scholarly journals Physiologically relevant binding affinity quantification of monoclonal antibody PF-00547659 to mucosal addressin cell adhesion molecule forin vitro in vivocorrelation

2016 ◽  
Vol 174 (1) ◽  
pp. 70-81 ◽  
Author(s):  
Mengmeng Wang ◽  
Amanda K Kussrow ◽  
Mireia Fernandez Ocana ◽  
Jeffrey R Chabot ◽  
Christopher S Lepsy ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Adhesion ◽  
Binding Affinity ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Affinity Quantification

scholarly journals Mapping of three carbohydrate attachment sites in embryonic and adult forms of the neural cell adhesion molecule.

1984 ◽  
Vol 99 (5) ◽  
pp. 1848-1855 ◽  
Author(s):  
K L Crossin ◽  
G M Edelman ◽  
B A Cunningham
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Sialic Acid ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Attachment Sites ◽  
Neural Cell Adhesion

The sialic-rich carbohydrate moiety of the neural cell adhesion molecule (N-CAM) undergoes major structural changes during development and plays a significant role in altering the homophilic binding of the molecule. In order to understand the mechanism of these changes, a cyanogen bromide (CNBr) fragment that contained 90% of the sialic acid of N-CAM was isolated and characterized according to the number of carbohydrate attachment sites and reactivity with specific monoclonal antibodies. The CNBr sialopeptide migrated on SDS PAGE as a broad zone of Mr 42,000-60,000. Upon treatment with neuraminidase, it was converted to a single component of Mr 42,000, and subsequent, limited treatment with endoglycosidase F gave four evenly spaced components of Mr 35,000-42,000, suggesting that it contained three attachment sites for N-linked oligosaccharides. The fragment reacted with monoclonal antibody 15G8, which detects the sialic acid in embryonic N-CAM, and with a monoclonal antibody, anti-(N-CAM) No. 2. Treatment with neuraminidase or with endoglycosidase F destroyed reactivity with 15G8 but not with anti-(N-CAM) No. 2. A similar CNBr sialopeptide was obtained from adult N-CAM; it contained sialic acid, had three N-linked oligosaccharides and reacted with anti-(N-CAM) No. 2 but not with 15G8 monoclonal antibodies. A peptide fragment, Fr2, comprising the NH2 terminal and middle regions of the molecule yielded a CNBr fragment closely similar to the fragment obtained from the whole molecule. The CNBr fragment from Fr2 reacted with monoclonal antibody anti-(N-CAM) No. 2. Fr1, comprising the NH2 terminal region alone, failed to react. These data confirm that the majority of the sialic acid is localized in the middle region of the N-CAM molecule and support the hypothesis that embryonic to adult conversion of N-CAM is the result of differences in sialidase or sialytransferase activity.

The 80L5C4 epitope overlaps with the homophilic binding site of the cell adhesion molecule gp80 of Dictyostelium

1992 ◽  
Vol 70 (3-4) ◽  
pp. 246-249 ◽  
Author(s):  
Xiang-Fu Wu ◽  
Rajender K. Kamboj ◽  
Jean Gariepy ◽  
Chi-Hung Siu
Keyword(s):  
Monoclonal Antibody ◽  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Epitope Mapping ◽  
Potent Inhibitor ◽  
Enzyme Linked Immunosorbent Assay ◽  
Amino Acid Residues ◽  
Homophilic Binding ◽  
Hydrophobic Residues

The monoclonal antibody (mAb) 80L5C4 is a potent inhibitor of the cell adhesion molecule gp80 of Dictyostelium discoideum. To map the exact location of the epitope recognized by mAb 80L5C4, overlapping hexapeptides were synthesized on plastic pins and the binding of mAb 80L5C4 to these peptides was monitored by enzyme-linked immunosorbent assay. The 80L5C4 epitope is mapped to a single hexapeptide sequence GYKLNV, which shares five amino acid residues with the octapeptide sequence YKLNVNDS involved in gp80 homophilic binding. Analogue studies indicate that the hydrophobic residues within this sequence are crucial for antigen recognition.Key words: monoclonal antibody, epitope mapping, cell adhesion molecule, Dictyostelium.

scholarly journals L1 Cell Adhesion Molecule as a Potential Therapeutic Target in Murine Models of Endometriosis Using a Monoclonal Antibody Approach

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e82512 ◽  
Author(s):  
Cássia G. T. Silveira ◽  
Dominique Finas ◽  
Peter Hunold ◽  
Frank Köster ◽  
Katharina Stroschein ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Therapeutic Target ◽  
Cell Adhesion Molecule ◽  
Murine Models ◽  
Potential Therapeutic Target ◽  
L1 Cell Adhesion Molecule
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