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 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.

scholarly journals Protein production, crystallization and preliminary crystallographic analysis of the four N-terminal immunoglobulin domains of Down syndrome cell adhesion molecule 1

2015 ◽  
Vol 71 (6) ◽  
pp. 775-778 ◽  
Author(s):  
Linna Cheng ◽  
Shu-Ang Li ◽  
Yamei Yu ◽  
Qiang Chen
Keyword(s):  
Down Syndrome ◽  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Rna Splicing ◽  
Cell Adhesion Molecule ◽  
Crystallographic Analysis ◽  
Homophilic Binding ◽  
Ig Superfamily ◽  
Cell Adhesion Molecule 1 ◽  
Insight Into

Down syndrome cell adhesion molecule 1 (Dscam1), a member of the immunoglobulin (Ig) superfamily, plays important roles in both the nervous and the immune systems. Via alternative RNA splicing,DrosophilaDscam1 encodes a vast family of Ig-containing proteins that exhibit isoform-specific homophilic binding. Whether different Dscam1 isoforms adopt the same dimerization mode is under debate, and the detailed mechanism of Dscam1 specificity remains unclear. In this study, eight different isforms of Dscam1 Ig1–4 have been cloned, overexpressed, purified to homogeneity and crystallized. X-ray data were collected to 1.9–4.0 Å resolution. These structures will provide the opportunity to perform extensive structural comparisons of different Dscam1 isoforms and provide insight into its specificity.

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

Vascular cell adhesion molecule-1 mediates lymphocyte adherence to cytokine-activated cultured human endothelial cells [published erratum appears in Blood 1990 Dec 1;76(11):2420]

Blood ◽  
1990 ◽  
Vol 76 (5) ◽  
pp. 965-970 ◽  
Author(s):  
TM Carlos ◽  
BR Schwartz ◽  
NL Kovach ◽  
E Yee ◽  
M Rosa ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Peripheral Blood ◽  
Cell Adhesion Molecule ◽  
Dermal Fibroblasts ◽  
Enzyme Linked Immunosorbent Assay ◽  
Vascular Cell Adhesion ◽  
Vascular Cell ◽  
Vascular Cell Adhesion Molecule ◽  
Cell Adhesion Molecule 1

The expression and function of a new cytokine-induced endothelial cell adhesion protein, vascular cell adhesion molecule-1 (VCAM-1), was characterized in vitro by using a monoclonal antibody, MoAb 4B9, which recognizes a functional epitope on this protein. As determined by enzyme-linked immunosorbent assay and radioimmunoprecipitation of metabolically labeled cells, VCAM-1 was minimally expressed on unstimulated human umbilical vein endothelium (HUVE), but was rapidly induced by recombinant human tumor necrosis factor-alpha (rhTNF-alpha), rh interleukin-1, and lipopolysaccharide. In contrast to intercellular adhesion molecule-1, VCAM-1 was not induced on dermal fibroblasts or arterial smooth muscle cells after stimulation with rhTNF, or on keratinocytes after stimulation with rh interferon-gamma. MoAb 4B9 significantly inhibited the adherence of peripheral blood lymphocytes (PBL) and lymphocytic cell lines, but not neutrophils, to rhTNF- activated HUVE. The inhibitory effect of MoAb 4B9 on PBL adherence to HUVE was additive to that produced by the CD18 MoAb 60.3. These results show that VCAM-1 mediates a CD18-independent pathway of peripheral blood lymphocyte adherence to cytokine-stimulated HUVE. We propose that lymphocyte binding to VCAM-1, induced on endothelium by cytokines, may be an important component of lymphocyte emigration at sites of inflammation or immune reaction.

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