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Protein glycosylation studies in mammalian cells and yeast

Huang, Kristen Marie
http://rave.ohiolink.edu/etdc/view?acc_num=case1057779808

Abstract Details

1994, Doctor of Philosophy, Case Western Reserve University, Biochemistry.
Protein glycosylation occurs within the endoplasmic reticulum and the Golgi complex. In mammalian cells, cell surface membrane glycoproteins become glycosylated as they move through the rough endoplasmic reticulum. The oligosaccharide chains are processed as the glycoprotein moves through the Golgi with the terminal sugar residues, galactose and sialic acid added in the trans-Golgi cisternae and trans Golgi network respectively. Following glycosylation membrane glycoproteins are transported to the cell surface. We have investigated the return of membrane glycoproteins to the Golgi complex after their appearance on the cell surface. We have found that, in a Chinese hamster ovary cell line, the mannose 6-phosphate receptor returns to the galactosyltransferase compartment of the Golgi complex. In addition, at least ten other cell surface glycoproteins follow this recycling pathway with similar kinetics. By analyzing a subset of membrane glycoproteins, we have determined that a significant fraction of the glycoprotein flux through the Golgi is attributable to recycling cell surface glycoproteins. Many of the steps in glycoprotein synthesis are conserved between mammalian cells and yeast cells. To better understand the process of glycosylation, we have isolated mutants in the yeast Schizosa ccharomyces pombe that are defective in protein glycosylation. These mutants synthesize and secrete glycoproteins that have smaller molecular weights than wild type strains. An analysis of the glycoprotein oligosaccharide chains revealed two of the mutants are defective in core oligosaccharide modification. One of these mutants is defective in UDP glucose 4-epimerase activity which results in decreased levels of UDP galactose and undergalacosylation of cellular glycoproteins. The other mutant is more likely defective in a glycosyltransferase. The isolation of such mutants will aid in cloning Schizosaccharomyces pombe genes involved in protein glycosylation.
Martin Snider (Advisor)
202 p.
Protein glycosylation studies mammalian cell yeast

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Citations

  • Huang, K. M. (1994). Protein glycosylation studies in mammalian cells and yeast [Doctoral dissertation, Case Western Reserve University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=case1057779808

    APA Style (7th edition)

  • Huang, Kristen. Protein glycosylation studies in mammalian cells and yeast. 1994. Case Western Reserve University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=case1057779808.

    MLA Style (8th edition)

  • Huang, Kristen. "Protein glycosylation studies in mammalian cells and yeast." Doctoral dissertation, Case Western Reserve University, 1994. http://rave.ohiolink.edu/etdc/view?acc_num=case1057779808

    Chicago Manual of Style (17th edition)

case1057779808
882
© 1994, all rights reserved.
This open access ETD is published by Case Western Reserve University School of Graduate Studies and OhioLINK.