Glycophosphatidyl-inositol (GPI)-linked carcinoembryonic antigen (CEA) family members, including CEA itself, are absent in rodents and seem to have evolved recently. We have shown previously that CEA-CEA binding required for intercellular adhesion involves a double reciprocal interaction between the N-terminal (N domain) and internal A3B3 domains of anti-parallel molecules on apposed cell surfaces. To answer the question of whether this binding mechanism also evolved with CEA, the adhesive binding mechanism for transmembrane biliary glycoprotein (BGP), presumably more primordial, was investigated. Since CEA and BGP can be expressed on the same cells, and can have opposite effects on the cell phenotype, heterotypic interactions between them were also of interest. A construct with a deletion (17 amino acids) in the N domain of BGP was created which is unable to mediate intercellular adhesion. This $ Delta$NBGP construct, along with BGP splice variant containing only the N domain and various chimeric CEA/NCAM (neural cell adhesion molecule) constructs, was used to establish the fact that both BGP-BGP and BGP-CEA binding are obligate N-N domain. Thus fundamentally different molecular adhesion mechanisms exist in the CEA family.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.23900 |
| Date | January 1996 |
| Creators | Keyston, Rebecca |
| Contributors | Stanners, C. P. (advisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Biochemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001494913, proquestno: MM12211, Theses scanned by UMI/ProQuest. |
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