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Biochemistry (Moscow)

, Volume 80, Issue 3, pp 260–275 | Cite as

Rat liver sinusoidal surface N-linked glycoproteomic analysis by affinity enrichment and mass spectrometric identification

  • Jianglin Li
  • Jun Gao
  • Miao Jiang
  • Jia Chen
  • Zhonghua Liu
  • Ping ChenEmail author
  • Songping LiangEmail author
Review

Abstract

Glycosylation in liver is one of the most biologically important protein modifications. It plays critical roles in many physiological and pathological processes by virtue of its unique location at the blood-tissue interface, including angiogenesis, liver cancer, cirrhosis, and fibrosis. To analyze glycosylation of plasma membrane proteins in liver sinusoidal endothelial cells (LSEC), N-glycopeptides of the LSEC surface were enriched using a filter-assisted sample preparation-based lectin affinity capture method and subsequently identified with mass spectrometry. In total, 225 unique N-glycosylation sites on 152 glycoproteins were identified, of which 119 (53%) sites had not previously been determined experimentally. Among the glycoproteins, 53% were classified as plasma membrane proteins and 47 (31%) as signaling proteins and receptors. Moreover, 23 cluster of differentiation antigens with 49 glycopeptides were detected within the membrane glycoproteins of the liver sinusoidal surface. Furthermore, bioinformatics analysis revealed that the majority of identified glycoproteins have an impact on processes of LSEC. Therefore, N-glycoproteomic analysis of the liver sinusoidal surface may provide useful information on liver regeneration and facilitate liver disease diagnosis.

Key words

liver sinusoidal endothelial surface N-glycoproteomic N-glyco-FASP mass spectrometry 

Abbreviations

CAM

cell adhesion molecule

CD

cluster of differentiation

ECM

extracellular matrix

EGFR

epidermal growth factor receptor

ER

endoplasmic reticulum

FASP

filter-aided sample preparation-based method

GO

gene ontology annotation

GRAVY

grand average hydropathy

KEGG

Kyoto Encyclopedia of Genes and Genomes

LC-MS/MS

liquid chromatography-tandem mass spectrometry

LSEC

liver sinusoidal endothelial cells

MS

mass spectrometry

NPM

plasma membrane pellet from the Nycodenz density centrifugation

PM

plasma membrane

SPM

LSEC PM fraction after sucrose density centrifugation

TMD

transmembrane domain

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Copyright information

© Pleiades Publishing, Ltd. 2015

Authors and Affiliations

  1. 1.Key Laboratory of Protein Chemistry and Developmental Biology of the Ministry of Education, College of Life SciencesHunan Normal UniversityChangshaP. R. China
  2. 2.Qingyuan City People’s Hospital of Jinan UniversityQingyuan, GuangdongP. R. China

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