scholarly journals Amino Acid-Functionalized Polyelectrolyte Films as Bioactive Surfaces for Cell Adhesion

2019 ◽  
Vol 11 (22) ◽  
pp. 19751-19762 ◽  
Author(s):  
M. S. Leal ◽  
X. Briones ◽  
V. Villalobos ◽  
Y. Queneau ◽  
A. Leiva ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Bioactive Surfaces

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.

scholarly journals Carborane–β-cyclodextrin complexes as a supramolecular connector for bioactive surfaces

2015 ◽  
Vol 3 (4) ◽  
pp. 539-545 ◽  
Author(s):  
P. Neirynck ◽  
J. Schimer ◽  
P. Jonkheijm ◽  
L.-G. Milroy ◽  
P. Cigler ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Biologically Active ◽  
Cyclodextrin Complexes ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Bioactive Surfaces

The supramolecular carborane–β-cyclodextrin system allows for effective monovalent immobilization of biologically active peptides resulting in efficient cell adhesion and spreading.

scholarly journals Ankyrin-binding proteins related to nervous system cell adhesion molecules: candidates to provide transmembrane and intercellular connections in adult brain.

1993 ◽  
Vol 121 (1) ◽  
pp. 121-133 ◽  
Author(s):  
J Q Davis ◽  
T McLaughlin ◽  
V Bennett
Keyword(s):  
Nervous System ◽  
Cell Adhesion ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Binding Proteins ◽  
Cytoplasmic Domain ◽  
System Cell

A major class of ankyrin-binding glycoproteins have been identified in adult rat brain of 186, 155, and 140 kD that are alternatively spliced products of the same pre-mRNA. Characterization of cDNAs demonstrated that ankyrin-binding glycoproteins (ABGPs) share 72% amino acid sequence identity with chicken neurofascin, a membrane-spanning neural cell adhesion molecule in the Ig super-family expressed in embryonic brain. ABGP polypeptides have the following features consistent with a role as ankyrin-binding proteins in vitro and in vivo: (a) ABGPs and ankyrin associate as pure proteins in a 1:1 molar stoichiometry; (b) the ankyrin-binding site is located in the COOH-terminal 21 kD of ABGP186 which contains the predicted cytoplasmic domain; (c) ABGP186 is expressed at approximately the same levels as ankyrin (15 pmoles/milligram of membrane protein); and (d) ABGP polypeptides are co-expressed with the adult form of ankyrinB late in postnatal development and are colocalized with ankyrinB by immunofluorescence. Similarity in amino acid sequence and conservation of sites of alternative splicing indicate that genes encoding ABGPs and neurofascin share a common ancestor. However, the major differences in developmental expression reported for neurofascin in embryos versus the late postnatal expression of ABGPs suggest that ABGPs and neurofascin represent products of gene duplication events that have subsequently evolved in parallel with distinct roles. The predicted cytoplasmic domains of rat ABGPs and chicken neurofascin are nearly identical to each other and closely related to a group of nervous system cell adhesion molecules with variable extracellular domains, which includes L1, Nr-CAM, and Ng-CAM of vertebrates, and neuroglian of Drosophila. The ankyrin-binding site of rat ABGPs is localized to the C-terminal 200 residues which encompass the cytoplasmic domain, suggesting the hypothesis that ability to associate with ankyrin may be a shared feature of neurofascin and related nervous system cell adhesion molecules.

scholarly journals Structural requirements for neural cell adhesion molecule-heparin interaction.

1990 ◽  
Vol 1 (8) ◽  
pp. 567-576 ◽  
Author(s):  
A A Reyes ◽  
R Akeson ◽  
L Brezina ◽  
G J Cole
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Adhesion Molecule ◽  
Synthetic Peptides ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Basic Amino Acid ◽  
Retinal Cell ◽  
Heparin Binding ◽  
Neural Cell Adhesion

Two biological domains have been identified in the amino terminal region of the neural cell adhesion molecule (NCAM): a homophilic-binding domain, responsible for NCAM-NCAM interactions, and a heparin-binding domain (HBD). It is not known whether these two domains exist as distinct structural entities in the NCAM molecule. To approach this question, we have further defined the relationship between NCAM-heparin binding and cell adhesion. A putative HBD consisting of two clusters of basic amino acid residues located close to each other in the linear amino acid sequence of NCAM has previously been identified. Synthetic peptides corresponding to this domain were shown to bind both heparin and retinal cells. Here we report the construction of NCAM cDNAs with targeted mutations in the HBD. Mouse fibroblast cells transfected with the mutant cDNAs express NCAM polypeptides with altered HBD (NCAM-102 and NCAM-104) or deleted HBD (HBD-) at levels similar to those of wild-type NCAM. Mutant NCAM polypeptides purified from transfected cell lines have substantially reduced binding to heparin and fail to promote chick retinal cell attachment. Furthermore, whereas a synthetic peptide that contains both basic amino acid clusters inhibits retinal-cell adhesion to NCAM-coated dishes, synthetic peptides in which either one of the two basic regions is altered to contain only neutral amino acids do not inhibit this adhesion. These results confirm that this region of the NCAM polypeptide does indeed mediate not only the large majority of NCAM's affinity for heparin but also a significant portion of the cell-adhesion-mediating capability of NCAM.

scholarly journals Amino acid sequences mediating vascular cell adhesion molecule 1 binding to integrin alpha 4: homologous DSP sequence found for JC polyoma VP1 coat protein

2013 ◽  
Vol 5 (3) ◽  
pp. 14
Author(s):  
Michael Andrew Meyer
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Coat Protein ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Amino Acid Sequences ◽  
Vascular Cell Adhesion ◽  
Vascular Cell ◽  
Vascular Cell Adhesion Molecule ◽  
Cell Adhesion Molecule 1

<p>The JC polyoma viral coat protein VP1 was analyzed for amino acid sequences homologies to the IDSP sequence which mediates binding of VLA-4 (integrin alpha 4) to vascular cell adhesion molecule 1. Although the full sequence was not found, a DSP sequence was located near the critical arginine residue linked to infectivity of the virus and binding to sialic acid containing molecules such as integrins (3). For the JC polyoma virus, a DSP sequence was found at residues 70, 71 and 72 with homology also noted for the mouse polyoma virus and SV40 virus. Three dimensional modeling of the VP1 molecule suggests that the DSP loop has an accessible site for interaction from the external side of the assembled viral capsid pentamer.</p>

scholarly journals The Impact of Bioactive Surfaces in the Early Stages of Osseointegration: An In Vitro Comparative Study Evaluating the HAnano® and SLActive® Super Hydrophilic Surfaces

2020 ◽  
Vol 2020 ◽  
pp. 1-11
Author(s):  
Rodrigo A. da Silva ◽  
Geórgia da Silva Feltran ◽  
Marcel Rodrigues Ferreira ◽  
Patrícia Fretes Wood ◽  
Fabio Bezerra ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Adhesion ◽  
Cell Cycle Progression ◽  
Cellular Adhesion ◽  
Biological Behavior ◽  
Early Stages ◽  
Genes Encoding ◽  
Bioactive Surfaces ◽  
The Impact

There is an increased effort on developing novel and active surfaces in order to accelerate their osteointegration, such as nanosized crystalline hydroxyapatite coating (HAnano®). To better understand the biological behavior of osteoblasts grown on HAnano® surface, the set of data was compared with SLActive®, a hydrophilic sandblasted titanium surface. Methodologically, osteoblasts were seeded on both surfaces up to 72 hours, to allow evaluating cell adhesion, viability, and set of genes encoding proteins related with adhesion, proliferation, and differentiation. Our data shows HAnano® displays an interesting substrate to support cell adhesion with typical spread morphologic cells, while SLActive®-adhering cells presented fusiform morphology. Our data shows that the cellular adhesion mechanism was accompanied with upexpression of integrin β1, Fak, and Src, favoring the assembling of focal adhesion platforms and coupling cell cycle progression (upmodulating of Cdk2, Cdk4, and Cdk6 genes) in response to HAnano®. Additionally, both bioactive surfaces promoted osteoblast differentiation stimulus, by activating Runx2, Osterix, and Alp genes. Although both surfaces promoted Rankl gene expression, Opg gene expression was higher in SLActive® and this difference reflected on the Rankl/Opg ratio. Finally, Caspase1 gene was significantly upmodulated in response to HAnano® and it suggests an involvement of the inflammasome complex. Collectively, this study provides enough evidences to support that the nanohydroxyapatite-coated surface provides the necessary microenvironment to drive osteoblast performance on dental implants and these stages of osteogenesis are expected during the early stages of osseointegration.

Peptide microarrays for the discovery of bioactive surfaces that guide cellular processes: a single step azide–alkyne “click” chemistry approach

2014 ◽  
Vol 2 (27) ◽  
pp. 4280-4288 ◽  
Author(s):  
Douglas Zhang ◽  
Kristopher A. Kilian
Keyword(s):  
Cell Adhesion ◽  
Click Chemistry ◽  
Single Step ◽  
Cellular Processes ◽  
Peptide Microarrays ◽  
Bioactive Surfaces

Mixed peptide microarrays were formed in a single step using copper-catalyzed “click” chemistry for exploring cell adhesion and differentiation.

Occludin confers adhesiveness when expressed in fibroblasts

1997 ◽  
Vol 110 (9) ◽  
pp. 1113-1121 ◽  
Author(s):  
C.M. Van Itallie ◽  
J.M. Anderson
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tight Junctions ◽  
Synthetic Peptides ◽  
Integral Membrane Protein ◽  
Cell Contact ◽  
Suspended Cell ◽  
Extracellular Loops ◽  
Cell Cell

Occludin is an integral membrane protein specifically associated with tight junctions. Previous studies suggest it is likely to function in forming the intercellular seal. In the present study, we expressed occludin under an inducible promotor in occludin-null fibroblasts to determine whether this protein confers intercellular adhesion. When human occludin is stably expressed in NRK and Rat-1 fibroblasts, which lack endogenous occludin and tight junctions but do have well developed ZO-1-containing adherens-like junctions, occludin colocalizes with ZO-1 to points of cell-cell contact. In contrast, L-cell fibroblasts which lack cadherin-based adherens junctions, target neither ZO-1 nor occludin to sites of cell contact. Occludin-induced adhesion was next quantified using a suspended cell assay. In NRK and Rat-1 cells, occludin expression induces adhesion in the absence of calcium, thus independent of cadherin-cadherin contacts. In contrast, L-cells are nonadhesive in this assay and show no increase in adhesion after induction of occludin expression. Binding of an antibody to the first of the putative extracellular loops of occludin confirmed that this sequence was exposed on the cell surface, and synthetic peptides containing the amino acid sequence of this loop inhibit adhesion induced by occludin expression. These results suggest that the extracellular surface of occludin is directly involved in cell-cell adhesion and the ability to confer adhesiveness correlates with the ability to colocalize with its cytoplasmic binding protein, ZO-1.

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