Comments on the Clinical Application of Fibronectin in Dentistry

1988 ◽  
Vol 67 (2) ◽  
pp. 515-517 ◽  
Author(s):  
B.S. Pearson ◽  
R.J. Klebe ◽  
B.D. Boyan ◽  
D. Moskowicz
Keyword(s):  
Cell Adhesion ◽  
Oral Surgery ◽  
Cell Attachment ◽  
Root Surface ◽  
Tooth Surface ◽  
Tooth Surfaces ◽  
Tissue Attachment ◽  
Cell Adhesion Proteins ◽  
Demineralized Bone

Several studies have demonstrated that citric acid demineralization of the root surface promotes tissue attachment. Since demineralization exposes collagen to which fibronectin binds, the role of fibronectin in the attachment of cells to the tooth surface has been of considerable interest. It is clear that fibronectin and other cell adhesion proteins can promote cell attachment to the tooth surface; therefore, attempts have been made to utilize these findings in a clinical setting. Using a quantitative ELISA procedure to measure the binding of fibronectin to demineralized bone and tooth, we have found that I μg fibronectin can saturate approximately 1 mg of either demineralized bone or demineralized tooth powder. Since serum contains 300 μg fibronectin per mL, the bleeding that occurs during oral surgery should saturate exposed tooth surfaces with amounts of fibronectin adequate for cell adhesion. Thus, exogenous fibronectin would appear to be of little clinical benefit.

scholarly journals Glycosylation of CD44 is implicated in CD44-mediated cell adhesion to hyaluronan.

1996 ◽  
Vol 132 (6) ◽  
pp. 1199-1208 ◽  
Author(s):  
A Bartolazzi ◽  
A Nocks ◽  
A Aruffo ◽  
F Spring ◽  
I Stamenkovic
Keyword(s):  
Cell Adhesion ◽  
Regulatory Mechanism ◽  
Cell Attachment ◽  
Glycosylation Site ◽  
Side Chain ◽  
Site Specific ◽  
Coated Substrate ◽  
Glycosylation Sites ◽  
Coated Surfaces

CD44-mediated cell adhesion to hyaluronate is controlled by mechanisms which are poorly understood. In the present work we examine the role of N-linked glycosylation and Ser-Gly motifs in regulating CD44-hyaluronate interaction. Our results show that treatment of a panel of human cell lines which constitutively express CD44 with the inhibitor of N-linked glycosylation tunicamycin results in the loss of attachment of these cells to hyaluronate-coated substrate. In contrast, treatment of the same cells with deoxymannojirimycin, which inhibits the conversion of high mannose oligosaccharides to complex N-linked carbohydrates, results in either no change or an increase in CD44-mediated adhesion to hyaluronate, suggesting that complex N-linked oligosaccharides may not be required for and may even inhibit CD44-HA interaction. Using human melanoma cells stably transfected with CD44 N-linked glycosylation site-specific mutants, we show that integrity of five potential N-linked glycosylation sites within the hyaluronate recognition domain of CD44 is critical for hyaluronate binding. Mutation of any one of these potential N-linked glycosylation sites abrogates CD44-mediated melanoma cell attachment to hyaluronate-coated surfaces, suggesting that all five sites are necessary to maintain the HA-recognition domain in the appropriate conformation. We also demonstrate that mutation of serine residues which constitute the four Ser-Gly motifs in the membrane proximal domain, and provide potential sites for glycosaminoglycan side chain attachment, impairs hyaluronate binding. Taken together, these observations indicate that changes in glycosylation of CD44 can have profound effects on its interaction with hyaluronic acid and suggest that glycosylation may provide an important regulatory mechanism of CD44 function.

Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion

1990 ◽  
Vol 95 (2) ◽  
pp. 263-277
Author(s):  
V.A. Lightner ◽  
H.P. Erickson
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Attachment ◽  
Solid Phase ◽  
Fluid Phase ◽  
Matrix Proteins ◽  
And Migration ◽  
Cover Up ◽  
Plastic Substratum

Hexabrachion is a large glycoprotein of the extracellular matrix (ECM) that is prominent in embryogenesis, wound healing and tumorigenesis. Because of the role of extracellular matrix proteins in the regulation of cell differentiation and migration, the interaction of hexabrachion with cells as well as with other components of the ECM is of great interest. Early reports suggested that hexabrachion does not bind to fibronectin or gelatin but does bind to chondroitin sulfate proteoglycans. However, more recent reports have suggested that hexabrachion binds to fibronectin and inhibits cell adhesion as well as cell migration on fibronectin. We have found no evidence of strong hexabrachion-fibronectin binding on either a solid-phase ELISA assay or in a fluid-phase sedimentation assay in which the reactants were allowed to dissociate. However, hexabrachion sedimentation was accelerated in a gradient containing fibronectin throughout. This demonstrates an association between hexabrachions and fibronectin, but the complex is apparently weak and readily reversible. The solid-phase ELISA also shows no evidence of hexabrachion binding to gelatin, laminin or types I, III, IV or V collagen. Hexabrachion does not support strong cell attachment of the cell lines tested. Moreover, hexabrachion can inhibit cell attachment to fibronectin. We demonstrate here that this inhibition requires the hexabrachion to be able to bind to the plastic substratum. The results suggest that hexabrachion inhibition is via a steric inhibition. When the hexabrachion molecules bind to the plastic, they cover up a significant fraction of the underlying fibronectin molecules. Antibody studies are presented that show that hexabrachion can nonspecifically block access of immunoglobulin G molecules to the underlying matrix. This steric blocking is not unique to hexabrachion.

scholarly journals Murine granulocytic cell adhesion to bone marrow hemonectin is mediated by mannose and galactose

Blood ◽  
1995 ◽  
Vol 86 (1) ◽  
pp. 135-140 ◽  
Author(s):  
BA Sullenbarger ◽  
MS Petitt ◽  
P Chong ◽  
MW Long ◽  
MS Wicha
Keyword(s):  
Bone Marrow ◽  
Cell Adhesion ◽  
Cell Attachment ◽  
Lectin Binding ◽  
Specific Attachment ◽  
Dependent Inhibition ◽  
Apparent Decrease ◽  
Dose Dependent Inhibition ◽  
Dose Dependent

Hemonectin (HN) is a bone marrow (BM) protein that promotes specific attachment of immature granulocytes and their precursors within the BM. We report that HN is a glycoprotein containing both mannose and galactose residues, and provide evidence that these carbohydrates mediate granulocytic cell adhesion to HN. Carbohydrate structure was determined by digoxigenin-conjugated lectin binding to HN and indicated the presence of mannose, galactose, sialic acid, and the absence of fucose-linked oligosaccharides. The role of carbohydrates in mediating cell adhesion was examined by chemical and enzymatic deglycosylation. Deglycosylation of HN with trifluoromethanesulfonic acid, which cleaves N- and O-linked oligosaccharides, inhibits 66% of cell attachment to HN, and results in an apparent decrease in molecular weight from 60 to 50 kD. Enzymatic deglycosylation with endo-B-N-acetylglucosaminidase H, which hydrolyzes specific N-linked mannose residues, inhibits 30% of cell adhesion to HN. Finally, the role of these specific sugars in hemonectin-mediated cell adhesion was confirmed with neoglycoprotein blocking. Preincubation of BM cells with mannosyl- and galactosyl-BSA probes produces a dose-dependent inhibition of cell attachment to HN, whereas fucosyl-BSA does not inhibit cell adhesion to HN. These results show that mannose and galactose partially mediate adhesion of BM granulocytes to HN.

The role of cell adhesion proteins?laminin and fibronectin?in the movement of malignant and metastatic cells

1985 ◽  
Vol 4 (2) ◽  
pp. 125-152 ◽  
Author(s):  
James B. McCarthy ◽  
Michael L. Basara ◽  
Sally L. Palm ◽  
Daryl F. Sas ◽  
Leo T. Furcht
Keyword(s):  
Cell Adhesion ◽  
Adhesion Proteins ◽  
Metastatic Cells ◽  
Cell Adhesion Proteins

scholarly journals Role of Myosin II in Axon Outgrowth

2003 ◽  
Vol 51 (4) ◽  
pp. 421-428 ◽  
Author(s):  
Jacquelyn Brown ◽  
Paul C. Bridgman
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Myosin Ii ◽  
Traction Force ◽  
Growth Cones ◽  
Matrix Proteins ◽  
Retrograde Flow ◽  
Complex Interactions ◽  
Cell Adhesion Proteins

The initial stages of nerve outgrowth carried out by growth cones occur in three fundamental cyclic steps. Each of these steps appears to require myosin II activity to variable degrees. The steps include the following: (a) exploration, involving extensions and retractions that are driven and controlled by the interaction of actin retrograde flow and polymerization; (b) adhesion of new extensions to the substrate, which has been shown to be mediated by complex interactions between extracellular matrix proteins, cell adhesion proteins, and the actin cytoskeleton; and (c) traction force generated during forward advance of the growth cone, resulting in the production of tension on the neurite.

scholarly journals Conditions for fibroblast adhesion without fibronectin

1986 ◽  
Vol 86 (1) ◽  
pp. 25-33
Author(s):  
A.S. Curtis ◽  
H. McMurray
Keyword(s):  
Cell Adhesion ◽  
Low Temperatures ◽  
Cell Attachment ◽  
Culture Conditions ◽  
Cell Binding ◽  
Good Adhesion ◽  
Fibroblast Adhesion ◽  
Fibronectin Binding ◽  
Serum Components

Conditions that permit the adhesion of BHK fibroblasts to a variety of surfaces after inhibition of protein synthesis and competition of any adsorbed fibronectin or vitronectin with the fibronectin cell-binding tetrapeptide, Arg-Gly-Asp-Ser (RGDS), are defined. Exposure of the cells to serum components at any stage in the preparation prevents cell attachment if cycloheximide or fibronectin tetrapeptide is present. If leupeptin is used cell adhesion and spreading occur even when all fibronectin synthesis is suppressed by cycloheximide inhibition, or fibronectin binding by tetrapeptide competition. The adhesions formed under these conditions appear by interference-reflection microscopy and by general properties to be identical to those formed by cells under normal culture conditions. The cell suspensions produced in the presence of leupeptin rather than other trypsin inhibitors show good adhesion at low temperatures, though the cells hardly spread at all. The results suggest that the role of fibronectin in cell adhesion should be reinterpreted in terms of its possible action as an activator rather than as a bonding molecule.

scholarly journals Histological changes in periodontal tissue caused by the application of citric acid in the treatment of periodontal disease

2007 ◽  
Vol 54 (4) ◽  
pp. 211-223
Author(s):  
Ruzica Nedeljkovic ◽  
Petar Bojic ◽  
Obrad Zelic
Keyword(s):  
Citric Acid ◽  
Periodontal Disease ◽  
Root Surface ◽  
Tooth Surface ◽  
Control Group ◽  
Periodontal Tissue ◽  
Full Width ◽  
Tooth Surfaces ◽  
Experimental Group ◽  
Exposed Root

Introduction: Surface conditioning of teeth with periodontal disease in the surgical treatment of periodontal disease has an important role in the reparation of periodontal tissue. The aim of this study was to evaluate histologically the effect of citric acid on the induction of connective tissue attachment, i.e. cementogenesis and the resorption of cementum and dentin after flap reposition on the exposed tooth surfaces. Materials and Methods: The study was conducted on 12 "White Landras" pigs, 6 male and 6 female, with deciduous dentition. The "split mouth" technique was used for more adequate assessment and comparison of data. Exposed surfaces of the upper left canine were treated with laterally positioned flap (LPF) and their counterparts with free gingival graft (FGG). The recipient site was prepared by tissue excision and the tooth surface was prepared using hand instruments. The donor site for LPF was the edentulous region lateral to the treated tooth, where the full width flap was lifted to completely cover the exposed root surface over the enamel-cementum junction. In the experimental group, a fresh solution of citric acid (pH=1) was applied for 3-5 min with a sterile cotton pellet prior to the flap reposition. The tooth was rinsed with saline and the wound was sutured with single sutures. In the control group, the identical surgical treatment was performed but without citric acid. FGG, i.e. half width flap taken from the edentulous region lateral to the treated teeth, was used to cover the exposed tooth surfaces. Prior to FGG positioning in the experimental group, citric acid was applied in the same manner as in animals treated with LPF. The graft covered the exposed root surface. Fixation was done with single sutures and the wound was additionally preserved with surgical dressing. The control group was treated without citric acid. The animals were sacrificed eight weeks after the treatment. The material was prepared in a routine manner for histological sampling under light microscopy. After 10% formalin fixation, the material was decalcified for 7-10 days. Paraffin molds were cut in 5 ?m thick slices which were stained with haematoxylin eosin (HE), Masson-Trichrome and Paf-Hallmi. Periodontal tissue status in experimental animals was analyzed under the light microscope. Results: Citric acid applied on the exposed tooth surface during the flap surgery had a positive effect on cementogenesis. Cementoblasts were observed along root cementum in thick rows. Newly formed cementum was hyperplastic, with regular laminar structure and more evident on animal models treated with full width flap. No damage of odontoblasts or pulpal connective tissue was observed.

scholarly journals Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion

2012 ◽  
Vol 197 (6) ◽  
pp. 819-836 ◽  
Author(s):  
Fangliang Zhang ◽  
Sougata Saha ◽  
Anna Kashina
Keyword(s):  
Cell Adhesion ◽  
Cell Attachment ◽  
Adhesion Formation ◽  
Cell Matrix ◽  
Intracellular Regulation ◽  
Dependent Cell ◽  
Cell Matrix Adhesion ◽  
Proteolytic Product ◽  
Cell Cell

Talin is a large scaffolding molecule that plays a major role in integrin-dependent cell–matrix adhesion. A role for talin in cell–cell attachment through cadherin has never been demonstrated, however. Here, we identify a novel calpain-dependent proteolytic cleavage of talin that results in the release of a 70-kD C-terminal fragment, which serves as a substrate of posttranslational arginylation. The intracellular levels of this fragment closely correlated with the formation of cell–cell adhesions, and this fragment localized to cadherin-containing cell–cell contacts. Moreover, reintroduction of this fragment rescued the cell–cell adhesion defects in arginyltransferase (Ate1) knockout cells, which normally have a very low level of this fragment. Arginylation of this fragment further enhanced its ability to rescue cell–cell adhesion formation. In addition, arginylation facilitated its turnover, suggesting a dual role of arginylation in its intracellular regulation. Thus, our work identifies a novel proteolytic product of talin that is regulated by arginylation and a new role of talin in cadherin-dependent cell–cell adhesion.

Cdk5 regulates cell-matrix and cell-cell adhesion in lens epithelial cells

2002 ◽  
Vol 115 (10) ◽  
pp. 2109-2117 ◽  
Author(s):  
Sewite Negash ◽  
Hwai-Shi Wang ◽  
Chun Gao ◽  
Dolena Ledee ◽  
Peggy Zelenka
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Cell Attachment ◽  
Dominant Negative ◽  
Lens Epithelial Cells ◽  
Fiber Cells ◽  
Cell Matrix ◽  
Dominant Negative Mutation ◽  
Cell Cell

Cdk5 is a member of the cyclin-dependent kinase family, which is expressed predominantly in terminally differentiated neurons. Lower levels of Cdk5 are also found in a wide variety of cell types, including the lens. Although Cdk5 has been shown to play an important role in neuronal migration and neurite outgrowth, its function in non-neuronal cells is not known. Therefore, this study was undertaken to explore the role of Cdk5 in the lens. Results showed that, within the adult mouse lens, Cdk5 was localized to the cytoplasm,especially along the lateral membranes of differentiating primary fiber cells,which suggests a role in cell-cell adhesion. Staining at the tips of elongating fiber cells was also particularly strong, suggesting a role in cell-matrix adhesion. To examine the possible role of Cdk5 in lens epithelial cell adhesion, we stably transfected N/N1003A rabbit lens epithelial cells with cDNAs for Cdk5 or a dominant-negative mutation, Cdk5-T33. Attachment to a fibronectin matrix, as measured with substrate-coated cell adhesion strips,was increased by Cdk5 overexpression, while an equivalent overexpression of Cdk5-T33 had no effect. Cdk5 also increased the rate of cell attachment and spreading as measured by electric cell-substrate impedance sensing (ECIS). In addition, Cdk5 overexpression decreased cell-cell adhesion as measured by a cell aggregation assay. These findings suggest that Cdk5 plays a role in regulating both cell-matrix and cell-cell interactions in the lens.

Platelet and Shear Rate Promote Tumor Cell Adhesion to Human Endothelial Extracellular Matrix - Absence of a Role for Platelet Cyclooxygenase

1989 ◽  
Vol 61 (03) ◽  
pp. 485-489 ◽  
Author(s):  
Eva Bastida ◽  
Lourdes Almirall ◽  
Antonio Ordinas
Keyword(s):  
Cell Adhesion ◽  
Shear Rate ◽  
Tumor Cell ◽  
Umbilical Vein ◽  
Blood Platelets ◽  
Flow Conditions ◽  
Tumor Cell Adhesion ◽  
Rate Dependent ◽  
Static Conditions

SummaryBlood platelets are thought to be involved in certain aspects of malignant dissemination. To study the role of platelets in tumor cell adherence to vascular endothelium we performed studies under static and flow conditions, measuring tumor cell adhesion in the absence or presence of platelets. We used highly metastatic human adenocarcinoma cells of the lung, cultured human umbilical vein endothelial cells (ECs) and extracellular matrices (ECM) prepared from confluent EC monolayers. Our results indicated that under static conditions platelets do not significantly increase tumor cell adhesion to either intact ECs or to exposed ECM. Conversely, the studies performed under flow conditions using the flat chamber perfusion system indicated that the presence of 2 × 105 pl/μl in the perfusate significantly increased the number of tumor cells adhered to ECM, and that this effect was shear rate dependent. The maximal values of tumor cell adhesion were obtained, in presence of platelets, at a shear rate of 1,300 sec-1. Furthermore, our results with ASA-treated platelets suggest that the role of platelets in enhancing tumor cell adhesion to ECM is independent of the activation of the platelet cyclooxygenase pathway.

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