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PubMed1980

Recognition of two initiation codons for the synthesis of phage fd gene 2 protein.

Bacteriophage fd gene 2 protein was specifically labeled with radioactive amino acids and was isolated from membranous cell structures as an apparently homogenous protein. Amino acid sequence analysis revealed that the protein was initiated at two distinct AUG codons close to the ribosome binding site. The two resulting translation products were found to begin with a deformylated methionine residue. Initiation at the first signal was used for 90% of the chains and at the second signal for 10% of the sequenced molecules. The use of one or the other chain start may influence functions of gene 2 protein.

Amino Acid Sequence↗
PubMed1989

The ultrastructural immunocytochemical localization of superoxide dismutase in the amphibian urinary bladder: effect of aldosterone.

Transmission electron microscopy and immunohistochemistry, the latter employing the avidin-biotin-peroxidase (ABC complex) technique, were utilized to localize copper-zinc superoxide dismutase (CuZn-SOD) enzyme activity in the epithelial cells of the toad urinary bladder mucosa. This 'scavenger' enzyme catalyses the dismutation (reduction-oxidation) of the superoxide anion (O2-), a toxic free radical generated during normal cellular respiration. In unstimulated epithelial cells, enzyme activity was seen in the cytosol of granular, mitochondrial-rich and goblet cells. The basal cells were generally devoid of enzyme activity. In addition to the cytosol, SOD activity was also seen in association with the apical plasma membrane of the epithelial cells. In the presence of the steroid hormone aldosterone (10(-7)M, 30 min-6h), CuZn-SOD activity was markedly increased along the luminal mucosal membrane of granular, mitochondrial-rich and goblet cells. This increase was seen as early as 30 min after the addition of hormone, and as long as 6h after treatment. The cytosolic reaction was usually decreased or absent under these conditions. From the data presented, it appears that CuZn-SOD is involved in electrolyte (sodium) transport in the epithelial cells of the toad urinary bladder. The latter may involve hormone-induced alterations in luminal cell membrane structure and chemistry.

Aldosterone↗
PubMed1996

Freeze-fracture immunogold labeling.

Several approaches have been developed to combine immunogold cytochemistry and freeze-fracture techniques. These methods are highly heterogeneous regarding both the sequence of the procedural steps and the aspect of the resulting images. They imply immunolabeling either before or after freeze-fracture or even immunolabeling of platinum/carbon replicas of the freeze-fractured membranes, and have been used alternatively or in parallel to address different questions related to cell membrane structure, composition and dynamics or to intracellular membrane traffic. This review will briefly describe these methods and report most of their immunogold cytochemical applications, with the aim of facilitating selection of the most appropriate approach.

Animals↗
PubMed1996

Calcium-cadmium interaction on sugar absorption across the rabbit jejunum.

The element Cd is considered to have no biological function and is highly toxic to humans and animals. Toxic effects of this metal upon cell membrane structure and function have been shown. On the other hand, Ca is an essential element in a wide variety of cellular activities. The present study was initiated to research whether the interaction between Ca and Cd could affect D-galactose absorption across the rabbit jejunum in vitro. In media with Ca2+, when CdCl2 was present at 0.5 or 1 mM, Cd was found to significantly reduce the sugar absorption. In Ca2+ -free media, where CaCl2, was omitted and replaced isotonically with choline chloride, the sugar transport was not modified by Cd, but when CaCl2 was replaced isotonically with MgCl2, the inhibition is observed. Verapamil at 10(-6)M (blocking mainly Ca2+ transport) did not modify the inhibitory effect of cadmium on D-galactose transport. When 10(-6)M of A 23187 (Ca2+ specific ionophore) was added in media with/without Ca2+; CdCl2 produced no change in D-galactose transport. These results suggest that Ca and Cd could have affinity for the same chemical groups of enterocyte membrane, which would be related with the intestinal absorption of D-galactose.

Analysis of Variance↗
PubMed2004

Global transcription profiles and intracellular pH regulation measured in Bacillus licheniformis upon external pH upshifts.

For optimization of propagation conditions for an industrially used Bacillus licheniformis, this study examines the effect of transferring cells at the early-stationary growth phase (pH 5.3) to fresh growth medium at pH 5.0-8.0. Intracellular pH (pH(i)) was measured on a single-cell level, using fluorescence ratio imaging microscopy after staining with 5(6)-carboxyfluorescein diacetate succinimidyl ester. Transcription profiles were determined using a genome DNA microarray. The optimum extracellular pH (pH(ex)) value for growth of B. licheniformis was found to be pH 7.0, resulting in the shortest lag phase, highest maximum specific growth rate and maximum biomass formation. An average pH gradient (Delta pH = pH(i) - pH(ex)) of approx. 1.0 was found in B. licheniformis 15 min after transfer to pH(ex) 5.0-8.0. Up-regulation of genes involved in sucrose uptake at pH 7.0 could be related to the optimum growth observed. Transcription profiles indicated that the organism was experiencing phosphate starvation upon transfer to pH 7.0 and pH 8.0. Mechanisms involved in pH(i) regulation appeared to include changes in fatty acid synthesis to yield a more rigid cell membrane structure at low pH(ex) values and conversion of pyruvate to acetoin instead of acetate for neutralization of low pH(ex) values.

Adaptation, Physiological↗
PubMed1980

Evidence of a specific complex between adriamycin and negatively-charged phospholipids.

Membrane-model systems (monolayers, small unilamellar vesicles) were used to study the interaction between adriamycin (ADM) and phospholipids. Adsorption of 3H-labeled adriamycin on different phospholipid monolayers demonstrated the specificity of adriamycin for negatively-charged phospholipids (cardiolipin, phosphatidylserine, phosphatidic acid). The stoichiometry has been found to be approx. 2 mol (1.8) adriamycin per mol cardiolipin and approx. 1 mol (0.75) adriamycin per mol phosphatidylserine and phosphatidic acid. No adsorption was detected with neutral lipids. Surface-potential measurements confirm the formation of a complex stabilized by electrostatic interactions without penetration of the drug into the lipid lipophilic phase. Some adriamycin derivatives were used to discriminate between the ionized hydrophilic and hydrophobic contributions in the complex formation. The absorption spectrum of adriamycin in the presence of cardiolipin resembles the behavior of the ADM-DNA complex. Moreover, the association constants of the two complexes are very similar (cardiolipin-ADM, 1.6 . 10(6) . M-1; ADM-DNA, 2.4 . 10(6) . M-1). To explain the high affinity of cardiolipin for adriamycin, we proposed that two essential interactions are responsible for the complex stabilization: an electrostatic interaction between the protonated amino groups of the sugar residues and the ionized phosphate residues, and an interaction between adjacent anthraquinone chromophores. These data strongly suggest competitive behavior between a membrane site and the target. Consequently, it must be assumed that the lipidic components of the cell membrane structure may be an important determinant in the behavior of adriamycin. This observation should be kept in mind in the building of new derivatives.

Calorimetry↗
PubMed1988

Biological effects of oxysterols on platelet function.

We have studied the in vitro exposure to various oxysterols on isolated rat platelets. The oxysterols (1-20 uM) were incubated either dissolved in methanol or as albumin-bound complexes. Aggregation (analyzed by turbidimetry) was measured after stimulation by thrombin or ADP. Serotonin secretion (analyzed by voltammetry) was measured after thombin stimulation. We found that platelet aggregation and serotonin secretion could be either not significantly affected (7B-hydroxy cholesterol) or potentiated (22S-hydroxy cholesterol, 3,5,6-hydroxy cholestan triol) or inhibited (25-hydroxy- and 7-oxo cholesterol), after in vitro incubation with different oxysterols. Our data indicate that a modulation of the platelet behavior occurs after in vitro incubation with different oxysterols, some derivatives acting as inhibitors and others as potentiators. These results provide new interesting information regarding the role of these sterols in cell membrane structure and function in relation to pathology.

Animals↗
PubMed1983

Ethanol and dopaminergic systems.

Chronic ethanol consumption produces derangements of cell membrane structure, perhaps by changing membrane lipid content. This impairment leads to modification of membrane-related processes. In fact, after chronic ethanol exposure, an increase in striatal adenylate-cyclase activity occurs. On the other hand, dopamine is unable to further potentiate the production of cyclic AMP. This finding demonstrates that the dopaminergic receptor associated with adenylate-cyclase activity is affected by chronic ethanol treatment. In particular, the affinity of the dopaminergic receptor labelled by 3H-Spiperone is enhanced. In addition, the receptor-adenylate cyclase coupling system is impaired after chronic in vivo exposure of animals to ethanol.

Adenylyl Cyclases↗
PubMed1988

Superoxide dismutase depletion and lipid peroxidation in rat liver microsomal membranes: correlation with liver carcinogenesis.

The depletion of superoxide dismutase in the liver of rats held on a copper-deficient diet for 8 weeks induces two profound modifications in microsomal membrane characteristics. These membranes show: (1) a low degree of peroxidation induced in vitro by both endogenous (NADPH and tert-butylhydroperoxide) and exogenous sources (xanthine/xanthine oxidase) of oxygen radicals as revealed by malondialdehyde and diene-conjugate production; (2) a strong decrease of polyunsaturated and an increase of monounsaturated fatty acid content. These alterations are similar to those found in microsomal membranes from fast-growing hepatomas which exhibit a pronounced saturation of fatty acid pattern and lack superoxide dismutase. These observations support the hypothesis that during hepatocarcinogenesis the loss of superoxide dismutase causes an oxidative stress that increases cellular membrane lipid peroxidation, as a consequence of which the cell responds by synthesizing more saturated fatty acids that permanently modify cell membrane structure and properties.

Animals↗
PubMedDate not supplied

Chronic ethanol exposure alters dopaminergic signal transduction processes.

A number of data suggest that the chronic ethanol treatment induces derangements of cell membrane structure leading to modifications of membrane related processes. In particular, alterations have been observed in the mechanisms of neurotransmitter recognition and in the coupling of the receptor with the effector system. Phosphorylation of specific proteins by cyclic AMP stimulated protein kinases represent the final step in the biological response in several distinct functional processes. Ethanol neurotoxic action therefore may affect neurotransmitter availability and release as well as receptors effector systems and protein phosphorylation. In this line, chronic ethanol treatment in rats decreases cyclic AMP dependent protein kinase activity in rat striatal membrane fractions. When lysine rich histone type III was used as exogenous substrate, cyclic AMP stimulated 32P incorporation was still decreased in the ethanol group. These data favor the hypothesis of a decreased capability of the enzyme to phosphorylate in response to cAMP.

Alcoholism↗
PubMed2006

Inhibitors of sphingolipid metabolism enzymes.

Sphingolipids are a family of lipids that play essential roles both as structural cell membrane components and in cell signalling. The cellular contents of the various sphingolipid species are controlled by enzymes involved in their metabolic pathways. In this context, the discovery of small chemical entities able to modify these enzyme activities in a potent and selective way should offer new pharmacological tools and therapeutic agents.

Amidohydrolases↗
PubMed2006

Epidermal growth factor-induced mobilization of a ganglioside-specific sialidase (NEU3) to membrane ruffles.

Human ganglioside-specific sialidase, NEU3, localized at cell membranes is thought to regulate various biological processes at cell surfaces. We here explored functional subcellular localization of the sialidase by immunofluorescence and found accumulation at leading edges of cell membranes in the presence of serum in culture. In response to EGF, the sialidase redistributed rapidly to ruffling cell membranes of squamous carcinoma A431 cells and co-localized with Rac-1. NEU3 overexpression enhanced Rac-1 activation and cell migration as compared with controls in HeLa cells as well as in A431 cells. Consistent with co-localization with Rac-1 by immunofluorescence, NEU3 was found to co-precipitate with activated Rac bound to GST-PAK-1 fusion protein. NEU3 silencing by siRNA, in contrast, resulted in inhibition of Rac-1 activation. These results indicate that NEU3 is able to mobilize to membrane ruffles in response to growth stimuli and activate the Rac-1 signaling by co-localization with Rac-1, leading to increased cell motility.

Animals↗
PubMed2006

Antibody immobilization to phospholipid polymer layer on gold substrate of quartz crystal microbalance immunosensor.

To modify gold electrode for immunosensor to construct an artificial cell membrane structure, water-soluble amphiphilic phospholipid polymer, poly[2-methacryloyloxyehtyl phosphorylcholine-co-n-butyl methacrylate-co-p-nitrophenyloxycarbonyl poly(ethylene glycol) methacrylate (PMBN)] was applied. The polymer had active ester groups for immobilization of biomolecules and it was converted partially to thiol groups for binding to gold substrates. The partially thiolated PMBN was adsorbed on a gold electrode of quartz crystal microbalance (QCM). Surface characterization of adsorbed PMBN layers was thoroughly investigated with reflectance anisotropy spectroscopy, ellipsometry spectroscopy, dynamic contact angle and X-ray photoelectron spectroscopy measurements. Among several PMBN, having different degree of thiolation, it was concluded that 21.5% thiolated PMBN layer had the most well-ordered phosphorylcholine groups in its outer surface. The proteins adsorption test revealed that the phosphorylcholine group on the outer side of PMBN layers, which was substituted their active ester groups by glycine, showed suppress the non-specific adsorption of proteins, such as bovine serum albumin and gamma-globulin. Also, through antigen-antibody binding evaluation, the anti-C-reactive protein antibody immobilized on the PMBN surface worked well and it was confirmed that denaturation of the antibody on the PMBN layers was hardly occurred in spite of 60 days storage at 4 degrees C. The antibody conjugated phospholipid polymer layer with well-ordered phosphorylcholine group could be outstanding functional membrane for biomedical diagnostic devices without non-specific binding and reduction of immunologic activity of immobilized antibody.

Antibodies↗
PubMed2006

Tracking peptide-membrane interactions: insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly.

Elucidating the role that charged membrane proteins play in determining cell membrane structure and dynamics is an area of active study. We have applied in situ correlated atomic force and confocal microscopies to characterize the interaction of the NAP-22 peptide with model membranes prepared as supported planar bilayers containing both liquid-ordered and liquid-disordered domains. Our results demonstrated that the NAP-22 peptide interacts with membranes in a concentration-dependent manner, preferentially inserting into DOPC (ld) domains. While at low peptide concentrations, the NAP-22 peptide formed aggregate-like structures within the ld domains, at high peptide concentrations, it appeared to sequester cholesterol into the ld domains and recruited phosphatidyl-myo-inositol 4,5-bisphosphate by inducing a blending effect that homogenizes the phase-segregated domains into one liquid-ordered domain. This study describes a possible mechanism by which the NAP-22 peptide can affect neuronal morphology.

Animals↗
PubMed2005

Annexin A5 inhibits engulfment through internalization of PS-expressing cell membrane patches.

Apoptosis and subsequent clearance of apoptotic cells are important for the prevention of diseases. Therefore, it is essential to understand the mechanisms underlying the biology of phagocytic clearance of apoptotic cells. The best characterized "eat me" signal on the surface of apoptotic cells is phosphatidylserine (PS). Recently, we demonstrated that annexin A5 mediates the internalization of PS-expressing membrane patches and down regulates surface expression of tissue factor. Here, we investigated the role of PS in the phagocytosis of apoptotic cells using annexin A5. Using a novel flow cytometric-based phagocytosis assay, we observed that engulfment was inhibited with 20% if annexin A5 was added to PS-expressing cells that had completed apoptosis. The inhibition increased to more than 50% if annexin A5 was added during the apoptotic process. This inhibition is specific for annexin A5, since the mutant M23 and annexin A1 did not further increase the inhibition of phagocytosis when added during the apoptotic process. Interestingly, cells with internalized annexin A5 still express PS at their surface. We conclude that other ligands within the PS-expressing membrane patch act together with PS as an "eat me" signal.

Animals↗
PubMed2006

Cortactin regulates podosome formation: roles of the protein interaction domains.

Cortactin, a multi-domain scaffolding protein involved in actin polymerization, is enriched in podosomes induced by phorbol ester in vascular smooth muscle cells. We generated several functional and truncation mutants of cortactin to probe the roles of various protein interaction domains in the regulation of the dynamics of podosome formation. At the onset of podosome genesis, cortactin clustered near the ends of stress fibers that appeared to act as nucleation platforms onto which the actin polymerization machinery assembled. Translocation of cortactin to these pre-podosome clusters required the intact N-WASp-binding SH3 domain. Overexpression of the C-terminal third of cortactin containing the intact SH3 domain inhibited podosome formation presumably by sequestering of N-WASp and prevented cortactin clustering. Subsequent assembly of the actin-rich core of podosomes required translocation of additional cortactin to the actin core, a process that required the actin-binding repeats, but not the Arp2/3-binding N-terminal acidic region nor the SH3 domain. These results suggest that the SH3 domain and the actin-binding repeat region are involved, respectively, in the early and late stages of podosome formation process.

Actins↗
PubMed2003

Requirement for PI 3-kinase gamma in macrophage migration to MCP-1 and CSF-1.

Phosphoinositide 3-kinases (PI3Ks) are important regulators of cell migration. The PI3K isoform gamma is primarily expressed in haematopoietic cells, and is activated by G protein-coupled receptors (GPCRs). Here, we investigate the contribution of PI3Kgamma to macrophage responses to chemoattractants, using bone marrow-derived macrophages from wild-type and PI3Kgamma-null mice. We observe that early membrane ruffling induced by MCP-1, which activates a GPCR, or by CSF-1, which activates a tyrosine kinase receptor, is unaltered in PI3Kgamma(-/-) mice, although by 30 min MCP-1-induced cell polarization was strongly reduced in PI3Kgamma(-/-) compared to wild-type macrophages. The migration behaviour of the macrophages was analysed by time-lapse microscopy in Dunn chemotaxis chambers. PI3Kgamma(-/-) macrophages showed reduced migration speed and translocation, and no chemotaxis to MCP-1. Interestingly, there was also a reduction in migration efficiency in PI3Kgamma(-/-) macrophages stimulated with CSF-1 although early CSF-1R signalling was normal. These results indicate that the initial actin reorganization induced by either a GPCR or tyrosine kinase receptor agonist is not dependent on PI3Kgamma, whereas PI3Kgamma is needed for optimal migration of macrophages to either agonist.

Actin Cytoskeleton↗
PubMed2000

p(1),p(4)-diadenosine 5'-tetraphosphate induces the uptake of arginine and citrulline by a pore on the plasma membrane of bovine aortic endothelial cells.

We have previously demonstrated that p(1),p(4)-diadenosine 5'-tetraphosphate (Ap(4)A) induces the release of nitric oxide (NO) and modulates the uptake of extracellular L-arginine (L-Arg) and L-citrulline (L-Cit) by bovine aortic endothelial cells (BAEC) [Hilderman, R.H. and Christensen, E.F. (1998) FEBS Lett. 427, 320-324 and Hilderman, R.H., Casey, T.E. and Pojoga, L.H. (2000) Arch. Biochem. Biophys. 375, 124-130]. In this communication we report that extracellular Ap(4)A enhances the uptake of L-Arg and L-Cit through a pore on the plasma membrane of BAEC that is selective for these two amino acids. We also demonstrate that Ap(2)A, which induces NO release, enhances L-Arg uptake while Ap(5)A, a vasoconstrictor, does not enhance the uptake of L-Arg. The potential physiological significance of the uptake of these two amino acids in relation to NO synthesis is discussed.

Animals↗