Cell adhesion to hydroxyl groups of a monolayer film

1988 ◽  
Vol 91 (2) ◽  
pp. 269-279
Author(s):  
N.F. Owens ◽  
D. Gingell ◽  
A. Trommler
Keyword(s):  
Cell Adhesion ◽  
Flow Chamber ◽  
Cell Contact ◽  
Hydroxyl Groups ◽  
Adjacent Area ◽  
Oh Groups ◽  
Monomolecular Films ◽  
Langmuir Blodgett Films ◽  
Long Chain Alcohol ◽  
Minimal Measure

We have studied cells on chemically defined monomolecular films of the long-chain alcohol docosanol. Langmuir-Blodgett films of the alcohol were deposited on glass coverslips, previously made hydrophobic with octadecyl groups. This gives films in which the alcohol headgroups face outwards to the water. Molecular orientation and film integrity were shown by a fluorescence adsorption test. Cell contacts on the films were observed in media without proteins by interference reflection microscopy (IRM) and the mechanics of detachment were examined by hydrodynamic shearing in a flow chamber. Cell contact with docosanol was compared with that on an adjacent area of octadecyl glass without a monolayer. Dictyostelium amoebae settled and spread on both docosanol and octadecyl glass, but little or no locomotion was seen on docosanol. On octadecyl glass the amoebae moved actively, forming ultrathin cytoplasmic lamellae, which look dark under IRM, and left distinctive trails of membranous debris. Hydrodynamic shearing showed that the amoebae stuck strongly to both surfaces and could not be removed from either at the maximum attainable wall shear stress of 6Nm-2. Red blood cells also adhered to both surfaces and removal from both occurred between 1 and 3Nm-2. IRM and scanning electron microscopy (SEM) studies indicated that this force leads to a minimal measure of red cell adhesion, since removal often involved the breakage of cytoplasmic tethers. Our results show that alcoholic -OH groups, in a two-dimensional array, provide a surface that is strongly adhesive for cells. No other method has made it possible to demonstrate cell adhesion purely to -OH groups, in a known orientation and density, and in the absence of any other functional groups on the interface.

scholarly journals Substrate Hydroxylation and Cell Adhesion

1986 ◽  
Vol 86 (1) ◽  
pp. 9-24 ◽  
Author(s):  
A.S. G. CURTIS ◽  
J. V. FORRESTER ◽  
P. CLARK
Keyword(s):  
Cell Adhesion ◽  
High Surface ◽  
Carboxyl Groups ◽  
Hydroxyl Groups ◽  
Oh Groups ◽  
Bhk Cells ◽  
Cellular Origin ◽  
Optimal Surface ◽  
Substrate Hydroxylation ◽  
Serum Free Conditions

Adhesion of BHK cells to a variety of polymer surfaces carrying measured densities of hydroxyl and carboxyl groups was studied. The effects on cell adhesion of blocking hydroxyl groups by acetylation and carboxyl groups with diazomethane were measured. Hydroxyl groups were required for cell adhesion, though the very high surface densities of these groups diminished cell adhesion. The optimal surface density of OH groups for BHK adhesion was 2000 per 1 × 10−11cm2. Carboxyl groups slightly inhibit cell adhesion, since blocking of these groups by methylation increased adhesion. The role of oxidizing systems of cellular origin in conditioning of the substrate, in serum-free conditions, was demonstrated for leucocytes and BHK cells, in particular by the result that oxidizable substrates such as phytane and poly(1,2-butadiene) could be made suitable for cell adhesion by contact with cells.

scholarly journals Development of Highly Efficient, Glassy Carbon Foam Supported, Palladium Catalysts for Hydrogenation of Nitrobenzene

Nanomaterials ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 1172
Author(s):  
Ádám Prekob ◽  
Mahitha Udayakumar ◽  
Gábor Karacs ◽  
Ferenc Kristály ◽  
Gábor Muránszky ◽  
...  
Keyword(s):  
Zeta Potential ◽  
Glassy Carbon ◽  
Palladium Nanoparticles ◽  
Palladium Catalysts ◽  
Sucrose Solution ◽  
Supported Catalyst ◽  
Carbon Foam ◽  
Hydroxyl Groups ◽  
Polyurethane Elastomers ◽  
Oh Groups

Glassy carbon foam (GCF) catalyst supports were synthesized from waste polyurethane elastomers by impregnating them in sucrose solution followed by pyrolysis and activation (AC) using N2 and CO2 gas. The palladium nanoparticles were formed from Pd(NO3)2. The formed palladium nanoparticles are highly dispersive because the mean diameters are 8.0 ± 4.3 (Pd/GCF), 7.6 ± 4.2 (Pd/GCF-AC1) and 4.4 ± 1.6 nm (Pd/GCF-AC2). Oxidative post-treatment by CO2 of the supports resulted in the formation of hydroxyl groups on the GCF surfaces, leading to a decrease in zeta potential. The decreased zeta potential increased the wettability of the GCF supports. This, and the interactions between –OH groups and Pd ions, decreased the particle size of palladium. The catalysts were tested in the hydrogenation of nitrobenzene. The non-treated, glassy-carbon-supported catalyst (Pd/GCF) resulted in a 99.2% aniline yield at 293 K and 50 bar hydrogen pressure, but the reaction was slightly slower than other catalysts. The catalysts on the post-treated (activated) supports showed higher catalytic activity and the rate of hydrogenation was higher. The maximum attained aniline selectivities were 99.0% (Pd/GCF-AC1) at 293 K and 98.0% (Pd/GCF-AC2) at 323 K.

scholarly journals Eap1p, an Adhesin That Mediates Candida albicans Biofilm Formation In Vitro and In Vivo

2007 ◽  
Vol 6 (6) ◽  
pp. 931-939 ◽  
Author(s):  
Fang Li ◽  
Michael J. Svarovsky ◽  
Amy J. Karlsson ◽  
Joel P. Wagner ◽  
Karen Marchillo ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Cell Adhesion ◽  
Biofilm Formation ◽  
Fungal Infections ◽  
Gene Dosage ◽  
Venous Catheter ◽  
Flow Chamber ◽  
Dependent Manner

ABSTRACT Candida albicans is the leading cause of systemic fungal infections in immunocompromised humans. The ability to form biofilms on surfaces in the host or on implanted medical devices enhances C. albicans virulence, leading to antimicrobial resistance and providing a reservoir for infection. Biofilm formation is a complex multicellular process consisting of cell adhesion, cell growth, morphogenic switching between yeast form and filamentous states, and quorum sensing. Here we describe the role of the C. albicans EAP1 gene, which encodes a glycosylphosphatidylinositol-anchored, glucan-cross-linked cell wall protein, in adhesion and biofilm formation in vitro and in vivo. Deleting EAP1 reduced cell adhesion to polystyrene and epithelial cells in a gene dosage-dependent manner. Furthermore, EAP1 expression was required for C. albicans biofilm formation in an in vitro parallel plate flow chamber model and in an in vivo rat central venous catheter model. EAP1 expression was upregulated in biofilm-associated cells in vitro and in vivo. Our results illustrate an association between Eap1p-mediated adhesion and biofilm formation in vitro and in vivo.

scholarly journals Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein alpha-agglutinin, a member of the immunoglobulin superfamily.

1993 ◽  
Vol 13 (4) ◽  
pp. 2554-2563 ◽  
Author(s):  
D Wojciechowicz ◽  
C F Lu ◽  
J Kurjan ◽  
P N Lipke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Adhesion ◽  
Amino Acid ◽  
Cell Surface ◽  
Consensus Sequence ◽  
Binding Domain ◽  
Immunoglobulin Superfamily ◽  
Cell Contact ◽  
Amino Acid Residues ◽  
Adhesion Proteins

alpha-Agglutinin is a cell adhesion glycoprotein expressed on the cell wall of Saccharomyces cerevisiae alpha cells. Binding of alpha-agglutinin to its ligand a-agglutinin, expressed by a cells, mediates cell-cell contact during mating. Analysis of truncations of the 650-amino-acid alpha-agglutinin structural gene AG alpha 1 delineated functional domains of alpha-agglutinin. Removal of the C-terminal hydrophobic sequence allowed efficient secretion of the protein and loss of cell surface attachment. This cell surface anchorage domain was necessary for linkage to a glycosyl phosphatidylinositol anchor. A construct expressing the N-terminal 350 amino acid residues retained full a-agglutinin-binding activity, localizing the binding domain to the N-terminal portion of alpha-agglutinin. A 278-residue N-terminal peptide was inactive; therefore, the binding domain includes residues between 278 and 350. The segment of alpha-agglutinin between amino acid residues 217 and 308 showed significant structural and sequence similarity to a consensus sequence for immunoglobulin superfamily variable-type domains. The similarity of the alpha-agglutinin-binding domain to mammalian cell adhesion proteins suggests that this structure is a highly conserved feature of adhesion proteins in diverse eukaryotes.

Adsorption of Benzene from Aqueous Solution Using Base Modified Expanded Perlite

2012 ◽  
Vol 622-623 ◽  
pp. 1779-1783
Author(s):  
Richard Appiah-Ntiamoah ◽  
Xuan Thang Mai ◽  
Francis W.Y. Momade ◽  
Hern Kim
Keyword(s):  
Zeta Potential ◽  
Adsorption Capacity ◽  
Linear Regression Analysis ◽  
Basic Medium ◽  
Maximum Adsorption Capacity ◽  
Hydroxyl Groups ◽  
Expanded Perlite ◽  
Oh Groups ◽  
Base Solution ◽  
Ph Range

In this study, the adsorption capacity of expanded perlite (EP) for benzene at low concentrations in water was investigated after EP was treated with sodium hydroxide (NaOH). IR spectra used to characterize the modified EP showed that there was no bonding between NaOH and the hydroxyl groups on the surface of EP. However, the NaOH provided a basic medium for negatively charged surface oxide ions (-SO-) to form on EP. This fact was corroborated by pH readings of the modification solution. This reduced in pH from 10 to 9 at the end of the reaction which indicated that the hydroxyl OH- groups on the EP underwent deprotonation and hence releases H+ into the solution, and also positive sites on EP adsorbed OH- ions from the base solution. Mahir et al. in their paper Zeta potential of unexpanded and expanded perlite samples in various electrolyte media confirmed that EP has no isoelectric point and exhibits negative zeta potential in the pH range of 2-11. The surface oxides (-SO-) were believed to have given EP it adsorptive potential. Adsorption isotherm values correlated reasonably well with the Langmuir isotherm model and it parameters (qo and K) were obtained using linear regression analysis. A maximum adsorption capacity (qo) value of 19.42 mg/g was achieved.

scholarly journals Changes in E-cadherin rigidity sensing regulate cell adhesion

2017 ◽  
Vol 114 (29) ◽  
pp. E5835-E5844 ◽  
Author(s):  
Caitlin Collins ◽  
Aleksandra K. Denisin ◽  
Beth L. Pruitt ◽  
W. James Nelson
Keyword(s):  
Cell Adhesion ◽  
Signaling Molecules ◽  
Membrane Dynamics ◽  
Cell Contact ◽  
Adhesion Assay ◽  
Cell Periphery ◽  
Actin Organization ◽  
Rigidity Sensing ◽  
E Cadherin ◽  
Cell Cell

Mechanical cues are sensed and transduced by cell adhesion complexes to regulate diverse cell behaviors. Extracellular matrix (ECM) rigidity sensing by integrin adhesions has been well studied, but rigidity sensing by cadherins during cell adhesion is largely unexplored. Using mechanically tunable polyacrylamide (PA) gels functionalized with the extracellular domain of E-cadherin (Ecad-Fc), we showed that E-cadherin–dependent epithelial cell adhesion was sensitive to changes in PA gel elastic modulus that produced striking differences in cell morphology, actin organization, and membrane dynamics. Traction force microscopy (TFM) revealed that cells produced the greatest tractions at the cell periphery, where distinct types of actin-based membrane protrusions formed. Cells responded to substrate rigidity by reorganizing the distribution and size of high-traction-stress regions at the cell periphery. Differences in adhesion and protrusion dynamics were mediated by balancing the activities of specific signaling molecules. Cell adhesion to a 30-kPa Ecad-Fc PA gel required Cdc42- and formin-dependent filopodia formation, whereas adhesion to a 60-kPa Ecad-Fc PA gel induced Arp2/3-dependent lamellipodial protrusions. A quantitative 3D cell–cell adhesion assay and live cell imaging of cell–cell contact formation revealed that inhibition of Cdc42, formin, and Arp2/3 activities blocked the initiation, but not the maintenance of established cell–cell adhesions. These results indicate that the same signaling molecules activated by E-cadherin rigidity sensing on PA gels contribute to actin organization and membrane dynamics during cell–cell adhesion. We hypothesize that a transition in the stiffness of E-cadherin homotypic interactions regulates actin and membrane dynamics during initial stages of cell–cell adhesion.

Homogeneous synthesis of GRGDY grafted chitosan on hydroxyl groups by photochemical reaction for improved cell adhesion

2010 ◽  
Vol 80 (3) ◽  
pp. 733-739 ◽  
Author(s):  
Yan Yang ◽  
Xiudong Liu ◽  
Weiting Yu ◽  
Houjiang Zhou ◽  
Xiaoxia Li ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Photochemical Reaction ◽  
Hydroxyl Groups ◽  
Homogeneous Synthesis

Proton spin–spin coupling constants and intramolecular hydrogen bonding in bromine derivatives of 1,3-dihydroxybenzene

1976 ◽  
Vol 54 (14) ◽  
pp. 2228-2230 ◽  
Author(s):  
Ted Schaefer ◽  
J. Brian Rowbotham
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonding ◽  
Proton Spin ◽  
Coupling Constants ◽  
Spin Coupling ◽  
Hydroxyl Groups ◽  
Oh Groups ◽  
Spin Coupling Constants ◽  
Spin Spin Coupling ◽  
Derivatives Of

The conformational preferences in CCl4 solution at 32 °C of the hydroxyl groups in bromine derivatives of 1,3-dihydroxybenzene are deduced from the long-range spin–spin coupling constants between hydroxyl protons and ring protons over five bonds. Two hydroxyl groups hydrogen bond to the same bromine substituent in 2-bromo-1,3-dihydroxybenzene but prefer to hydrogen bond to different bromine substituents when available, as in 2,4-dibromo-1,3-dihydroxybenzene. When the OH groups can each choose between two ortho bromine atoms, as in 2,4,6-tribromoresorcinol, they apparently do so in a very nearly statistical manner except that they avoid hydrogen bonding to the common bromine atom.

scholarly journals The Role of Carboxyl and Hydroxyl Groups of Humic Acid in Removing AuCl4- from Aqueous Solution

2017 ◽  
Vol 17 (1) ◽  
pp. 95 ◽  
Author(s):  
Sri Sudiono ◽  
Mustika Yuniarti ◽  
Dwi Siswanta ◽  
Eko Sri Kunarti ◽  
Triyono Triyono ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Humic Acid ◽  
Peat Soil ◽  
Sharp Decrease ◽  
Hydroxyl Groups ◽  
Mixed Solution ◽  
Oh Groups ◽  
Characterization Result ◽  
Ft Ir

Humic acid (HA) extracted from peat soil according to the recommended procedure of the International Humic Substances Society (IHSS) has been tested to remove AuCl4- from aqueous solution. The removal was optimum at pH 2.0 and it was mainly dictated by attachment through hydrogen bonding to unionized carboxyl (–COOH) groups and reduction by the action of the hydroxyl (–OH) groups to gold (Au) metal. The removal of AuCl4- improved after HA was purified through repeated immersion and shaking in a mixed solution containing 0.1 M HCl and 0.3 M HF. When the purification led to the sharp decrease in ash content from 39.34 to 0.85% (w/w) and significant increase in both the –COOH and –OH contents from 3240 to 3487 mmol/kg and from 4260 to 4620 mmol/kg, respectively; the removal of AuCl4- improved from 0.105 to 0.133 mmol/g. This improvement of AuCl4- removal by the purified HA was accompanied by higher ability in reduction to Au metal. The attached AuCl4- on –COOH groups of both crude and purified HAs was qualitatively observed by the characterization result of FT-IR spectroscopy, while the presence of Au metal on the surface of those HAs was verified by the characterization result of XRD.

Antisense RNA inactivation of gene expression of a cell-cell adhesion protein (gp64) in the cellular slime mold Polysphondylium pallidum

1996 ◽  
Vol 109 (5) ◽  
pp. 1009-1016
Author(s):  
S. Funamoto ◽  
H. Ochiai
Keyword(s):  
Gene Expression ◽  
Cell Adhesion ◽  
Antisense Rna ◽  
Resistant Cell ◽  
Cell Contact ◽  
Cellular Slime Mold ◽  
Adhesion Protein ◽  
Cell Adhesion Protein ◽  
Polysphondylium Pallidum ◽  
Cell Cell

The gp64 protein of Polysphondylium pallidum has been shown to mediate EDTA-stable cell-cell adhesion. To explore the functional role of gp64, we made an antisense RNA expression construct designed to prevent the gene expression of gp64; the construct was introduced into P. pallidum cells and the transformants were characterised. The antisense RNA-expressing clone L3mc2 which had just been harvested at the growth phase tended to re-form in aggregates smaller in size than did the parental cells in either the presence or absence of 10 mM EDTA. In contrast, 6.5-hour starved L3mc2 cells remained considerably dissociated from each other after 5 minutes gyrating, although aggregation gradually increased by 50% during a further 55 minutes gyrating in the presence of 10 mM EDTA. Correspondingly, L3mc2 lacked specifically the cell-cell adhesion protein, gp64. We therefore conclude that the gp64 protein is involved in forming the EDTA-resistant cell-cell contact. In spite of the absence of gp64, L3mc2 exhibited normal developmental processes, a fact which demonstrates that another cell-cell adhesion system exists in the development of Polysphondylium. This is the first report in which an antisense RNA technique was successfully applied to Polysphondylium.

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