alexa Structural Analysis of N-glycans attached to Pig Kidney Na+/K+-ATPase | OMICS International | Abstract
ISSN: 2153-0637

Journal of Glycomics & Lipidomics
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Research Article

Structural Analysis of N-glycans attached to Pig Kidney Na+/K+-ATPase

Mayumi Kanagawa1, Kana Matsumoto1, Noriyuki Iwasaki2, Yutaro Hayashi1,3 and Yoshiki Yamaguchi1*
1Structural Glycobiology Team, Systems Glycobiology Research Group, Chemical Biology Department, RIKEN, Advanced Science Institute, 2-1 Hirosawa Wako, Saitama 351-0198, Japan
2Bruker Daltonics K.K., 3-9 Moriya, Kanagawa, Yokohama, Kanagawa 221-0022, Japan
3Deptartment of Biochemistry, Kyorin University School of Medicine, 6-20-2 Shinkawa, Mitaka, Tokyo 181-8611, Japan
Corresponding Author : Yoshiki Yamaguchi
Structural Glycobiology Team
Systems Glycobiology Research Group
Chemical Biology Department
RIKEN ASI, 2-1 Hirosawa Wako
Saitama 351-0198, Japan
Tel: +81-48-467-9619
Fax: +81-48-467-9620
E-mail: [email protected]
Received February 04, 2013; Accepted February 11, 2013; Published February 14, 2013
Citation: Kanagawa M, Matsumoto K, Iwasaki N, Hayashi Y, Yamaguchi Y (2013) Structural Analysis of N-glycans attached to Pig Kidney Na+/K+-ATPase. J Glycomics Lipidomics S5:005. doi:10.4172/2153-0637.S5-005
Copyright: © 2013 Kanagawa M, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Na+/K+-ATPase is a membrane glycoprotein composed of α, β, and γ subunits, generating ion gradients across plasma membranes. Ion pumping is mainly accomplished by the α subunit, while the glycosylated β subunit binds tightly to the α subunit to assemble the pump and plays an essential role in the stabilization and maturation of Na+/K+-ATPase. Accumulating evidence suggests that the N-glycans of the β subunit contribute to cell-cell interaction and the tightness of cell contacts is modulated by N-glycan branching. However, N-glycan function is not fully understood due to a lack of detailed information on the oligosaccharide structure. We, here, perform glycosylation profi ling of the N-glycans attached to pig kidney Na+/K+-ATPase in order to better understand the mechanism of Na+/K+-ATPase-mediated cell adhesion.                  We purifi ed Na+/K+-ATPase from pig kidney outer medulla to homogeneity and solubilized it with the detergent C12E8. The enzyme thus obtained was identifi ed as α1β1 subtype by LC-MS/MS analysis of tryptic digests. During the course of MS analysis, we found that Lys456 of the α subunit was partially modifi ed with 4-hydroxynonenal, an aldehydric lipid peroxidation product. Three N-glycosylation sites on the β1 subunit were confi rmed to be fully occupied by time course analysis of enzymatic deglycosylation monitored by SDS-PAGE. HPLC profi ling of pyridylaminated oligosaccharides derived from Na+/K+-ATPase showed that high-mannose type oligosaccharides predominate while most of the less abundant complex-type oligosaccharides are capped with galactose residues. No glycans could be detected on the four consensus N-glycosylation sites on the α1 subunit. We briefl y discuss the possibility that oligomerization of Na+/K+- ATPase via β-β interactions assembles the N-glycans and promotes cell-cell adhesion.

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