Antibody recognition of peptide sequences from the cell-cell adhesion proteins: N- and E-cadherins

Intercellular junctions present a formidable challenge for the paracellular delivery of drugs. Cadherins are calcium-dependent cell-cell adhesion molecules, which are responsible for the formation and regulation of these junctions. Anti-E-cadherin monoclonal antibody can bind to E-cadherin (uvomorul...

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Bibliographic Details
Published inPeptide research Vol. 9; no. 5; p. 233
Main Authors Lutz, K L, Szabo, L A, Thompson, D L, Siahaan, T J
Format Journal Article
LanguageEnglish
Published United States 01.09.1996
Subjects
Amino Acid Sequence
Antibodies, Monoclonal
Cadherins - immunology
Cell Adhesion
Cell Polarity
Conserved Sequence
Enzyme-Linked Immunosorbent Assay - methods
Epitope Mapping
Molecular Sequence Data
Peptide Fragments - chemical synthesis
Peptide Fragments - immunology
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Summary:Intercellular junctions present a formidable challenge for the paracellular delivery of drugs. Cadherins are calcium-dependent cell-cell adhesion molecules, which are responsible for the formation and regulation of these junctions. Anti-E-cadherin monoclonal antibody can bind to E-cadherin (uvomorulin) and inhibit cell-cell adhesion through the inhibition of cadherin-cadherin interactions. The objective of this study was to utilize this monoclonal anti-E-cadherin antibody to map the extracellular domains of E- and N-cadherin. This was accomplished by using two different enzyme-linked immunosorbent assays (ELISAs), a regular indirect ELISA and an immobilized-peptide ELISA. Two peptides from each extracellular domain were recognized by this anti-E-cadherin antibody. By mapping the extracellular domains of cadherins, peptides that have discrete roles in cell-cell adhesion can be identified. This will aid in the design of synthetic peptides that can modulate intercellular junctions to improve drug delivery.
ISSN:1040-5704