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003 OCoLC;

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035 a| (Sirsi) o56722795;

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049 a| EREE;

050 4 a| QL638.I3b| F85 2003;

100 1 a| Fuller, James R.,e| author.?| UNAUTHORIZED;

245 10 a| Calnexin association with major histocompatibility class II molecules in Ictalurus punctatus /c| by James R. Fuller.;

264 0 c| 2003.;

300 a| vi, 61 leaves :b| illustrations (some color) ;c| 28 cm;

336 a| textb| txt2| rdacontent;

337 a| unmediatedb| n2| rdamedia;

338 a| volumeb| nc2| rdacarrier;

502 b| M.S.c| East Carolina Universityd| 2003;

500 a| Presented to the faculty of the Department of Biology.;

500 a| Advisor: Thomas J. McConnell;

520 3 a| Calnexin is a chaperone that associates with [nu]-Iinked glycoproteins. In mouse and human cell lines, calnexin has been shown to associate with [alpha] chain, [beta] chain, and invariant chain (Ii) of the Major histocompatibility complex (MHC) class II nonameric, ([alpha][beta])₃Ii₃ assembly. We propose that calnexin assumes the same role with the glycosylated molecules of MHC class II in the Channel catfish, Ictalurus punctatus, as it does in murine and human systems, and have analyzed the [nu]-glycosylation of catfish MHC class II molecules. In all mammals, [alpha] chain, [beta] chain, and li all bear A-linked oligosaccharide binding sites. In I. punctatus, the [alpha] chain lacks the glycosylation consensus sequence, and gel shift assays have confirmed the lack of glycosylation. We also have shown by coprecipitation and Western blot that MHC class II associates with calnexin in the 28S T lymphocyte cell line derived from I. punctatus. This is novel because of the finding that a chain and li of I. punctatus do not bear any [nu]-linked oligosaccharide binding sites; however, calnexin could be binding to [beta] chain of the nonameric complex. This is the first demonstration of calnexin association with nonmammalian vertebrate MHC class II.;

504 a| Includes bibliographical references (leaves 54-61).;

650 0 a| Channel catfish.=| ^A112918;

650 0 a| Fishesx| Cytology.=| ^A190211;

650 0 a| Major histocompatibility complex.=| ^A13757;

650 7 a| Channel catfish.2| fast0| (OCoLC)fst00852101;

650 7 a| Fishesx| Cytology.2| fast0| (OCoLC)fst00926401;

650 7 a| Major histocompatibility complex.2| fast0| (OCoLC)fst01006236;

655 7 a| dissertations.2| aat0| (CStmoGRI)aatgf300028029;

655 7 a| Academic theses.2| fast0| (OCoLC)fst01726453;

655 7 a| Academic theses.2| lcgft;

655 7 a| Thèses et écrits académiques.2| rvmgf0| (CaQQLa)RVMGF-000001173;

700 1 a| McConnell, Thomas J.,e| degree supervisor.?| UNAUTHORIZED;

710 2 a| East Carolina University.b| Department of Biology.=| ^A637467;

856 41 z| Access via ScholarShipu| http://hdl.handle.net/10342/11993;

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Calnexin association with major histocompatibility class II molecules in Ictalurus punctatus / by James R. Fuller.

Author/creator	Fuller, James R. author.
Other author	McConnell, Thomas J., degree supervisor.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Production	2003.
Description	vi, 61 leaves : illustrations (some color) ; 28 cm
Supplemental Content	Access via ScholarShip
Subjects	Channel catfish. Fishes--Cytology. Major histocompatibility complex.

Summary	Calnexin is a chaperone that associates with [nu]-Iinked glycoproteins. In mouse and human cell lines, calnexin has been shown to associate with [alpha] chain, [beta] chain, and invariant chain (Ii) of the Major histocompatibility complex (MHC) class II nonameric, ([alpha][beta])₃Ii₃ assembly. We propose that calnexin assumes the same role with the glycosylated molecules of MHC class II in the Channel catfish, Ictalurus punctatus, as it does in murine and human systems, and have analyzed the [nu]-glycosylation of catfish MHC class II molecules. In all mammals, [alpha] chain, [beta] chain, and li all bear A-linked oligosaccharide binding sites. In I. punctatus, the [alpha] chain lacks the glycosylation consensus sequence, and gel shift assays have confirmed the lack of glycosylation. We also have shown by coprecipitation and Western blot that MHC class II associates with calnexin in the 28S T lymphocyte cell line derived from I. punctatus. This is novel because of the finding that a chain and li of I. punctatus do not bear any [nu]-linked oligosaccharide binding sites; however, calnexin could be binding to [beta] chain of the nonameric complex. This is the first demonstration of calnexin association with nonmammalian vertebrate MHC class II.
General note	Presented to the faculty of the Department of Biology.
General note	Advisor: Thomas J. McConnell
Dissertation note	M.S. East Carolina University 2003
Bibliography note	Includes bibliographical references (leaves 54-61).
Genre/form	dissertations.
Genre/form	Academic theses.
Genre/form	Academic theses.
Genre/form	Thèses et écrits académiques.

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Calnexin association with major histocompatibility class II molecules in Ictalurus punctatus / by James R. Fuller.

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