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 (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.
Lutz
K L
KL
Department of Pharmaceutical Chemistry, Simons Laboratories, University of Kansas Lawrence 66047, USA. siahaan@smissman.hbc.ukans.edu
Szabo
L A
LA
Thompson
D L
DL
Siahaan
T J
TJ
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D015820:Cadherins / Q000276:immunology*; D002448:Cell Adhesion; D016764:Cell Polarity; D017124:Conserved Sequence; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods*; D018604:Epitope Mapping; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology*
D000911:Antibodies, Monoclonal; D015820:Cadherins; D010446:Peptide Fragments