Molecular chaperones calnexin and calretculin in the channel catfish, Ictalurus punctatus / by Joshua E. Pitzer.
| Author/creator | Pitzer, Joshua E. author. |
| Other author | McConnell, Thomas J., degree supervisor. |
| Other author | East Carolina University. Department of Biology. |
| Format | Theses and dissertations |
| Production | 2001. |
| Description | 117 leaves : illustrations ; 28 cm |
| Supplemental Content | Access via ScholarShip |
| Subjects |
| Subject | Major Histocompatibility Complex (MHC) class II molecules present peptides to CD4 T cells in the course of activating a specific immune response. For normal antigen presentation the MHC class II molecules must be properly folded and assembled in the endoplasmic reticulum. MHC folding in mammals involves the endoplasmic reticulum resident proteins calnexin and calreticuhn that function as molecular chaperones. While chaperone function has been extensively examined in mammals, little is known of chaperone function in lower vertebrates. Characterizing these molecular chaperones in animals other than mammals provides evidence of the conservation of protein structure and function through evolution. Complete cDNA sequences of calnexin and calreticuhn have been generated in the vertebrates human, mouse, rat, dog, and frog species. Herein is described the isolation and characterization of calnexin and calreticuhn within the channel catfish, Ictalurus punctatus. Using RACE techniques, the complete cDNA sequences of the two molecular chaperones were generated. Isolation of the molecular chaperone genes has allowed comparison of the calnexin and calreticuhn genes from catfish to the other species. The deduced amino acid sequence of catfish calnexin has 72% identity to human calnexin, while catfish calreticuhn has 80% identity to human calreticuhn. Both calnexin and calreticuhn have the calreticuhn family signature domains and various calreticulin-like repeats that define these proteins. In order to understand the functional interactions of calnexin, polyclonal and monoclonal antibodies were generated against calnexin. These antibodies were used in conjunction with MHC class II [3 antibodies in protein association experiments. Calnexin and MHC class II P chains were found to be associated. Therefore, calnexin and calreticuhn are present in the channel catfish and show a high degree of similarity to their mammalian counterparts. These results suggest calnexin may be functioning as a molecular chaperone in MHC class II folding. |
| General note | Presented to the faculty of the Department of Biology. |
| General note | Advisor: Thomas J. McConnell |
| Dissertation note | M.S. East Carolina University 2001 |
| Bibliography note | Includes bibliographical references (leaves 109-117). |
| Genre/form | Academic theses. |
| Genre/form | Academic theses. |
| Genre/form | Thèses et écrits académiques. |