Modulation of the Cellular Junction Protein E-Cadherin in Bovine Brain Microvessel Endothelial Cells by Cadherin Peptides

Lutz, Karen L.; Siahaan, Teruna J.

doi:10.3109/10717549709051891

Cited by 22 publications

(23 citation statements)

References 17 publications

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“…7). As in our BBMEC aggregation assay (Lutz and Siahaan, 1997), HAV24 peptide was more potent than HAV10 peptide in the present assay. This may be due to the propensity to preserve the conformation of the HAV motif in longer peptides (HAV24) than in smaller peptides (HAV10).…”

Section: Discussionmentioning

confidence: 52%

“…HAV peptides were derived from the conserved HAV motif at the EC1 domain of E-cadherin. Previously, we have shown that these peptides block E-cadherin-mediated cell-cell adhesion of BBMEC and MDCK cells (Lutz and Siahaan, 1997;Pal et al, 1997;Makagiansar et al, 2001;Sinaga et al, 2002). The long HAV24 and HAV10 peptides showed significant and dose-dependent inhibitory activities to almost the same extent as DECMA-1 mAb (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…HAV peptides had been shown to inhibit E-cadherin-mediated aggregation of BBMEC (Lutz and Siahaan, 1997;Pal et al, 1997) and to increase paracellular porosity of MDCK cell monolayers (Makagiansar et al, 2001;Sinaga et al, 2002). We also have discovered ADT peptides from another region of EC1 domain, called a bulge region, that can modulate E-cadherin-mediated cell-cell adhesion in MDCK cell layers (Sinaga et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Synthetic peptides containing an HAV sequence can interfere with cadherin-mediated cell-cell adhesion (Blaschuk et al, 1990a,b;Noe et al, 1999;Williams et al, 2000). We have shown that HAV peptides from EC1 of E-cadherin can effectively inhibit E-cadherin-mediated aggregation of bovine brain microvessel endothelial cells (BBMECs) (Lutz and Siahaan, 1997;Pal et al, 1997) and increase the paracellular porosity of Madin-Darby canine kidney (MDCK) cell monolayers (Makagiansar et al, 2001;Sinaga et al, 2002). Recent studies indicate that the trans-interactions between cadherins of opposing cells involve not only EC1-to-EC1 interaction but also interactions of multiple domains (Leckband and Sivasankar, 2000;ChappuisFlament et al, 2001;Perret et al, 2004).…”

mentioning

confidence: 99%

“…Thus, larger cadherin peptides (i.e., 10 -24 amino acids) have difficulty in penetrating the tight junctions to reach the adherens junctions. Another method is the cell aggregation assay in which the extent of aggregation of single cells is evaluated as a function of inhibitor concentrations (Lutz and Siahaan, 1997;Pal et al, 1997;Noe et al, 1999;Renaud-Young and Gallin, 2002;Shan et al, 2004). Unfortunately, it is difficult to quantitate the effect of the peptides in inhibiting the E-cadherin-mediated cell adhesion in this assay.…”

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confidence: 99%

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Inhibition of E-Cadherin-Mediated Homotypic Adhesion of Caco-2 Cells: A Novel Evaluation Assay for Peptide Activities in Modulating Cell-Cell Adhesion

Kobayashi

Ikesue²,

Majumdar³

et al. 2006

The Journal of Pharmacology and Experimental Therapeutics

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Transient modulation of E-cadherin-mediated cell-cell adhesion may improve paracellular drug delivery through biological barriers. Therefore, there is a need to develop an efficient method to evaluate cadherin peptides that can modulate the intercellular junctions. The objective of this study was to establish a novel assay to evaluate peptide activity in modulating E-cadherin-mediated homophilic interactions, based on the homotypic adhesion of Caco-2 cells. Fluorescence-labeled Caco-2 single cells were incubated with Caco-2 monolayers that were treated beforehand with Ca 2ϩ -free medium. The homotypic adhesion in the presence or absence of peptide and antibody was determined fluorometrically. The Ca 2ϩ -deficient pretreatment dramatically increased the number of single cells bound to the monolayers. Immunofluorescence staining showed that some of E-cadherins became accessible without surfactant-induced permeabilization of Caco-2 cell monolayers after the Ca 2ϩ -deficient pretreatment. The homotypic adhesion was largely dependent on extracellular Ca 2ϩ concentrations and significantly inhibited by the presence of anti-E-cadherin monoclonal antibody DECMA-1. In contrast, DECMA-1 did not inhibit E-cadherin-independent adhesion, such as the homotypic adhesion of Caco-2 cells in the absence of Ca 2ϩ or the heterotypic adhesion of Molt-3 T cells to Caco-2 monolayers. These results indicate the predominant involvement of E-cadherin-mediated cell-cell adhesion in this assay. E-cadherinderived peptides, which had been shown in our previous studies to inhibit E-cadherin-mediated cell-cell adhesion, significantly inhibited homotypic adhesion in a dose-dependent manner. These results, taken together, suggest that the present assay can be used for evaluation of peptide, protein, or antibody activity in modulating the E-cadherin-mediated homophilic interactions in the context of whole live cells.

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Section: Discussionmentioning

confidence: 52%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Inhibition of E-Cadherin-Mediated Homotypic Adhesion of Caco-2 Cells: A Novel Evaluation Assay for Peptide Activities in Modulating Cell-Cell Adhesion

Kobayashi

Ikesue²,

Majumdar³

et al. 2006

The Journal of Pharmacology and Experimental Therapeutics

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Pathways for Drug Delivery to the Central Nervous System

Yathindranath

Sun

et al. 2016

Drug Delivery

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The Role of Covalent Dimerization on the Physical and Chemical Stability of the EC1 Domain of Human E-Cadherin

Trivedi

Davis

Shabaik

et al. 2009

Journal of Pharmaceutical Sciences

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The objective of this work was to evaluate the solution stability of the EC1 domain of E-cadherin under various conditions. The EC1 domain was incubated at various temperatures (4, 37, and 70 °C) and pH values (3.0, 7.0, and 9.0). At pH 9.0 and 37 or 70 °C, a significant loss of EC1 was observed due to precipitation and a hydrolysis reaction. The degradation was suppressed upon addition of DTT, suggesting that the formation of EC1 dimer facilitated the EC1 degradation. At 4 °C and various pH values, the EC1 secondary and tertiary showed changes upon incubation up to 28 days, and DTT prevented any structural changes upon 28 days of incubation. Molecular dynamics simulations indicated that the dimer of EC1 has higher mobility than does the monomer; this higher mobility of the EC1 dimer may contribute to instability of the EC1 domain.

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Modulation of the Cellular Junction Protein E-Cadherin in Bovine Brain Microvessel Endothelial Cells by Cadherin Peptides

Cited by 22 publications

References 17 publications

Inhibition of E-Cadherin-Mediated Homotypic Adhesion of Caco-2 Cells: A Novel Evaluation Assay for Peptide Activities in Modulating Cell-Cell Adhesion

Inhibition of E-Cadherin-Mediated Homotypic Adhesion of Caco-2 Cells: A Novel Evaluation Assay for Peptide Activities in Modulating Cell-Cell Adhesion

Pathways for Drug Delivery to the Central Nervous System

The Role of Covalent Dimerization on the Physical and Chemical Stability of the EC1 Domain of Human E-Cadherin

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