytoskeletal alterations are among the main effects of ischemia and may induce apoptosis. Rat kidneys were preserved in University of Wisconsin (UW) solution for 24 h. Some groups of animals underwent 45 min of warm ischemia (WI) to evaluate its effect on both the actin cytoskeleton and apoptosis (assessed by caspase-3 activity and TUNEL staining). Swinholide A (SwinA) and Latrunculin B (LB), two actin cytoskeleton-targeted agents, were administered to assess the effect of direct actin disruption on apoptosis. Jasplakinolide (JP), a compound that stabilizes actin filaments, was administered to evaluate the effect of actin stabilization. Apoptosis was evaluated at 3 h of ex vivo reperfusion using the isolated perfused rat kidney (IPK) model. RESULTS: Apoptosis increased during reperfusion with WI or administration of actin disruptor agents. Administration of stabilizing agents reversed apoptosis in kidneys that had previously undergone WI or had received an actin disruptor agent. CONCLUSION: The disruption of the actin cytoskeleton during ischemic conditions associated with kidney preservation induces apoptosis upon reperfusion through caspase-3 activation.

Actin Cytoskeleton↗
PubMed1989

Preparation and characterization of mitotic cytoskeletons from embryos of the sea urchin Strongylocentrotus franciscanus.

We present here a preparation protocol and molecular characterization of mitotic cytoskeletons isolated from embryos of the spiny red sea urchin, Strongylocentrotus franciscanus. The mitotic cytoskeletons are produced by detergent lysis of S. franciscanus embryos during cell division and consist of a mitotic apparatus enclosed in a thin shell of cortical filaments. Mitotic cytoskeletons produced in this way are stable for a year at liquid nitrogen temperature. S. franciscanus is of interest because it is commercially available in large quantities and each animal provides prodigious amounts of gametes. Furthermore, embryos from this sea urchin will develop synchronously at high densities and are an excellent source of quantities of cytoskeletal proteins appropriate for biochemical studies.

Animals↗
PubMed1994

Correlation between inhibition of cytoskeleton proteolysis and anti-vesiculation effect of calpeptin during A23187-induced activation of human platelets: are vesicles shed by filopod fragmentation?

Platelets were incubated in the presence of calpeptin to inhibit calpain-mediated cytoskeleton proteolysis during further activation by Ca2+ ionophore A23187. The appearance of filamin and myosin subfragments (93 kDa and 135 kDa, respectively) was inhibited by low calpeptin doses (1 microgram/ml). Higher doses (10-20 micrograms/ml) were required to completely inhibit talin and filamin degradation. Vesiculation strongly depended on cytoskeleton proteolysis and was reduced by 60% when platelets were preincubated with 10 micrograms/ml calpeptin. Activated platelets bore longer and more filopods when pretreated with calpeptin. Filopods were straight and regular when high calpeptin doses were used, whereas they were shorter and broader with bloated surfaces when calpeptin was omitted. Some bloated areas were also found in straight filopods. These results suggest that the cytoskeleton proteolysis, and more specifically filamin proteolysis, induced bloating of filopod surfaces, thus facilitating fragmentation of filopod into vesicles.

Blood Platelets↗
PubMed1984

Association of leukotriene B4 with the cytoskeleton of rabbit neutrophils. Effect of chemotactic factor and phorbol esters.

Following its addition to a suspension of rabbit neutrophils, leukotriene B4 is rapidly (less than 1 min) recovered from the cytoskeletal fraction (Triton X-100 insoluble pellet) of these cells. The association of leukotriene B4 with the cytoskeleton can be competed with by leukotriene B4 itself and by 20-OH leukotriene B4 but not by 20-COOH leukotriene B4. In addition, the preincubation of the cells with fMet-Leu-Phe or with phorbol 12-myristate 13-acetate, but not with 4 alpha-phorbol 12,13-didecanoate, results in a greatly decreased association of leukotriene B4 with the cytoskeleton. These results suggest that a specific association between the leukotriene B4 receptors and the cytoskeleton may be involved in signal transduction in the leukotriene B4 stimulated neutrophils.

Animals↗