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Int. J. Mol. Sci. 2016, 17(6), 925; doi:10.3390/ijms17060925

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

1
Department of Biochemistry and Molecular Biology, Brody School of Medicine, East Carolina University, 600 Moye Boulevard, Greenville, NC 27834, USA
2
Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University, 600 Moye Boulevard, Greenville, NC 27834, USA
3
Department of Biology, East Carolina University, 1000 E. 5th Street, Greenville, NC 27858, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Cheorl-Ho Kim
Received: 14 March 2016 / Revised: 2 May 2016 / Accepted: 3 June 2016 / Published: 13 June 2016
(This article belongs to the Special Issue Glycan–Receptor Interaction)
View Full-Text   |   Download PDF [3254 KB, uploaded 13 June 2016]   |  

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 Pro5 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 properties. View Full-Text
Keywords: glycobiology; N-glycan; transmembrane glycoprotein; cell surface glycan; cell–cell adhesion; cell motility; lateral heterogeneity of proteins in membranes; cadherin glycobiology; N-glycan; transmembrane glycoprotein; cell surface glycan; cell–cell adhesion; cell motility; lateral heterogeneity of proteins in membranes; cadherin
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Hall, M.K.; Weidner, D.A.; Zhu, Y.; Dayal, S.; Whitman, A.A.; Schwalbe, R.A. Predominant Expression of Hybrid N-Glycans Has Distinct Cellular Roles Relative to Complex and Oligomannose N-Glycans. Int. J. Mol. Sci. 2016, 17, 925.

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