SYNTHESIS AND OLIGOSACCHARIDE PROCESSING OF NORMAL AND ALTERED IMMUNOGLOBULIN M DURING B-CELL DIFFERENTIATION (GLYCOPROTEIN, GLYCOPEPTIDE, MUTANT, CARBOHYDRATE, ASPARAGINE-LINKED).

Persistent Link:
http://hdl.handle.net/10150/187906
Title:
SYNTHESIS AND OLIGOSACCHARIDE PROCESSING OF NORMAL AND ALTERED IMMUNOGLOBULIN M DURING B-CELL DIFFERENTIATION (GLYCOPROTEIN, GLYCOPEPTIDE, MUTANT, CARBOHYDRATE, ASPARAGINE-LINKED).
Author:
BECKMANN, M. PATRICIA.
Issue Date:
1985
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Glycoproteins play a key role in cellular growth and differentiation. In order to study glycoprotein biosynthesis and processing, we have chosen the murine Immunoglobulin M (IgM) system as a model. Our system utilizes hybridoma, lymphoma and plasmacytoma cell lines which synthesize intracellular, membrane-bound and secreted IgM. Each type of IgM is synthesized during a specific phase of B-cell differentiation. We have examined the kinetics of IgM synthesis and processing in cells at each developmental stage. The rate of synthesis of membrane-bound and soluble IgM are different. Characteristic rates for membrane versus soluble IgM may be dependent on the extent of oligosaccharide processing. The membrane-bound IgM contains more high-mannose oligosaccharide than does the secreted product. In addition, we have begun to determine how protein structural requirements can affect final glycosylation patterns on the glycoprotein. Two cell lines were studied which secreted smaller than normal IgM heavy chains in tissue culture. One cell line studied (208) contains one glycosylation site, while another (562) retains three sites on the molecule synthesized in tissue culture. Studies performed on these cell lines in tissue culture indicate greater processing of the oligosaccharides on these mutant IgM molecules when compared to the parental cell line (PC700). Studies on the 208 IgM molecules synthesized in the mouse and purified from ascites fluid confirm these results. Upon injection into the mouse, the 562 cell line reverts to produce protein and carbohydrate structures characteristic of the parental cell line. Studies on the 562 protein purified from ascites fluid illustrate the need for more precisely defined cell lines and genetic engineering for the study of altered protein structures.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Glycoproteins -- Physiological effect.; Glycoproteins -- Synthesis.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Biochemistry; Graduate College
Degree Grantor:
University of Arizona
Advisor:
Grimse, William J.

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleSYNTHESIS AND OLIGOSACCHARIDE PROCESSING OF NORMAL AND ALTERED IMMUNOGLOBULIN M DURING B-CELL DIFFERENTIATION (GLYCOPROTEIN, GLYCOPEPTIDE, MUTANT, CARBOHYDRATE, ASPARAGINE-LINKED).en_US
dc.creatorBECKMANN, M. PATRICIA.en_US
dc.contributor.authorBECKMANN, M. PATRICIA.en_US
dc.date.issued1985en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractGlycoproteins play a key role in cellular growth and differentiation. In order to study glycoprotein biosynthesis and processing, we have chosen the murine Immunoglobulin M (IgM) system as a model. Our system utilizes hybridoma, lymphoma and plasmacytoma cell lines which synthesize intracellular, membrane-bound and secreted IgM. Each type of IgM is synthesized during a specific phase of B-cell differentiation. We have examined the kinetics of IgM synthesis and processing in cells at each developmental stage. The rate of synthesis of membrane-bound and soluble IgM are different. Characteristic rates for membrane versus soluble IgM may be dependent on the extent of oligosaccharide processing. The membrane-bound IgM contains more high-mannose oligosaccharide than does the secreted product. In addition, we have begun to determine how protein structural requirements can affect final glycosylation patterns on the glycoprotein. Two cell lines were studied which secreted smaller than normal IgM heavy chains in tissue culture. One cell line studied (208) contains one glycosylation site, while another (562) retains three sites on the molecule synthesized in tissue culture. Studies performed on these cell lines in tissue culture indicate greater processing of the oligosaccharides on these mutant IgM molecules when compared to the parental cell line (PC700). Studies on the 208 IgM molecules synthesized in the mouse and purified from ascites fluid confirm these results. Upon injection into the mouse, the 562 cell line reverts to produce protein and carbohydrate structures characteristic of the parental cell line. Studies on the 562 protein purified from ascites fluid illustrate the need for more precisely defined cell lines and genetic engineering for the study of altered protein structures.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectGlycoproteins -- Physiological effect.en_US
dc.subjectGlycoproteins -- Synthesis.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineBiochemistryen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorGrimse, William J.en_US
dc.contributor.committeememberLindell, Thomas J.en_US
dc.contributor.committeememberBrendel, Klausen_US
dc.contributor.committeememberBourque, Don P.en_US
dc.contributor.committeememberLaw, John H.en_US
dc.identifier.proquest8511699en_US
dc.identifier.oclc693602486en_US
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