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001 ocn166236042;

003 OCoLC;

005 20260420152327.0;

008 070821s2004 xx a bm 000 0 eng d;

035 a| (Sirsi) o166236042;

035 a| (OCoLC)166236042;

049 a| EREE;

050 4 a| QL638.I3b| T45 2004;

100 1 a| Thankappan, Anil,e| author.;

245 10 a| Characterization of glycans on major histocompatibility complex class II molecules in channel catfish, Ictalurus punctatus /c| by Anil Thankappan.;

264 0 c| 2004.;

300 a| 57 leaves :b| illustrations ;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| 2004;

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

500 a| Advisor: Thomas J. McConnell;

520 3 a| The glycans associated with mammalian Major Histocompatibility Complex (MHC) class II molecules are fairly well characterized. In the present study using enzymatic methods we characterized the glycans associated with MHC class II in channel catfish to understand glycosylation patterns in a teleost. Extensive assays did not reveal any indications of O-linked glycosylation on class II molecules of catfish. Unlike for the mammalian class II molecules, channel catfish derived 28S T cells were found to express high mannose N-glycans on class II molecules as seen from endo H experiments. Whereas our studies on peripheral blood leukocytes revealed that catfish possess the ability to transform high mannose to complex type sugars, but the majority of the class II cell surface glycoproteins were of the high mannose type, perhaps indication of an alternate trafficking pathway. Glycosylation in the channel catfish, a model system for teleost, may have significant differences from the glycosylation patterns characterized in mammalian systems.;

504 a| Includes bibliographical references (leaves 48-56).;

650 0 a| Channel catfish.;

650 0 a| Major histocompatibility complex.;

650 0 a| Fishesx| Immunology.;

650 0 a| Glycosylation.;

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

650 7 a| Fishesx| Immunology.2| fast0| (OCoLC)fst00926518;

650 7 a| Glycosylation.2| fast0| (OCoLC)fst00943811;

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.;

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

856 41 z| Access via ScholarShipu| http://hdl.handle.net/10342/12798;

949 a| Click on web addressw| asish| joyner101;

949 a| Click on web addressw| asish| hsl111;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 1090732;

999 a| ASK AT SPECIAL COLLECTIONS DESKw| ASISc| 1i| MQ1932611l| JSCJTHDm| JOYNERr| Ys| Yt| JSCJTHDu| 8/21/2007x| ETDz| JSPECCOLLo| .STAFF. 0;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 1090732-3001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 2/10/2026x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 1090732-4001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 2/10/2026x| ETDz| HERESOURCE;

Characterization of glycans on major histocompatibility complex class II molecules in channel catfish, Ictalurus punctatus / by Anil Thankappan.

Author/creator	Thankappan, Anil author.
Other author	McConnell, Thomas J., degree supervisor.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Production	2004.
Description	57 leaves : illustrations ; 28 cm
Supplemental Content	Access via ScholarShip
Subjects	Channel catfish. Major histocompatibility complex. Fishes--Immunology. Glycosylation.

Summary	The glycans associated with mammalian Major Histocompatibility Complex (MHC) class II molecules are fairly well characterized. In the present study using enzymatic methods we characterized the glycans associated with MHC class II in channel catfish to understand glycosylation patterns in a teleost. Extensive assays did not reveal any indications of O-linked glycosylation on class II molecules of catfish. Unlike for the mammalian class II molecules, channel catfish derived 28S T cells were found to express high mannose N-glycans on class II molecules as seen from endo H experiments. Whereas our studies on peripheral blood leukocytes revealed that catfish possess the ability to transform high mannose to complex type sugars, but the majority of the class II cell surface glycoproteins were of the high mannose type, perhaps indication of an alternate trafficking pathway. Glycosylation in the channel catfish, a model system for teleost, may have significant differences from the glycosylation patterns characterized in mammalian systems.
General note	Presented to the faculty of the Department of Biology.
General note	Advisor: Thomas J. McConnell
Dissertation note	M.S. East Carolina University 2004
Bibliography note	Includes bibliographical references (leaves 48-56).
Genre/form	dissertations.
Genre/form	Academic theses.
Genre/form	Academic theses.
Genre/form	Thèses et écrits académiques.

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Characterization of glycans on major histocompatibility complex class II molecules in channel catfish, Ictalurus punctatus / by Anil Thankappan.

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