Expression of the endoplasmic reticulum protein calnexin in the channel catfish, ictalurus punctatus / by Benjamin D. Machon.
| Author/creator | Machon, Benjamin D. author. |
| Other author | McConnell, Thomas J., degree supervisor. |
| Other author | East Carolina University. Department of Biology. |
| Format | Theses and dissertations |
| Production | 2000. |
| Description | 51 leaves : illustrations (some color) ; 28 cm |
| Supplemental Content | Access via ScholarShip |
| Subjects |
| Summary | The molecular chaperone calnexin is a resident endoplasmic reticulum (ER) protein that functions in quality control by preventing immature, unassembled and misfolded glycoproteins from exiting the ER. Calnexin binds newly synthesized glycoproteins in the ER containing monoglucosylated (Glc1Man9GlcNac2) N-linked glycans, generated by the concerted actions of the glucose trimming enzymes, glueosidase I, glucosidase II and and the reglucosylation enzyme UDP-glucose glycoprotein glucosyltransferase. Calnexin has been found to associate with many glycoproteins including class II MHC α and β and invariant chain proteins. However the majority of information about MHC class II maturation has been discovered using mammalian cell types. Here the channel catfish, Ictalurus punctatus, was used as a model system to analyze chaperone function in a teleost. As an important first step towards understanding quality control of MHC class II assembly in teleosts, a series of experiments was performed to determine if calnexin is present and functional in Ictalurus. Immunopřcipitation and Western Blotting experiments have determined the presence of calnexin in an Ictalurus punctatus B cell line. It was also determined that anti-invariant chain antibodies assayed reacted specifically with murine invariant chain molecules, but did not crossreact with a putative catfish invariant chain. Using an anti- catfish MHC class II β antibody it also was ascertained that newly synthesized class II molecules can also be precipitated with this reagent and the association of MHC class II β and calnexin might be weak in the catfish when compared to mammals. |
| General note | Submitted to the faculty of the Department of Biology. |
| General note | Advisor: Thomas J. McConnell |
| Dissertation note | M.S. East Carolina University 2000 |
| Bibliography note | Includes bibliographical references (leaves 46-51). |
| Genre/form | dissertations. |
| Genre/form | Academic theses. |
| Genre/form | Academic theses. |
| Genre/form | Thèses et écrits académiques. |
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|---|---|---|---|---|
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| Electronic Resources | ✔ Available |