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    Predominant Expression of Hybrid N-Glycans Has Distinct Cellular Roles Relative to Complex and Oligomannose N-Glycans

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    Author
    Hall, M. Kristen; Weidner, Douglas A.; Zhu, Young; Dayal, Sahil; Whitman, Austin A.; Schwalbe, Ruth
    Abstract
    Glycosylation modulates growth, maintenance, and stress signaling processes. Consequently, altered N-glycosylation is associated with reduced fitness and disease. Therefore, expanding our understanding of N-glycans in altering biological processes is of utmost interest. Herein, clustered regularly interspaced short palindromic repeats/caspase9 (CRISPR/Cas9) technology was employed to engineer a glycosylation mutant Chinese Hamster Ovary (CHO) cell line, K16, which expresses predominantly hybrid type N-glycans. This newly engineered cell line enabled us to compare N-glycan effects on cellular properties of hybrid type N-glycans, to the well-established Pro´5 and Lec1 cell lines, which express complex and oligomannose types of N-glycans, respectively. Lectin binding studies revealed the predominant N-glycan expressed in K16 is hybrid type. Cell dissociation and migration assays demonstrated the greatest strength of cell–cell adhesion and fastest migratory rates for oligomannose N-glycans, and these properties decreased as oligomannose type were converted to hybrid type, and further decreased upon conversion to complex type. Next, we examined the roles of three general types of N-glycans on ectopic expression of E-cadherin, a cell–cell adhesion protein. Microscopy revealed more functional E-cadherin at the cell–cell border when N-glycans were oligomannose and these levels decreased as the oligomannose N-glycans were processed to hybrid and then to complex. Thus, we provide evidence that all three general types of N-glycans impact plasma membrane architecture and cellular propertie
    URI
    http://hdl.handle.net/10342/7972
    Subject
    glycobiology; N-glycan; transmembrane glycoprotein; cell surface glycan; cell–cell adhesion; cell motility; lateral heterogeneity of proteins in membranes; cadherin
    Date
    2016-06
    Citation:
    APA:
    Hall, M. Kristen, & Weidner, Douglas A., & Zhu, Young, & Dayal, Sahil, & Whitman, Austin A., & Schwalbe, Ruth. (June 2016). Predominant Expression of Hybrid N-Glycans Has Distinct Cellular Roles Relative to Complex and Oligomannose N-Glycans. , (), - . Retrieved from http://hdl.handle.net/10342/7972

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    MLA:
    Hall, M. Kristen, and Weidner, Douglas A., and Zhu, Young, and Dayal, Sahil, and Whitman, Austin A., and Schwalbe, Ruth. "Predominant Expression of Hybrid N-Glycans Has Distinct Cellular Roles Relative to Complex and Oligomannose N-Glycans". . . (), June 2016. November 29, 2023. http://hdl.handle.net/10342/7972.
    Chicago:
    Hall, M. Kristen and Weidner, Douglas A. and Zhu, Young and Dayal, Sahil and Whitman, Austin A. and Schwalbe, Ruth, "Predominant Expression of Hybrid N-Glycans Has Distinct Cellular Roles Relative to Complex and Oligomannose N-Glycans," , no. (June 2016), http://hdl.handle.net/10342/7972 (accessed November 29, 2023).
    AMA:
    Hall, M. Kristen, Weidner, Douglas A., Zhu, Young, Dayal, Sahil, Whitman, Austin A., Schwalbe, Ruth. Predominant Expression of Hybrid N-Glycans Has Distinct Cellular Roles Relative to Complex and Oligomannose N-Glycans. . June 2016; (): . http://hdl.handle.net/10342/7972. Accessed November 29, 2023.
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