Basigin, the mouse form of the human protein EMMPRIN, is commonly found as a transmembrane homodimer with carboxy termini in the cytosol and extracellular amino-termini. Because of its important role as a cell-to-cell junction molecule, and possible implications for cancer research, a Basigin null mouse was developed in 1996 by Igakura et al., to aid in the study of this protein. Their early research demonstrated that Basigin plays a large role in embryonic development. Mice lacking the Basigin gene are blind from the time of eye opening, and have demonstrated a lack of aversion to offensive odors such as acetic acid and isogine, as well as increased sensitivity to electric foot shock (Naruhashi et al., 1997). Further research demonstrated that Basigin is associated with cell-to-cell communication within the retina of the eye (Ochrietor et al., 2002), and in the olfactory system (Igakura et al., 1996). It is thought that Basigin acts as a chaperone for several Monocarboxylate Transporters (MCTs), accompanying them for proper placement in the cell membrane. The focus of this current study is to explore the role and function of Basigin in the olfactory bulb of the mouse. Data from biochemical analysis of tissue samples show that MCTs in the olfactory bulb are unaffected by absence of Basigin. Further study involving immunohistochemistry reveals that MCT2 is the most abundant transporter present in normal olfactory bulbs, and that a metabolic defect does not likely underlie the anosmia exhibited by Basigin null mice.
| Identifer | oai:union.ndltd.org:unf.edu/oai:digitalcommons.unf.edu:etd-1128 |
| Date | 01 January 2011 |
| Creators | Gambon, Paul L |
| Publisher | UNF Digital Commons |
| Source Sets | University of North Florida |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | UNF Theses and Dissertations |
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